Koch ChaSarn Journal of Science Vol.37 No.1 1
Cheddar Cheese Review: I Cheese
Cheddar cheese is one of the most popular cheese varieties in the world. It can be
categorized as hard cheese. According to its standard of identity, Cheddar cheese is required
to have a minimum of 50% fat content and a maximum of 39% moisture content. Cheddar
cheese is rennet coagulated and will require up to two years of aging before consumption.
The production of Cheddar cheese can be divided into two stages, which are manufacture
and ripening. The manufacture of Cheddar cheese consists of preparing and standardizing
milk, adding starter culture with rennet, coagulating milk, cutting the coagulum into small
cubes, heating and agitating the cubes, removing the whey, fusing the curd into slabs
followed by milling or continuous stirring the Cheddar curd, salting, pressing, vacuum
packaging, and ripening prior to consumption.
Keywords: Cheddar cheese, milk protein, rennet coagulation
The global cheese consumption is expected
to reach 21 million metric tons, which is a 20%
increase, between 2008 and 2015 (PRWeb,
2008). About two-thirds of total U.S. cheese
production in 2010 was from Cheddar and
Cheddar cheese is ranked
the second behind Mozzarella with a difference
of only approximately 22,000 lbs (National
Agriculture Statistics Service, 2011). Although
Cheddar making is a cheese relatively simple
process, it is still challenging to produce Cheddar
cheese with consistent quality (Lawrence et al.,
Food Science and Technology Program, Faculty of Science and Technology
Muban ChombuengRajabhat University, Chombueng, Ratchaburi 70150
2 37 1
2004). Cheddar cheese manufacture has been
continuously studied for almost 150 years as
the first reliable Cheddar cheese analyses were
reported and published in 1877 (van Slyke, 1893).
Significant improvements in the cheese
manufacture have been made over a century.
For instances, pasteurization process was
applied to the cheese milk in the beginning of
the 1900's. The use of pasteurized milk in place
of raw milk for the Cheddar cheese manufacture
was proven to provide more uniform and better
quality Cheddar cheese, which ultimately
provided more profits for the cheese
manufacturers (Price, 1927).
Mechanization for the Cheddar cheese
manufacture was introduced around the 1950's.
The mechanized system could essentially
shorten the whole cheese manufacture,
which would be beneficial for the cheese
manufacturers (Czulak, 1958; Olsen, 1980).
The objective of this article is to give an overall
review on manufacture of Cheddar cheese.
Cheese is a complex biological system.
To manufacture Cheddar cheese with consistent
quality, good quality and clean-tasting milk
that has relatively low microbial count is
needed (Farkye, 2004). Some aspects of
milk quality maybe defined under a broad
range of characteristics including microbial,
chemical and enzymatic.
Raw milk can contain pathogenic bacteria
such as Escherichia coli, Salmonella, Listeria,
Campylobacter, Mycobacterium and Brucella.
Yeast growth during cheese ripening can also
originate from raw milk. However, most, if
not all, current Cheddar cheese production in
industrial scale use pasteurized milk. Thus, pathogenic
bacteria and yeast from raw milk will be of
no greater threat to public health. Proteinases
from psychrotrophic bacteria in milk such as
Pseudomonas fluorescens and P. putrefaciens are
heat stable, which are not affected by pasteurized
temperature. These enzymes can hydrolyze
C-terminal region of β-casein and α
resulting in bitter hydrophobic peptides that
can cause bitter flavor to accumulate during
cheese ripening (Sheehan, 2013).
Antibiotics are the main chemical residues that
can be found in milk. Normally, antibiotics are used
to treat mastitis or infections of the cow mammary
gland caused from bacterial infection. If present in
cheese milk, antibiotic residues will cause
partial or total inhibition of starter culture
growth and acid production. During Cheddar
cheese manufacture, if low levels of antibiotic
residues are present, rate of acidification during
draining and salting is reduced, which will
result in longer manufacture time and may
cause a higher pH in cheese. High levels of
antibiotic residues can cause a complete termination
Koch ChaSarn Journal of Science Vol.37 No.1 3
of acidification after rennet addition, which
will result in an exceptionally high pH in cheese.
This resultant cheese may also have an uneven
texture with pasty body and unusual off-
flavors (Sheehan, 2013).
Plasmin is the main indigenous proteinase
in milk. If high level of plasmin is present in
milk, the rate of primary proteolysis will also be
elevated. This will result in longer rennet
gelation time and low gel firmness with more
porous and open structured rennet gel.
