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Animal glues: a review of their key properties relevant to conservation



Collagen-based animal glues are widely used in the conservation of artefacts, serving as adhesives, binders and consolidants for organic and inorganic materials. With a variety of different animal glues on the market, such as hide and bone glues, fish glues, isinglass and gelatin, their individual properties need to be well understood in order to choose a glue fit for a specific purpose. This paper reviews a wide range of publications on currently available animal glues, with respect to their specific physical, chemical and mechanical properties.
Collagen-based animal glues are widely used in
the conservation of artefacts, serving as adhesives,
binders and consolidants for organic and inorganic
materials. With a variety of different animal glues on
the market, such as hide and bone glues, fish glues,
isinglass and gelatin, their individual properties
need to be well understood in order to choose a
glue fit for a specific purpose. This paper reviews
a wide range of publications on currently available
animal glues, with respect to their specific physical,
chemical and mechanical properties.
Animal glues are natural polymers derived from
mammalian or fish collagen – the major structural
protein constituent of skins, connective tissue, cartilage
and bones. These glues may exhibit varied physical,
chemical and mechanical properties depending on their
origin and method of preparation. In the manufacture of
objects and artefacts, an extensive traditional knowledge
exists on which animal glues are most suitable for
specific purposes. However, conservators sometimes
lack the confidence to make informed choices between
the different collagen-based glues available when
conserving objects.
The selection and preparation of glues are discussed in
patent descriptions, woodworking and artists’ manuals,
as well as conservation literature and product details
from suppliers [1, 2]. There is also a large amount of
technical research on the properties of collagen and
gelatin published in scientific journals on polymer-
and bio-technology, medical science and the food and
brewing industry. However, much of this literature
is not readily accessible to conservators and it can
be ambiguous or contradictory. This paper seeks to
provide a review of the literature and to identify which
properties of glue need to be considered when making
decisions about conservation treatments.
The applications of collagen-based glue in the
conservation field are diverse, ranging from its use as an
adhesive, consolidant or binding medium for pigments
and filler particles [3–8]. Generally, the following key
properties need to be considered:
chemical structure and denaturation of the protein
gelling properties: gelling temperature (Tgel), gel
strength and setting times.
properties of the glue solution: viscosity, surface
tension and pH.
properties of the dried film: cohesion, adhesion
and final bond strength, mechanical behaviour
in changing ambient environment, and ageing
Types of commercially available animal glue
Hide glues are primarily derived from bovine skins
and those of smaller mammals, although connective
tissue may also be used. Bone glues are predominantly
prepared from fresh (‘green’) bones or sometimes
extracted bones (degreased and demineralised, known
as ossein) from cattle and pigs. Hide and bone glues are
produced and sold as coarse powders, pearls, cubes,
and cakes or plates, though the latter two appear to be
increasingly rare [9]. Commercial gelatin, the purified
active ingredient of any collagen-derived glue (pure
denatured collagen), may be obtained from either skin
or bone sources [9, 10] and is supplied in the form of
thin sheets, plates or powder.
As the name suggests, rabbit skin glues should be
produced purely from rabbit skins [10, 11], though
collagenous waste from various small mammals may
also be used [12]. Some suppliers sell rabbit skin glue
that is mixed with bovine hide glue to alter its properties
[13]. The information on the source, pre-treatment,
or additives provided by suppliers may not always
be reliable, as they may not have been given accurate
information by the manufacturers. It is generally
assumed that most animal glues contain preservatives
of some kind (e.g. sulphur dioxide) [9, 14]. Even rabbit
skin compressed into cubes, a by-product from the felt
industry commercially sold as a raw (and thus usually
thought to be a pure) form of rabbit skin glue [10], has
recently been found to contain preservatives [9]. Some
traditional glues, such as the deer glue used in Japan as
a binder for some inks, are now made from bovine or
porcine gelatin manufactured to match the properties of
the traditional genuine material [15].
The skins of non-oily types of fish [16, 17], as well as
their bones [10, 12, 18, 19], are used to manufacture fish
glues which are sold in liquid form. The swim bladders
of various species are the source for isinglass [20–24],
which is available either in the form of complete dried
bladders or membranes, thin plates or fine strips.
In recent years, fish skin and bone gelatin has also
become available in the food industry as a substitute for
mammalian gelatin [25–27].
A number of industrially manufactured cold liquid
animal glues are available that have modified properties
and a long shelf life. These glues usually contain
additives that alter their natural behaviour, extending
the working time at room temperature, or decreasing
the propensity for biodeterioration and reducing the
dried film’s sensitivity to moisture. However, the exact
composition of industrially tailored collagen-derived
glues and their overall performance may be difficult
to judge, as manufacturers tend to keep their recipes
Animal glues: a review of their key properties relevant to conservation
Nanke C. Schellmann
secret. Furthermore, conservation requirements such
as long-term stability and resolubility are unlikely to
be a priority for commercial manufacturers. Given the
range of additives that may be present in industrial glue
formulations, minimally modified glues represent the
safest option for conservation.
Chemical structure and properties
Chemical structure and denaturation
Collagen consists of long protein molecules composed
of naturally occurring amino acids that are linked in a
specific sequence by covalent peptide bonds. Due to
the spatial conformation of some amino acid groups
(notably proline and hydroxyproline) and the many
ionisable and polar functional groups in the protein
chain, the individual chains form triple-stranded helical
coils that are generally believed to be internally stabilised
by hydrogen-bonding [7, 25, 29–33].
Collagen is insoluble in cold water [30, 34] and is
transformed into soluble gelatin by denaturation, a
process of critical importance for the performance
of the resulting glue. This is achieved by hot water
extraction (hydrolytic breakdown) [9, 34–39]. Pre-
treatment (either acidic or basic) is necessary for
most skin and bone collagen, but is not required for
the extraction of isinglass from fish bladders, which
contain less cross-linkage within the collagen. During
extraction, the bonds (predominantly H-bonds) in the
triple-helix structures of the collagen are broken so
that it separates into disordered ‘random’ coils of single
protein chains, thus completing the transition to gelatin
[40]; in perfect conditions gelatin is pure denatured
collagen. The temperature (Td) at which denaturation
occurs is dependent on the chemical structure of the
proteins in the particular collagen source, notably on
the content of the amino acid derivatives proline (Pro)
and hydroxyproline (Hyp). These are supposed to be
largely responsible for the stabilising H-bonded water
bridges in the triple helix [41] and are present more
abundantly in mammalian collagen than in marine
species [42]. Thus, adult mammalian collagen denatures
at 40–41°C [31, 33], while isinglass and other fish
collagens denature at lower temperatures. The Td of
fish collagens ranges from approximately 15°C for deep
cold water fish (such as cod used for fish glue) [10, 43]
up to 29°C for most warm water species [31, 33, 44],
which are the preferred source of isinglass produced for
commercial clarification of alcoholic beverages. There
are also a few tropical fish species that reach Td levels of
up to 36°C [31, 44].
The process of denaturation is necessary for collagen
to convert to gelatin, which can be used as a glue.
Cleavage of the single protein molecule may also occur
during pre-treatment, extraction and dissolution, and
will significantly affect the properties of the gelatinous
glue. The more vigorous the extraction process (i.e.
the more extreme the pH, the longer the treatment
and the higher the temperature during extraction), the
more bonds within the protein molecule are randomly
cleaved, leading to ever decreasing molecular weights
[34, 37, 39, 45]. Mild extraction at moderate pH and
low temperature yields gelatinous matrices containing
protein fractions of long chain length and high
molecular weight (MW) [38, 46]. As a general rule,
gentle processing is appropriate for the hides of young
mammals, as well as all fish skin and swim bladders,
because they are rich in collagen and the collagen is not
so strongly stabilised by the additional chemical bonds
that develop in older mammals. Furthermore, glues that
are derived from fish cleave more easily on extensive
heating than those of mammalian origin owing to their
chemical structure [40, 46]. Conservators should thus
be aware that when preparing a collagen-based solution,
mild procedures should be employed [4, 46]. Preparation
temperatures for collagen-based glues are generally
recommended to be around 55–63°C. However, there is
little loss of gel strength on heating at high temperatures
(e.g. 80–90°C), even in the case of isinglass, but only if
the solution is kept at these temperatures for no more
than a few minutes [46, 47].
Gelation and gelling temperature (Tgel)
Although the process of denaturation, with the loss of
the triple helix arrangement of the protein molecules,
is irreversible, some helical structure can be restored
during gelling and drying. On gelling the single
random protein coils undergo partial rearrangement
(renaturation) back into collagen-like triple helices [7,
26, 46, 48-50]. However, the misalignment of the single
strands means that renaturation causes nodes (‘junction
zones’) involving only part of certain strands. The
remainder of these strands may form further nodes so
that a continuous three-dimensional network structure
emerges. The degree of renaturation is dependent on
the chemical composition (Pro and Hyp content), the
chain length of the molecules (molecular weight, MW),
concentration in solution and temperature [42, 49, 51].
High Pro and Hyp content, high MW, high solution
concentrations and slow drying at a low temperature
promote a high degree of renaturation and the
development of a highly ordered network structure [34,
37, 48, 52]. The number of nodes that are established
by the formation of H-bonds (and probably also by
electrostatic interaction [42]) within and between the
molecules determines gel strength and the rigidity and
elasticity of the glue matrix [7, 46, 51].
The ability to form a rigid gel on cooling, which can be
repeatedly reliquefied by reheating, is one of the unique
properties of collagen-based glues. The temperature at
which gelation of the glue solution occurs (Tgel) depends
mainly on the collagen source, but is also affected by
the degree of protein cleavage. Gelation temperatures
decrease with lower denaturation temperature (Td)
and also with increasing cleavage of the molecules.
Mammalian gelatin gels at around 30–35ºC, and cold
water fish gelatin remains liquid down to around 8ºC
[14, 43, 53]. However, this temperature will be lowered
if the preparation temperature of the glue is significantly
Gel strength
Gel strength is a measure of the gel rigidity of gelatinous
glues, and is strongly influenced by the molecular weight
of the constituent proteins [34, 54]. According to
several authors [35, 39], the average molecular weight
(AMW) of animal glues can range from around 20000 to
250000 g.mol-1. It is thought that permanent gelling
does not take place below an AMW of 20000 g.mol-1
[38, p. 43]. Isinglass from sturgeon, if prepared under
mild conditions, reaches average molecular weight values
of well over 150000 g.mol-1 [4, 33, 46], while liquid fish
glue has AMW values of around 60000 g.mol-1 [10, 14],
placing it at the lower end of the range. For most other
commercial collagen-based adhesives, information on
AMW is not readily available.
Characterisation by AMW is only common for fish
glues, which are liquid at room temperature. Most
other gelatinous glues are usually characterised by their
gel strength, as AMW does not describe the molecular
weight distribution and therefore may not always
correlate reliably with the physical and mechanical
properties of a glue [34, p. 60] (Table 1). However, it
would be expected that high AMW adhesives, such as
skin glues, have higher gel strength and viscosity, gel
more rapidly and produce stronger bonds.
Gel strength is strongly influenced by AMW but also
shows a linear correlation with the degree to which
the protein solution renatures during gelation [55],
i.e. the higher the degree of formation of helical
structures, the higher the gel strength. The presence of
salts also influences gel strength, which decreases with
an increasing concentration of ions in solution [42,
Gel strength, also known as Bloom strength, is measured
in grams (g), or Bloom grams (gB), and equals the force
required to make a specified depression into a gel sample
prepared under standard conditions [25, 35, 37, 39].
Manufacturers commonly distinguish between grades
of glue by their Bloom strength, which usually covers
a wide range, being as low as 30 g for weak bone glues
and rigorously extracted hide glues, and up to around
500 g for very strong hide glue [10, 11, 35, 37, 57].
Gelatins derived from tropical fish have significantly
lower Bloom values than mammalian gelatins [58],
since the degree of stabilisation of the triple helix by
H-bonding is lower. Gelatins extracted from cold water
fish do not have specified gel strengths as they are liquid
at room temperature [42].
As gel strength is dependent on the structural
conformation of the gelatinous matrix, it is useful
for estimating the toughness, strength and resilience
of the resulting bond. Furthermore, Bloom strength
also correlates with the water-sorption capacity of the
glue (in gel and solid state), viscosity (at least to some
degree), and gelling temperature (Tgel), which generally
all increase with rising Bloom value. High Bloom glues
require a lower solid content in solution than glues with
a lower Bloom rating to be effective as an adhesive, as
they offer many sites for intermolecular bonding in a
given volume [35, 56]. Mammalian skin glues are usually
considered to have the highest AMW and produce the
strongest gels and films [10], particularly those extracted
by acid pre-treatment. Generally, acid pre-treated glues
(type A gelatins) contain larger fractions of high MW
than alkaline pre-treated collagen derivatives (type B
gelatins), whose MW distribution is skewed towards
lower MW fractions [9, 34, 46].
Open (gelling) time, tack and drying
The setting time of animal glues depends primarily on
Tgel and gel strength. The lower the Tgel and gel strength,
the longer the open time of the solution (i.e. the longer
it takes for the glue to gel). High Bloom hot hide glues
tend to gel rapidly, as gelation occurs at comparatively
high temperatures [10, 11, 14, 39, 59]. Gelatinous
glues derived from fish, which have low Tgel due to
their chemical structure [42, 43, 58], and cold-set liquid
hide glues are convenient to use when long open times
are required. Commercial fish glues usually contain
preservatives [60] and, sometimes, small amounts of
other additives such as colour brightener, deodorizing
agents or fragrance [10]. Liquid hide glues generally
have further additives to inhibit gelation at room
temperature [17, 28]. These are typically salts (e.g.
urea, thiourea) or phenols that extend the setting time
by inhibiting renaturation of the gelatinous matrix [28,
52]. Some manufacturers claim that their liquid hide
glue does not contain gelling inhibitors [17], in which
case the gelatinous matrix must be considerably affected
by molecular cleavage to achieve the comparatively
low MW that is necessary for the glue to be in a liquid
The ability of collagen-based glue to develop tack upon
gelation is a unique property. In general, glues of higher
Bloom strength develop tack faster than lower Bloom
glues. The tack ‘strength’ of glue can be empirically
tested by conservators between two fingertips. Isinglass
solutions may appear to be less tacky than equivalent
concentrations of mammalian gelatin or hide glue, as
they take longer to set at room temperature, since their
lower gelation temperature delays the development of
Drying time generally depends on the ambient
temperature and relative humidity (RH). After gelation,
the glue matrix dries by evaporation of water and this
process can be accelerated by elevating the temperature.