Because plasmin is relatively high-heat stable, its
contribution to primary proteolysis is more
obvious in cheeses that used high cooking
temperature during manufacture such as
Swiss and grana-type cheeses.Comparing to
Cheddar cheese, the level of plasmin activity
in high-cook cheeses is higher because plasmin
inhibitor is inactivated (Sheehan, 2013).
Originally, milk proteins were believed to
be a simple homogeneous protein, but about a
century or more ago, milk proteins were divided into
two broad classes. The first fraction, which
is about 80% of the protein in bovine milk,
is precipitated at pH 4.6 (isoelectric pH) at 30ºC,
and is now called casein. The second minor
fraction, makes up about 20% of protein, is
soluble under those conditions, and is now
referred to as whey protein, serum protein,
or non-casein nitrogen (Dalgleish, 1982). It is
suggested that the proteins in casein micelles are
bound together by two types of bonding,
and it is a balance between the attractive
hydrophobic interactions and electrostatic
repulsion. Hydrophobic interaction is the
driving force for the formation of casein micelles, while
electrostatic repulsions are limiting the growth of
polymers or in other words defining the degree
of polymerization. The conformation of α
and β-caseins when they are adsorbed at
hydrophobic interfaces form a train-loop-
train and a tail-train structure, respectively,
and both caseins polymerize or self-associate,
by hydrophobic interactions.
Accordingly, the self-association of caseins
makes it possible for polymerization to occur.
Calcium phosphate nanoclusters, or CCP,
are considered to be one of the linkages
between casein micelles and act as neutralizing
agents of the negative charge of the phos-
phorserine residues. Consequently, electro-
static repulsion is reduced and the hydrophobic
interaction between caseins is still dominant,
resulting in more associations of proteins.
Unlike the other caseins, κ-caseins can only
interact hydrophobically and acts as a
propagation terminator, because they do not
have a phosphoserine cluster to bind calcium
and also another hydrophobic point to prolong
the chain (Horne, 1998). The structure of
casein micelle is as shown in Figure 1.
4 37 1
Figure 1 The dual bonding model of casein micelle structure, with α-, β-, κ-casein portrayed as indicated.
Bonding appears between the hydrophobic regions, shown as rectangular bars, and by linkage of hydrophilic
regions containing phosphoserine clusters to colloidal calcium phosphate (CCP) clusters. Molecules of κ-
casein (K) limit further growth of the structure.
Adapted from Goff, 1995 and Horne, 1998
Importance of calcium-phosphate and
κ-casein to the casein micelle
One of many important functions of the
casein micelle is to solubilize calcium
phosphates in milk (Farrell Jr. et al., 2006).
The dry matter of bovine casein has been
found to consist of about 94% protein and
6% mineral, which is colloidal calcium phosphate
(CCP) (Horne, 2006). The relationship between
investigated for over a century. However, this
relationship has not yet been fully understood
(Fox and Brodkorb, 2008). As hypothesized
by De Kruif and Holt (2004), CCP could be
bound and stabilized by phosphopeptide
portions of α
- and β-caseins, resulting in the
formation of calcium-phosphate nanoclusters
CCP and casein micelles has been vigorously
or CCP (Figure 2). This CCP would randomly
grow and precipitate without bridging with
peptides. In addition, the formation of CCP
is believed to generate casein micellestructure by
randomly binding with phos-phorproteins
until a size limited colloid is formed.
Koch ChaSarn Journal of Science Vol.37 No.1 5
Figure 2 Casein-calcium/phosphate cross-linked network; the black strands represent casein network, the
oval dots with the black tails represent organic phosphate, the oval dots represent inorganic phosphate, and
the circle dots represent calcium ions.
Source: Metzger, 2009 (personal communication).
According to Horne and his dual-binding
casein micelle structure model, CCP is considered
to begin the process of casein micelle formation
by acting like a bridge and neutralizing agent for
the phosphoproteins, which hydrophobically
interact to each other. The hydrophobic blocks
of protein-protein interactions and the CCP
linkage further generate the casein micelle
formation. This casein micelle has a gel-like
structure with embedded CCP and κ-caseins
as chain terminator (Horne, 1998; Farrell Jr. et al.,
2006). CCP along with hydrogen bonds,
hydrophobic and electrostatic interactions
are responsible for casein micelle stability.