However, collagen-based adhesives should be allowed to
dry as slowly as possible, as a longer period of molecular
mobility after gelation and during drying encourages the
development of highly ordered network structures [52].
This maximises the elasticity and strength (toughness) of
the resulting glue film. Isinglass naturally develops highly
stable and elastic films if dried at room temperature,
being slightly above its Tgel [9].
Properties of gelatinous glue solutions
The viscosity of the glue solution is primarily dependent
on the molecular weight distribution [51]; the greater
the proportion of molecules of higher MW the higher
the viscosity [2, 35]. For a given MW distribution,
the viscosity increases with increasing solution
concentration and decreasing temperature [39, 51, 61].
The degree to which collagen-like helices [62, p. 128]
Table 1 Comparison of the properties of different glue types. The glues are qualitatively ranked relative to one another for each property, i.e. within each individual column. Numerical data is only
referred to in those cases where information was consistent in the literature
PROPERTY molecular weight (MW) [Ref.] gel / Bloom strength [gB] [Ref.] degree of helicity [Ref.] viscosity [Ref.] pH (approximate values) [Ref.]
decreases with rigorous pretreatment
and with excessive/prolonged heating increases with higher MW and
increasing helicity increases with higher MW,
higher Pro and Hyp content
and increasing solution
increases with increasing Bloom,
dependent on isoelectric point
(pI) and pH
influences the viscosity
bone glue low to medium low to medium (down to
50 gB) [9–11,
14, 35,
37, 57,
low to medium low to medium (min.
viscosity around pH
4.5– 5.5)
[10, 14,
69] 5– 7 [5, 10,
35, 37,
hide glue high [10] high (up to 500 gB, hide
glue pearls produce lower
Bloom values than hide
glue grains)
14, 35,
37, 57,
medium to very
high medium to high (min.
viscosity of alkaline
pretreated glue at
around pH 4.5–5.5,
and of of acid
pretreated glue at pH
7.0– 9.0)
[10, 14,
17, 30,
34, 35,
51, 56,
6.5–7.4 (wider variations
are possible) [9–11,
16, 35,
rabbit skin glue high [10] high (up to 500 gB) [9, 10,
14] high to very high high (min. viscosity at
around pH 7.0– 9.0) [9, 10,
14] 5.0–7.5 (wider variations
are possible) [9–11,
110000–168000 (type A
gelatin achieves higher
values than type B
[9, 26,
34, 45,
46, 54]
medium to high (but can
be produced to achieve
Bloom values as low as
75 gB)
medium to high medium to high
(type B gelatin
comparatively more
viscous than type A
[56, 61] 5.0–6.5 [10, 61]
isinglass (from
fish swim
c.150000 and higher up
to 300000 [4, 33,
46] medium to high medium to high highest [4, 22,
46, 65] 6.0–7.5 [19, 61,
71, 79]
fish gelatin
(from fish
skin, bone and
96000–196000 [26, 45,
54] low to medium [58] medium medium to high (min.
viscosity between pH
[43, 54] 3.5–5.0 [10, 43,
54, 58]
liquid fish glue 60000 [14, 57] low to medium high (4000–
6000 mPa.s at
[10, 14,
53] 4.0–6.0 (higher pH values
may be possible) [10, 14]
cold liquid
hide glue
n.a. medium high (4000 mPa.s
at manufactured
[10] 6.5 [10]
n.a. data not available
Table 1 (contd.)
PROPERTY mechanical strength [Ref.] elasticity [Ref.] stress development
in fluctuating RH
[Ref.] stability in fluctuating
[Ref.] resolubility with age [Ref.]
increases with increasing content of
helical structures increases with increasing molecular
weight, helicity and solution
increases with increasing
helicity increases with increasing helicity decreases with lower original solution
bone glue low to medium more elastic than hide
glue (but more brittle) medium less stable than hide /
rabbit skin glue more resoluble than hide
glue [90]
hide glue high (tensile strength
typically around 39
[76] less elastic (stiffer) than
bone glue and gelatin
from aquatic sources
[26, 58] high [6, 28] more stable than bone
glue, less sensitive
than cold liquid hide
[6, 28] generally thought to be
rabbit skin glue high, but lower than
other hide glue [23, 39,
78] more elastic than hide
glue [23, 84] high [76, 86] less sensitive to
moisture than hide
[5, 39] generally thought to be
high (low Bloom value
gelatin will achieve lower
mechanical strength)
less elastic (stiffer) than
gelatin from aquatic
[26, 58] medium to high less stable than
isinglass generally thought to be
isinglass (from
fish swim
high [4] more elastic than hide
glue very high [4] higher than
mammalian gelatin [79] (contradictory data) [23, 79]
fish gelatin
(from fish
skin, bone and
medium [26, 27,
53] more elastic than
mammalian gelatin (but
more brittle)
medium to high n.a. generally thought to be
liquid fish glue medium [26, 27,
53] more elastic than hide
glue (but more brittle) medium less stable than cold
liquid hide glue [17] resoluble (after 6 months
RH and temperature
cold liquid
hide glue
n.a. n.a. n.a as stable as hide glue
(after 6 months RH
and temperature
[17] resoluble (after 6 months
RH and temperature
n.a. data not available
and intermolecular bonds have developed within the
network (gel/Bloom strength) further contributes to
higher viscosity [63, 64]. Strongly denatured gelatinous
solutions (such as bone glues) or those affected by a
high degree of molecular cleavage will normally have a
comparatively low viscosity. At a given Bloom strength,
alkaline pre-treated (Type B) gelatins are generally more
viscous than acid pre-treated (Type A) gelatins [56]
(Table 1).
Viscosity is an important factor in the choice of adhesive
for bonding or consolidation, as it will affect the degree
of penetration into a substrate. If the viscosity is too
low the glue may penetrate too far into the substrate,
leaving a joint starved of adhesive. For consolidation of
porous materials, high viscosity may prevent adequate
penetration and cause stress to develop at the interface
between consolidated and unconsolidated areas.
Unfortunately, the viscosity values for animal glues given
in the literature and by suppliers vary widely and are
not easily compared. Measurements were often taken
under different experimental conditions and at different
degrees of cleavage in the protein molecules [4, 21, 35,
37, 46].
Isinglass has a much higher viscosity than hide glue at
an equivalent solution concentration and temperature
(above Tgel), which can be explained by its comparatively
high proportion of high molecular weight fractions
(which, in the following paragraphs, will be referred to
as high Molecular Weight Distribution (MWD)) [4, 22,
46, 65]. This is contrary to what is often stated in the
literature and to the traditional beliefs about the handling
properties of isinglass [20, 21, 61]. However, where low
viscosity values have been obtained for isinglass, it is
likely that the particular preparation procedure of the
glue used for the tests resulted in greater cleavage of
the protein molecules [46]. Despite isinglass having a
large fraction of high MW compounds, its low gelling
temperature compensates for this by allowing more
time for the glue to penetrate porous substrates at room
temperature, therefore improving its penetration ability
in comparison to gelatin and rabbit skin glue of similar
high MW fractions, which will gel faster [8, 66].
In order to obtain glue solutions of low viscosity, it is
not always advisable to dilute viscous high Bloom glues
excessively. The use of an over-diluted glue may result
in swelling, leaching or staining of the substrate if it is
water sensitive [67]. In such cases, a glue with a lower
gel strength would be preferable.
Surface tension
Slow gelation and lower viscosity promote uniform film
formation as the glue is able to spread evenly, providing
adequate wetting of the surface. Wetting is improved
with a decrease in the surface tension of the glue solution.
Sauer and Aldinger [68] confirm that a decrease in
surface tension of a gelatinous solution is directly linked
to the presence of fats. Free fatty acids and neutral
fats are regarded as particularly effective in reducing
surface tension even in small concentrations. With the
exception of rabbit skin glue (which has comparatively
high fat levels of around 5% [9, 11]), most animal glues
and gelatins contain less than 1% fat because of modern
manufacturing methods [9, 10, 54, 58, 69] and may
require additives to reduce the surface tension.
Ethanol is commonly added to lower the surface tension
and improve the wetting abilities of collagen-based glues
[21, 70, 71]. In one case beer containing 9% alcohol
was added to fish glue that was used in the conservation
of Boulle-marquetry, and was shown to improve the
wetting properties leading to stronger joints between
the wood and brass components [70]. However, alcohol
may also raise the gelling temperature, speeding up the
gelation and decreasing the time for which the glue
is workable [28, p. 102, 110], and may also promote
swelling of the substrate. Alternatively, surfactants can
be added to lower the surface tension [3, 8, 28, 72,
p. 123].
Animal glues can have an undesirable tendency to foam,
developing small air bubbles in the glue matrix which
can disrupt the uniformity of the dried glue film and
weaken bonds [5, 59]. Natural fats or free fatty acids
present in glues play a vital role in reducing foaming [5,
68, 73], although some authors still express some doubt
that there is a direct correlation between fat content
and tendency to foam [9]. Nevertheless, Skans [73,
p. 66] suggested that a natural fat content of above 5%
would inhibit the development of pinholes in gesso for
gilding. Sauer and Aldinger [68] have demonstrated an
unambiguous dependency of the degree of foaming on
fat content, whereas no direct relationship could be
established with surface tension. They also could not
find any influence of protein degradation products
on foaming, while pH was established to have an
inconsistent effect.
For conservation applications, the choice of adhesive
may be dependent on the pH sensitivity of the substrate
[71]. Collagen-based glues can display varying pH
values that are difficult to predict purely on the basis
of the glue type or treatment during manufacture. The
assumption that glues which undergo alkaline pre-
treatment display a slightly alkaline pH and acid-treated
ones have an acidic pH [39, p. 171] is incorrect. It is
stated in the literature that hide and fish glue solutions
often have a fairly neutral pH in the range of 6.5 to
7.4, although wider variations are possible [9–11, 16,
35, 68]. In general, bone glues tend to be slightly more
acidic [5, 10, 39], with pH levels between 5 and just
below 7 [35, 37]. Pure gelatins from mammals and fish
range between pH 5.0–6.5 and 3.5–5.0 respectively [10,
53, 54, 58, 61]. Isinglass yields solutions with a pH in
the neutral range [19, 61, 71]. Conservators should test
the pH value of the chosen glue before use if sensitivity
of the substrate is of potential concern.
Apart from being a relevant aspect to consider in
conjunction with the sensitivity of the substrate, pH
values also have an influence on the properties of the
glue, as the viscosity increases when the pH of the
solution shifts away from its isoelectric point (pI) [1, 37,
61, 74]. Since proteins and amino acids are amphoteric
in nature (i.e. containing both acidic and basic functional
groups), they have an isoelectric point, which is the
pH at which all positive and negative charges within
the molecule are balanced and the molecule carries no
net electrical charge. If the electrical potential of the
ions is unbalanced, solution viscosity and Tgel increase,
as well as the capacity for water-sorption and swelling
ability, while gel strength decreases [9, 46, 52, 61, 62].
Commercial animal glues extracted by alkaline pre-
treatment (most hide and bone glues, type B gelatins)
usually have a pI of approximately 4.5 to 5.5, whereas
glues derived from acid pre-treated collagen sources
commonly display pI values of between 7.0 to 9.0 [17,
30, 34, 35, 51, 56, 75]. For practical purposes, this
means that glues having a pH near their pI value (such
as bone glues and type B gelatins) will already be at the
lowest possible viscosity, as opposed to those which
have pH values different from their pI, where to achieve
the lowest possible viscosity the pH would have to be
modified to take it closer to the pI (Table 1). The effect
of the pH of a glue solution on its surface tension is
inconsistent [28, p. 75, 68].
Mechanical properties of the dried film
Cohesion, adhesion and bond strength
The cohesive strength of the gelatinous matrix of a glue is
determined by its molecular structure and intermolecular
bonding, as expressed by the Bloom value. To produce an
animal glue film that is as strong as possible in the dried
state, the same rules apply as for obtaining a high gel
strength (i.e. high MW distribution/minimum cleavage
of protein molecules, maximum renaturation/content of
collagen-like triple-helices, high intra-/intermolecular
stabilisation). The cohesion strength of animal glues can
be improved by the addition of a suitable amount of an
alcohol, such as ethanol or glycerine [28, p. 108]. To
achieve strong bonding, chemical adhesion between the
glue and the substrate is as important as high cohesion
within the glue matrix.
Hide glues generally have greater cohesive strength than
the bone glues with highly cleaved molecules, which
display a lower tensile strength and are much more
brittle (Table 1). The tensile strength of hide glues is
typically around 39 megapascals (MPa) (5700 pounds
per square inch, psi) [76]. Mammalian collagen tends
to yield stronger glues than most aquatic sources, owing
to the reduced number of stabilising inter- and intra-
molecular bonds in fish collagen [33, 49]. Cold water
fish gelatins in particular have a lower propensity to
reform helical structures due to their small proportion of
the amino acid derivatives, Hyp and Pro, and therefore
show a comparatively low tensile strength of around 22
MPa (3200 psi) [26, 27, 53]. This value is comparable
to the strength of bovine bone gelatin [54].
A high tensile strength similar to that of hide glue
has been reported for mildly prepared isinglass from
sturgeon [4], making it a useful adhesive for bonding
wooden joints. The literature confirms that isinglass
has often been used for structural woodwork in the Far
East [24, 77]. Although rabbit skin glue has a high gel
strength, it has been stated as having lower cohesion
and bonding strength than other hide glues [23, 39,
78]. This is thought to be due to its high fat content
[9, 23].
Elasticity, resistance to impact (toughness) and creep
As for many of the other physical properties of gelatin-
based glue films, the elasticity and stiffness are greatly
dependent on their MW distribution [63], the degree
to which helical structures reform on gelling and the
intra-/intermolecular bonding [7, 26]. The stiffness of
the glue (elastic modulus, known as Young’s modulus
E, mathematically calculated from the ratio of stress to
strain values) increases with a higher ratio of high MW
fractions, higher solution concentrations and with a
greater renaturation level in the network [26, 45, 55].
Stabilisation of the gel network by increased electrostatic
bonding induced by pH levels above or below the pI
also increases the stiffness [42]. Mammalian gelatin
generally has a higher modulus and therefore greater
stiffness than fish gelatin due to its higher network
stabilisation by intra- and intermolecular bonding [26,
58]. Isinglass is also more elastic than mammalian
gelatin [79].