It was found that the micelles dissolve into
small particles in milk solution once the CCP is
removed by acidification, dialysis or Cachelator;
thus this phenomenon suggests that CCP
play an important role in cementing the
micelles together (Fox and Brodkorb, 2008
At the concentration of protein and
calcium found in bovine milk, Ca-sensitive
- and β-caseins) are readily
precipitated by calcium bound to their
phosphoserine residues. However, κ-casein,
which is soluble in calcium, can interact and
stabilize about 10 times its mass around the
core of Ca-sensitive caseins. In addition,
because of the negative charge from oligo-
saccharide chains at the carboxy-terminal
ends of κ-caseins, they can provide steric
stabilization for the casein micelles in milk.
It has long been believed that κ-casein is
6 37 1
the only type of casein protein in the
surface layer. This has been confirmed by
the decrease in hydrodynamic diameter
during renneting, since chymosin removes
the protruding macropeptide portion of κ-
casein. However, other researchers have found
that N-terminal residues of all caseins are
released by super-polymerized amino peptidase
that cannot diffuse into the micelle. These
phenomena suggest that κ-casein is not
very exposed and that the surface of the
micelle is not exclusively covered with κ-casein.
Consequently, some of the other casein
fractions are also located on the surface of
the micelle (Horne, 2003; Horne, 2006;
Farrell Jr. et al., 2006; Fox and Brodkorb,
2008). A study by Dalgleish et al. (2004)
suggested that the casein micelle surface
was more complex than just a simple hard
sphere covered by a ‘hairy layer’. The
electron micrograph from their study also
suggested that the micelles consist of
seemingly casein tubules with the end
protruding from the bulk structure that
protects the micelles. They then hypothesized
that κ-casein is probably only located at the
ends of the tubes and not evenly covering
the entire surface, since the amount of κ-
casein in milk is not sufficient to cover the
entire micelle surface on its own
Cheddar cheese manufacture
Milk is a highly perishable food; thus,
cheese manufacture is a form of milk preservation. All
cheeses from both acid and rennet coagulate
can be roughly classified, based on their moisture
content, as soft, semisoft (semi hard), hard,
or very hard (Figure 3). (Farkye, 2004).
Figure 3 Classification of cheeses based on their moisture content.
Adapted from Farkye, 2004.
Koch ChaSarn Journal of Science Vol.37 No.1 7
Cheddar cheese can be categorized as hard
cheese, which will require some pressure to chew
and break its structure apart. Cheddar cheese is
rennet coagulated and required two months
to two years of aging before consumption.
Cheddar cheese that has been ripened for a
longer period of time will allow its flavor,
aroma and texture to be fully developed (Mc
Sweeney, 2004). The production of Cheddar
cheese can be divided into two stages, which
are manufacture and ripening. The manufacture
of Cheddar cheese (Figure 4) consists of preparing
and standardizing milk, adding starter culture
with rennet, coagulating milk, cutting the
coagulum into small cubes, heating and
agitating the cubes, removing the whey,
fusing the curd into slabs followed by milling or
continuous stirring the Cheddar curd, salting,
pressing, vacuum packaging, and ripening prior
to consumption. (Hill, 1995; Lawrence et al.,
2004; Fox and McSweeney, 2004).
Figure 4 The manufacture diagram of Cheddar cheese.
Adapted from Avila, 2014.
8 37 1
The ripening process of Cheddar cheese will not
be process of Cheddar cheese will not be
discussed in this paper.
Rennet coagulation of milk
Rennet is a general term for proteinase
used to coagulate milk. Milk coagulants from
several sources such as vegetable, animal,
bacteria and fungi have been used in cheese
making. Rennet, a natural coagulant extracted
from the fourth stomach of the calf was the
main choice for the early cheese makers.
Traditionally, rennet extracted from
young calf stomachs are used to make
Cheddar cheese. This rennet contains 88–94%
chymosin, providing approximately 90% of total
milk clotting activity, and 6–12% pepsin,
providing approximately 10% of milk clotting
activity. Bovine chymosin is an aspartyl
proteinase containing approximately 320 amino
acid residues. Its physiological role is to coa-
gulate milk in the young mammal stomach,
resulting in an increase in the digestion efficiency.
(Horne and Banks, 2004; McSweeney, 2007).
The cheese production has increased, while
the supply of calf rennet has decreased; thus
this led to the use of alternative products,
which are other types of aspartyl proteinases.