The moisture content of an animal glue has an important
effect on the mechanical properties. Under normal
ambient conditions (50% RH and room temperature)
gelatin-based glue films contain 12–14% of structural
water bound to the polar groups of the protein
macromolecules [52, p. 654]. This water contributes to
the stabilisation of the helical structures within the glue
and a specific amount of water is needed to maintain
structural stability. Above around 25% moisture content
the glue turns from a glassy to a rubbery state at room
temperature [52]. Excessive dehydration of gelatinous
films below a moisture content of 0.2% leads to the
development of covalent cross-links between the protein
molecules, which ultimately renders the glue insoluble
in water [80, p. 509].
In general, gelatinous glue films with a low moisture
content are very brittle regardless of the collagen
source and molecular structure [34, p. 63, 52]. Even
at a normal (12–14%) water content, gelatinous films
undergo brittle fracture under impact. Randomly coiled
structures exhibit much lower resistance to impact
(greater brittleness) than helical glue matrices in the glassy
state. Glue recipes often contain additives such as sugar
alcohols (e.g. glycerine, sorbitol) and polysaccharides
(e.g. dextrins) to improve elasticity and toughness
[28, 34, 81, 91]. One traditional recommendation for
achieving elastic and resilient glue films is the addition
of honey [4, 18, 21, 22, 61, 82]. Sugars are hygroscopic
and so stabilise the protein molecules by introducing
additional hydrogen bonds involving water [25, 83],
inducing an increase in gel strength and viscosity.
Although these additives do not actually plasticise the
glue matrix, they are often referred to as plasticisers in
the literature. A high proportion of fat also improves
elasticity, although it simultaneously reduces the gel
strength of the glue and final bond strength [23, 84].
A higher water content or an excess of hygroscopic
additives generates a reduction in the glass transition
temperature of the glue [61, 81], which can promote an
unwanted tendency to creep (elongation with time).
Stability in ambient environment and sensitivity to
fluctuating levels of moisture and heat
Drying of collagen-derived glue films leads to the
development of high internal stress and tensile forces
within the glue matrix, while increasing humidity
generally causes progressive loss of tension [4, 85]. This
behaviour is dependent on the physical and chemical
structure of the glue. A high degree of collagen-like
triple-helix arrangement in a gelatin film has been
shown to result in a reduced tendency to swell [34, 55],
but is also responsible for increasing stress values due
to stronger cohesion. Isinglass from sturgeon, which
contains a high proportion of helical structures (due to
its high MWD, despite its lower Hyp and Pro content),
develops particularly high stress levels, which it is
suggested are twice as high as in hide glue [4].
If kept under moderate relative humidity conditions over
a long period of time, initial stresses within gelatinous
films relax owing to the absence of covalent cross-links
[86]. Under fluctuating environmental conditions, the
mechanical properties of collagen-based glues are subject
to continual change [85]. Considerable development of
internal stresses will affect the glue’s elasticity, strength
and physical stability and may lead to significant damage
to the substrates [48, 85–87].
At high RH levels (above 85%) animal glue films undergo
a continuing reformation of helical structures. This
will result in new, higher stresses on subsequent drying
and can lead to severe shrinkage due to contraction of
the glue matrix [48, 85, 86]. Cycling of RH can cause
further strain – for rabbit skin glue, non-permanent total
dimensional changes of up to 6% have been reported
as the result of a single RH cycle [76, 86], which are
only partly recoverable. According to Zumbühl [48],
contraction mechanisms compete with plastic relaxation
processes above 65% RH. However, even at high RH
levels plastic relaxation may not sufficiently compensate
for these stresses and continuous cycling further reduces
the ability for stress relaxation [48]. This will result in
permanent shrinkage of the glue matrix (up to 5% for
rabbit skin glue [76]) and, in this case, loss of tension is
only possible by substrate deformation or mechanical
destruction (embrittlement) of the glue film [48].
At low RH levels, more randomly coiled gelatinous
structures (such as bone glues), which have comparatively
low tensile strength and low resistance to stress, induce
relaxation at an early stage by developing cracks in the
glue matrix, thereby preventing high stresses on the
substrate. These glues also show a greater tendency to
creep under stress at high RH levels [61, p. 14]. Although
animal glues containing a high degree of helical structure
exhibit comparatively high stress when exposed to
extreme and fluctuating environmental conditions, they
still display greater stability in their strength properties
than more randomly coiled structures. The strength
properties of hot hide glue have been shown to be less
sensitive to fluctuating RH and temperature than those
of cold liquid hide glue [6, 28]. Liquid fish glues are even
less stable than cold liquid hide glues under fluctuating
conditions [17]. It has also been suggested that a high fat
content, such as in rabbit skin glue, accounts for better
stability in moist conditions [5, 39]. Common methods
for improving the glue film’s hardness and resistance
to water are the addition of tanning agents, such as
aluminium trisulphate (alum), disodium triborate
(borax), sodium acetate or formaldehyde [9, 28, 35, 91].
These salts remove a certain amount of bound water
from the proteinaceous matrix by covalently bonding
to the hydrophilic sites in the glue, thus inducing the
formation of numerous new cross-links between the
protein molecules.
Mechanical properties of animal glues used as gap fillers
Although the excessive shrinkage and brittleness of
animal glues at low RH [88] makes them inferior gap
fillers on their own, modification with ‘plasticisers’ and
bulking agents can alter their properties, improving
their suitability for this application [39, 81]. Hard films
with a minimum tendency to distort can be achieved
by the addition of fillers such as magnesium sulphate
or mineral clays together with sugars and dextrins [28,
The addition of an inert filler dramatically changes
the physical and mechanical performance of animal
glues, depending on the proportion of glue present.
A high pigment concentration significantly reduces
intermolecular bonding within the glue medium [76,
86] and thus impedes dimensional changes of the
matrix in response to relative humidity changes [76]. In
addition, with the lack of chemical adhesion between a
proteinaceous binder and inert filler particles, the glue
is substantially weakened and this leads to low tensile
strength [7]. Therefore high MW glues, with their long
protein strands and ability to develop stabilising H-
bonds, are appropriate for fillers and gesso with a high
pigment concentration.
Ageing characteristics
Whilst substantial research has been published on the
behaviour of collagen-derived glues in a fluctuating
environment, information on the ageing mechanisms
and behaviour on exposure to light seems to be more
limited. According to Michel et al., isinglass from
sturgeon, of all animal glues, best retains its mechanical
properties with thermal and ultraviolet (UV) light ageing
and RH cycling [79, p. 271]. It shows markedly less
change in strength and stiffness than pure mammalian
gelatin. Mammalian gelatin increases in tensile strength
but becomes stiffer and more brittle upon artificial
ageing under UV light, fluctuating RH and temperature.
Isinglass from sturgeon remains much tougher and more
elastic than gelatin [79, p. 274]. It also develops the least
permanent dimensional change, whereas gelatin films
swell or creep slightly during ageing, and other animal
glues show an even more marked effect.
Collagen-derived glues, unless they have been modified
by the addition of tanning agents which causes them
to become relatively resistant to water, generally swell
readily when exposed to water and redissolve when
heated, even after centuries [23, 39]. Neher [89]
established that the Bloom strengths of hide and rabbit
skin glues are not correlated to their water-resolubility
and that all tested samples were completely and equally
successfully reversible after one month of natural
drying. Wooden joints bonded with fish glue or cold
liquid hide glue have also been shown to be detachable
with water after six months of natural ageing or RH and
temperature cycling [17]. An effect of the tannic acids of
oak wood and walnut on their resolubility could not be
established in this study.
The dependence of water-resolubility on original
solution concentration has been demonstrated for aged
and UV-irradiated hide and bone glues at concentrations
of between 2.5 and 20% [90, p. 302]. This research
showed that the lower the original concentration, the
lower the resolubility of the glue film. Bone glues were
more resoluble than hide glues, supposedly because
of their more pronounced molecular cleavage in the
protein matrix (Table 1).
Przybylo tested isinglass from sturgeon obtained from
different suppliers [23], and found that the source,
origin and preparation temperature have no significant
effect on the resolubility of the glue in water after
natural and artificial ageing, as all the films in the test
series remained resoluble. In contrast, Michel et al. [79]
report that their artificially-aged sturgeon isinglass films
were insoluble in water, even though no significant
molecular changes within the protein were detected.
The contradictory results of these two studies may be
due to different preparation procedures and artificial
ageing conditions, which varied in the type of light
source as well as cycles of exposure time, temperature
and RH.
Resolubility of animal glues may be reduced in cases
where the protein has come into contact with metal
ions (e.g. metal foils, tools, pigments), or with certain
organic pigments and tannins, either before, during or
even after their application [12, 23, 78]. Resolubility
of collagen-derived glue containing no additives is thus
very much dependent on the environment to which it
has been exposed, rather than being predetermined by
the type of glue. Cold liquid hide and fish glues, the
ingredients of which are often unknown to the supplier
and end user, may already contain additives that promote
cross-linking and, therefore, increase insolubility.
Colour changes on ageing
Hide and bone glues are generally much more strongly
coloured (amber to brown) and less transparent than
gelatin or isinglass because of their higher impurity
content. Higher levels of denaturation and molecular
cleavage also intensify the colour of gelatinous solutions
[47]. This phenomenon may be responsible for the
general observation that the higher the Bloom value, the
less yellow the gelatin [56]. Gelatin and isinglass appear
clear and virtually colourless if dried to thin films, even
though they yield slightly yellow or whitish solutions
[10, 14, 43, 56, 58, 61]. They are also very light fast
and show hardly any discolouration or yellowing with
age [8, 30, 79], which is why they are the only collagen-
derived glues suitable for pigment consolidation.
Isinglass is particularly popular for this purpose, as its
low refractive index, when compared with mammalian
gelatin, causes the least change in appearance of the
pigments after drying [71, 79].
This review of the different types of currently available
animal glue has shown that collagen-derived adhesives
vary in their chemical, physical and mechanical
properties. Being a natural polymer, performance is
partly dependent on the original collagen source, which
determines the glue’s chemical composition, but is also
strongly affected by the extraction and preparation
procedures. Molecular weight distribution is an
important factor which directly influences the protein
solution viscosity and contributes to gel strength and
Tgel. The degree of stabilisation of the protein matrix
by hydrogen and other chemical bonding is determined
by amino acid composition, preparation procedures
and drying time. This has an even greater impact on
the performance of the glue, and significantly affects its
strength, mechanical behaviour, sensitivity to ambient
environment and stability with age. Changes in pH
and the addition of hygroscopic additives (plasticisers)
and salts can alter many of these properties. However,
manipulation of one individual factor cannot necessarily
be realised without simultaneously changing a whole
range of other properties. As most of the properties are
dependent on each other, selection of the appropriate
glue should be based on a correct balance rather than on
individual properties.
It has become evident that much important data that
would allow comparison of the properties of the different
types of glues is still missing. Very few gelatinous
glues have been prepared and tested under the same
conditions, and insufficient characterisation of these
glues makes it difficult to draw exact conclusions for a
general glue type, as physical and mechanical properties
can vary substantially. However, a summary of the data
does reveal general qualitative trends that can be used
by conservators to make well-informed decisions on the
suitability of a particular collagen-based glue for a given
The author would like to thank Shayne Rivers, Senior
Furniture Conservator at the Victoria and Albert
Museum, London, and Dr Ambrose C. Taylor, Imperial
College, London, for their ongoing support in discussing
this paper and their valuable advice.
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77 Burgio, L., Rivers, S., Higgitt, C., Spring, M., and Wilson,
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78 Wehlte, K., Werkstoffe und Techniken der Malerei,
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79 Michel, F., Geiger, T., Reichlin, A., and Teoh-Sapkota, G.,
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(2002) 257–275.
80 Yannas, I.V., and Tobolsky, A.V., ‘Cross-linking of gelatine by
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81 Thornton, J., ‘A brief history and review of the early practice
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82 Petukhova, T., ‘A history of fish glue as an artist’s material:
Applications in paper and parchment artifacts’, The Book and
Paper Group Annual of the American Institute of Conservation
19 (2000) 19–29.
83 Choi, Y.H., Lim, S.T., and Yoo, B., ‘Measurement of dynamic
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84 Djagny, K.B., Wang, Z., and Xu, S., ‘Conformational changes
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85 Hedley, G., ‘Relative humidity and the stress/strain response
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on the mechanical properties of collagen under equilibrium
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June 1988, American Institute for Conservation, Washington
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88 Grattan, D.W., and Barclay, R.L., ‘A study for gap-fillers
for wooden objects’, Studies in Conservation 33 (1988)
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Strengths of Animal Glues and Five Different Methods of
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und Konservierungswissenschaften, Technische Universität
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Nanke Schellmann trained as a violin maker in
Mittenwald (Bavaria) before undertaking several years
of internships in the conservation departments of the
National Gallery (Frames) and the Wallace Collection
in London, the Bavarian National Museum, Munich
and the Germanic National Museum, Nuremberg. In
2003, she received an MA in Furniture Conservation
from the Royal College of Art/Victoria and Albert
Museum (RCA/V&A) Joint Conservation Programme,
London, UK. On finishing, she joined the workshop
of Clemens von Schoeler, Munich as a conservator for
furniture and historic wooden interiors. Since 2005
she has attended additional courses in natural sciences
at the Ludwig-Maximilians-University, Munich and is
currently undertaking a PhD at the University of Fine
Arts Dresden, together with the V&A Mazarin Chest
Project and Imperial College, London, in the field of
oriental lacquer conservation.
Correspondence can be sent to:
Nanke Schellmann
Mazarin Chest Project
Furniture, Textiles and Frames Conservation
Victoria and Albert Museum
South Kensington
London SW7 2RL
... Živalske produkte obrtniki in umetniki že stoletja uporabljajo kot sestavino za izdelavo lepil, premazov in veziv (Buck, 1990;Schellmann, 2007). Lepila iz živalskih produktov delimo na glutinska (lepila iz kož, kit, kosti, roževine in rib), kazeinska (lepila iz mleka) in krvnoalbuminska (lepila iz krvnega albumina) (Resnik, 1989). ...
... Znano je, da se je ribja želatina, pridobljena iz ribjega plavalnega mehurja, že pred več stoletji uporabljala za lepljenje lesa (Schellmann, 2007). Dandanes se ribji klej še vedno uporablja pri izdelavi in popravilu glasbil, konzerviranju starih lesenih Sitar, M., Pondelak, A., Grbec, S., & Šernek, M.: Shear strength of fish glue bonds of glued wood evaluated by the ABES method stavb in restavriranju lesenih artefaktov, konzerviranju papirja ter tudi na primer za lepljenje pohištva iz mahagonija na Kitajskem (Petukhova, 1989;Pang, 2002;Schellmann, 2007). ...
... Znano je, da se je ribja želatina, pridobljena iz ribjega plavalnega mehurja, že pred več stoletji uporabljala za lepljenje lesa (Schellmann, 2007). Dandanes se ribji klej še vedno uporablja pri izdelavi in popravilu glasbil, konzerviranju starih lesenih Sitar, M., Pondelak, A., Grbec, S., & Šernek, M.: Shear strength of fish glue bonds of glued wood evaluated by the ABES method stavb in restavriranju lesenih artefaktov, konzerviranju papirja ter tudi na primer za lepljenje pohištva iz mahagonija na Kitajskem (Petukhova, 1989;Pang, 2002;Schellmann, 2007). Uporaba naravnega ribjega kleja se je uveljavila zaradi njegovih odličnih lastnosti: trdnosti, prožnosti, netoksičnosti, topnosti v vodi ter reverzibilnosti. ...
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V prispevku smo s pomočjo sistema za avtomatizirano vrednotenje zlepljenosti (ABES) ugotavljali razvoj strižne trdnosti ribjega kleja pri lepljenju lesa. Uporabili smo bukov (Fagus sylvatica L.) furnir, ki smo ga lepili pri konstantnem tlaku 12 barov, medtem ko smo spreminjali temperaturo in čas stiskanja. Temperatura je znašala med 25 °C in 100 °C, z intervalom 25 °C, čas stiskanja pa od 1 minute do 60 minut. Dosežena maksimalna strižna trdnost je znašala okoli 10 N/mm2, dosegli smo jo pri vseh štirih proučevanih temperaturah stiskanja. Na podlagi rezultatov študije smo ugotovili, da strižna trdnost ribjega kleja pri različnih temperaturah segrevanja neenakomerno narašča. Pri višjih temperaturah segrevanja hitreje dosežemo maksimalne strižne trdnosti. Strižne trdnosti spoja lepila iz ribjega kleja smo ugotavljali tudi po standardih EN 204 in EN 205.
... The second additive was a natural polymer derived from fish collagen with adhesive properties [22]. The purest form of fish glue is so-called isinglass, which is obtained from the skins of non-oily fish species or their bones, heated in water, then cooled and dried to produce gelatin or glue. ...
... The obtained results are not consistent with those of the study carried out by Sickels [9], where it is reported that animal glue increases workability. On the other hand, the study by Schellmann [22] states that animal glue may have an undesirable tendency to form small air bubbles in the glue matrix. The same effect, that animal glue acts as a foaming agent, was also noted by Elert et al. [13]. ...
... Elert et al. [13] attribute this effect to the delay in carbonization caused by the organic additive and the resulting large air bubbles, which can have a negative effect on the mechanical properties. According to Schellmann [22], animal glue can act as a foaming agent, leading to the formation of air bubbles during the mixing of grouts, which can reduce the strength. This effect of air bubbles could be a possible reason why the compressive strength of grout LS-G1 with animal glue did not increase compared to the reference grout LS. ...
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Organic additives from plant and animal extracts were commonly used in lime mortar in the past to improve and modify its properties. In modern times, they have been replaced by inorganic additives. The objective of this research is to investigate the influence of fish animal glue and the role of the filler particle size distribution on the fresh and hardened properties and durability of lime grouts. Wet density, water retention, fluidity, and injectability were tested in the fresh state. It was found that the particle size distribution of the selected filler, which can increase the packing density of the solid particles of the grout, and the W/B ratio have a great influence on water retention and fluidity. In the hardened state, porosity and compressive and splitting tensile strength were evaluated on 90-day- and 365-day-old specimens. The presence of animal glue improved the mechanical properties, due to a higher carbonation rate. The combination of the two fillers that resulted in a better packing of filler particles decreased the splitting tensile strength of the grout. To investigate the durability of the selected grouts, adhesion strength was measured on disc-sandwich models after non-accelerated and accelerated aging. The results show that the adhesive strength of grouts aged under laboratory conditions is lower than that of grouts subjected to accelerated aging.
... Gelatin is simply obtained by converting the triple helix of collagen into random coils (18). During gelatin extraction, the triple helices are first cleaved into single-stranded α-helix (3,5,19). However, during the subsequent gelatinization and drying process of the gelatin, these triple helices are subsequently formed (7,19). ...
... During gelatin extraction, the triple helices are first cleaved into single-stranded α-helix (3,5,19). However, during the subsequent gelatinization and drying process of the gelatin, these triple helices are subsequently formed (7,19). These helices act as physical cross-links in the gelatin, resulting in a three-dimensional lattice structure. ...
Full-text available
The present research was aimed to investigate the effects of sulfuric acid on the structures of gelatin polypeptides. Gela-tin samples were immersed in 0.5 M sulfuric acid solution for different periods of 15, 30, 60, 120, 240, 480, 960, and 1920 s, with possible structural changes analyzed by Fourier-transform infrared spectroscopy (FT-IR). Spectra at amide I and II regions were scrutinized using the Gaussian deconvolution method for the resulting changes in the protein secondary structure. The hydrolysis process initially led to a decrease in the α-helix chain and an increase in random coil and β-sheet structures. An equilibrium was formed in degradation and these structures were sequentially turned on each other. Results revealed a correlation between the peak intensity changes of these conformations, so that the degradation process could be observed in the conversion of α-helix to random coil and β-sheet structures and vice versa, indicating the oxidation and expansion of protein structure at the onset of the degradation process.
... There are many mechanisms used by plants to ensure that their fruits adhere to carrier animals (36), the two principle ones being hooks or viscid outgrowths (structures that secrete sticky substances). We attempted to simulate the adherence properties of both these by creating an adhesive pad stuck to the tags that; (i) simulated the physical structure of natural burs, (ii) used a tacky glue (40) and (iii) used natural burs. To do this, we standardized a tag-animal interface consisting of a speci c area of plastic, onto one side of which various hooks and protrusions were attached. ...
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Background: The attachment of electronic tags to animals has led to data collection that has hugely enhanced our understanding of wild animal behavioural ecology and physiology. However, animals are normally captured and restrained/sedated so that the tags can be attached, which is stressful for the animals and threatens to compromise the quality of the data gathered, at least during an initial acclimation period. We note that many plant seeds have evolved to become attached to passing animals and suggest that an approach, based on plant burs, could be used to attach tags to animals without capture or restraint. Methods: We present a framework for ‘bur-tagging’ and provide details of the design of a bur-tagging system, highlighting issues that we feel should be considered for the approach to be successful. Results: We report how the tagging site in the environment and animal neophobia critically affect the probability that an animal will be tagged over any given time period and also document what needs to be done to ensure that only the target species is tagged as well as illustrating the steps that can be taken to enhance the accuracy of tag placement on the animal. In addition, we discuss the criticality of the choice of the adhesive mechanism between the tag and the animal and illustrate how animals react to being tagged using this system. Conclusion: Although in an early stage of development, we believe that ‘bur-tagging’ shows great promise for deploying sophisticated electronic tags on wild animals with less stress than the conventional capture and restraint approach.
... Their stabilization is complicated by the high risk of optical changes caused by consolidation, and limited availability of treatment methods and materials. Among these, Isinglass [1], Funori, Jun-Funori, Tri-Funori [2][3][4], and Methocel A4C [5] have become established as effective and stable consolidants. The few other materials in occasional use, such as ethyl hydroxyethyl cellulose (EHEC), hydroxy propyl cellulose (HPC), and hydroxy ethyl cellulose (HEC), have been assessed in past studies to be of average or insufficient stability for conservation treatments [5]. ...
Full-text available
Paintings and other works of art created with fragile and mechanically unstable powdery me-dia present challenges to conservators. Frequently, powdery media is water-sensitive, extreme-ly fragile, tends to delaminate, and may be altered by even the slightest physical action or in-teraction with liquids. Materials that can provide an efficient stabilization without unaccepta-bly altering the optical characteristics of the delicate substrate are extremely limited. Among these, Funori, Isinglass, and Methocel A4C have become established for this use. In bench prac-tice, consolidants are frequently applied in a non-contact way, using ultrasonic and pneumatic aerosol generators to minimize the impact of the consolidant on sensitive substrates. However, nebulizing the available materials is problematic in bench practice, because of their high vis-cosity and, only extremely low concentrations can be nebulized using low kinetic impact ul-trasonic or pressure-based misting systems adopted from the healthcare industry. As a poten-tial innovative solution, this study introduces novel ultra-low viscosity (ULV) cellulose ethers (ULV-HPMC) for stabilisation of unstable porous and powdery surfaces, which have been suc-cessfully applied in bench practice for the pilot treatment of Edvard Munch painting on canvas and two 19th c. Thai gouache paintings on panel. Novel ULV-HPMC materials have multiple desirable qualities for consolidation treatments in conservation, and in accelerated aging tests marginally outperformed Methocel A4C, considered to be one of the most stable consolidants in the practice of conservation. Because of the ultra-low viscosity, higher concentrations of ULV-HPMC materials can be applied as water-based aerosols in a non-contact way and in few-er applications, which is a significant advantage in the treatment of delicate water-sensitive surfaces. Notably, novel ULV biopolymers are low-cost, derive from sustainable and renewable sources, and do not raise health and environmental concerns. Such novel materials and methods seamlessly resonate with the ICOM-CC’s Melbourne 2014 declaration, EU Green Deal, and the UN’s Sustainable Development goals and show potential for adding new sustainable materials with exceptionally low viscosity to the conservator’s toolbox.
... As consolidates and adhesives for organic and inorganic materials, animal glues are natural polymers derived from fish collagen, connective tissue, cartilage, and bones 70 . Gilded tin foil in the fresco was used by medieval painters to decorate the corona with noticeable fungal spores where lead-based paints were applied 19 . ...
Full-text available
This study focuses on the magnificent decoration of a painted and gilded wooden panel with signs of fungal biodeterioration caused by Aspergillus species in the Mausoleum of Sultan al-Ashraf Qaytbay, Cairo, Egypt. Numerous spectroscopic analyses and investigation techniques, including Scanning Electron Microscope Equipped with Energy Dispersive X-ray analysis (SEM–EDX), Fourier Transform Infrared analysis (FTIR), and X-Ray Diffraction (XRD) have been used to study the materials that comprise this painted and gilded wooden panel composition. Aspergillus niger , A. flavus , and A. terreus were recognized as isolated fungi, and their accession numbers are OQ820164, OQ820163, and OQ820160, respectively. The findings showed that the wooden support is of pinewood ( Pinus halepensis ), the white priming layer on top of the wooden support was identified as gypsum, the blue paint layer has been proposed to be Azurite, Au (gold) was the primary composition of the gilding layer, while Pb (lead) was detected in some spots, suggesting the use an alloy of gold with lead, and finally, animal glue was the bonding medium. Based on these findings, mimic samples with identical substrates and structural components have been designed, and the biodeterioration signs by the growing of the three Aspergillus species— A. niger , A. flavus and A. terreus were evaluated via SEM and color change. However, A. niger was discovered with density growth on surfaces of pinewood, gypsum, and Azurite and with less growth on the gilding layer after 6-month incubation. This contrasts with A. terreus and A. flavus , which had greater density growth on Azurite and stucco than on pinewood and less growth on the gilding layer. The used analytical methods with detailed analyses revealed the novelty and significant future aspects of the conservation of the painted and gilded wooden panel. Particularly given that this location is used for prayer and is crowded with people five times a day, which increases the accumulation of fungi and negatively affects both the historic Mosque and the worshippers' health.
... Today, the reuse of wastes from fish production, including isinglass, presents a promising avenue for addressing both environmental and technological challenges. Isinglass, a protein-rich substance obtained from fish bladders, is commonly used in the beer and wine industry as a fining agent [43][44][45]. However, its potential extends far beyond this traditional application. ...
Full-text available
The presented work discusses in detail the preparation of a cheap and environmentally friendly biopolymer membrane from isinglass and its physicochemical characterisation. One of the possible uses of the obtained membrane can be as a separator between electrodes in novel green electrochemical devices as in, for example, electric double-layer capacitors (EDLCs). The functionality of the mentioned membrane was investigated and demonstrated by classical electrochemical techniques such as cyclic voltammetry (CV), galvanostatic cycling with potential limitation (GCPL), and electrochemical impedance spectroscopy (EIS). The obtained values of capacitance (approximately 30 F g−1) and resistance (approximately. 3 Ohms), as well as the longevity of the EDLC during electrochemical floating at a voltage of 1.6 V (more than 200 h), show that the proposed biopolymer membrane could be an interesting alternative among the more environmentally friendly energy storage devices, while additionally it could be more economically justified.
Analysis of pH and cosolvent effects on protein structure is a popular study in food biophysics research since the function of protein is primarily dependent on its structure. The structure-function relationship of protein could be well reflected in changes in non-covalent interactions of protein. In this aspect, the present work deals with the Fourier transform infrared (FT-IR) spectroscopy analysis of ovalbumin (OVA) in different pH conditions with and without cosolvent sucralose (SUC) inclusion. The FT-IR spectrum of proteins provides an absorption spectrum in the frequency region of 4000-400 cm-1. These absorption bands consist of amide A, amide B, and amide I to amide VII. The results are interpreted in terms of noncovalent interactions, such as van der Waals interactions, hydrogen bonds, and hydrophobic and electrostatic interactions. The obtained results indicate that OVA is denatured from its native state against pH and SUC inclusion.
Early fungal infection of citrus is one of the common diseases found during the storage period of citrus, and fungus that infects citrus will spread to the entire batch of citrus as the degree of infection deepens, causing enormous economic losses. Therefore, early detection of fungal infection of citrus is fundamental. The purpose of this study is to explore the qualitative identification of early fungal infections in citrus by using Fourier transform near-infrared (FT-NIR) combined with a variety of chemometric methods. First, discrete wavelet transform (DWT) is used to filter the noise of the spectral signal, then combined with a PLS-DA model, that helps discriminate healthy from infected Citrus. Subsequently, four different feature variable selection methods were introduced, Then, the linear discriminant analysis (LDA) and support vector machine (SVM) two classifiers were combined to establish a qualitative model for the degree of fungal infection. The modeling results show that the SVM modeling effect is better than LDA, and the DWT-CARS-SVM based on the RBF kernel function has the best result, the accuracy rates of the training set and test set are 100% and 97%. The results indicate that FT-NIR spectroscopy, combined with chemometric methods, is able to distinguish early fungal infections in citrus.
A comprehensive guide to the technology and conservation of both Asian and European lacquer.
The comparison of physical and mechanical properties of socks knitted from cotton, linen and bamboo yarn has been carried out, it has shown that the properties of socks from bamboo yarn are close to those of the socks of cotton yarn and surpass them by hygroscopicity in two times.