Rennet substitutes should have high milk clotting
activity compared to general proteolytic
activity and specific activity on κ-casein. Rennet
substitutes include bovine and porcine
pepsins, microbial aspartyl proteinases, and
fermentation-produced chymosin cloned from
microorganisms. Rennet extracted from older
bovine contains about 6–10% chymosin and
90–94% pepsin. Bovine pepsin is quite
effective once blended with chymosin. Porcine
pepsin is unstable at pH more than 6; thus it
is usually used along with calf rennet.
Some yeasts and molds such as Rhizomu
cormeihei, R. corpusillus, and Cryphonectria
parasitica can naturally produce proteinase.
Fermentation-produced chymosin or recombinant
chymosin is produced by fermentation
of identical calf protein chymosin obtained
from cloning calf chymosin into host micro-
organisms (Kluyveromyces lactis, Aspergillus
niger, and Escherichia coli). These rennets
have shown excellent results in cheese
processing, but their use is still subjected to
regulation (McSweeney, 2007).
The coagulation reaction can be divided
into two phases, as shown in Figure 5. The primary
phase: the protolithic enzymes (chymosin, pepsin
or microbial proteinases) cleaveκ-caseins at a
specific bond. The secondary phase: casein
micelles start to aggregate. These coagulation
phases are in fact overlapping, since casein
micelles may begin to aggregate before the
κ-casein hydrolysis is completed. As previously
mentioned, κ-caseins are glycosylated with
hydrophilic short sugar chain in the carboxy-
terminal ends called glycomacropeptide
(GMP). This GMP consists of residues 106-
169, and hydrophobic para-κ-casein (residues 1-
Koch ChaSarn Journal of Science Vol.37 No.1 9
105). In order for the bovine casein micelles
to aggregate, κ-casein has to be hydrolyzed
at the Phe
bond between para-κ-
casein and GMP.Chymosin is considered suitable
for cheese manufacture, because it is specifically
active in hydrolysis of the Phe
κ-casein. Thus, during milk coagulation, κ-casein
is hydrolyzed at the Phe
and the hydrophilic GMP is released into the
serum phase, while para-κ-casein remains
bound to the casein network. The ongoing
loss of GMP results in the decrease in the
micelles zeta potential from -20 mV to about
-10 mV, and destabilization of the micelles.
Once κ-caseins have been sufficiently
hydrolyzed; casein micelles will aggregate
(Dalgleish, 1993; Horne and Banks 2004). In
addition, the micellar calcium and phosphate
are dissolved into the serum phase at the
lower pH (Denmark and Walstra, 2004).
Figure 5 Two stages of rennet coagulation. Primary stage–rennet enzyme cuts off κ-casein fragments, thus
removing the net negative charge from the micelle surface. Secondary stage–casein micelles aggregate and
form a gel network.
Adapted from Dalgleish, 1993.
Milk coagulation properties
Milk coagulation properties (MCP) are
important factors for cheese processing,
cheese yield, and cheese quality. The most
common approach to study MCP is to
monitor the viscosity of milk samples after
rennet addition that have been maintained
at a fixed temperature. The formgraph is an
apparatus that allows simultaneous evaluation
of MCP from several milk samples.
Formagraph-based MCP measurement is
based on movement of small-loop
stainless-steel pendulums immersed in
linearly oscillating samples of coagulating
milk. Forces are applied to the pendulums
because of the gel formation in the moving
milk samples. These forces are recorded,
10 37 1
and a typical formagraph is produced as
shown in Figure 6. From the formagraph,
three parameters that are considered to be
useful in order to monitor MCP include: 1)
rennet coagulation time (RCT, r, min), which
measures the interval from zero (enzyme or
rennet addition time) to the baseline begins
to widen, 2) the time to curd firmness of 20
, min), which measures the interval
from the start of gel formation to the time
that oscillation width becomes 20 mm, and
3) the curd firmness 30 min after rennet
, mm), which corresponds to the
width of the formagraph 30 min after
enzyme addition (Bittante, 2011).
Figure 6 Diagram of rennet coagulation time (r = RCT, min) and time to curd firmness of 20 mm (k
, min), and
curd firmness 30 min after enzyme addition (a
, mm) as a function of time as recorded with the Formagraph.
Adapted from Bittante, 2011.
Many indigenous factors have great
impact on MCP such as ruminant species,
breeds, and genetic variants of milk protein
especially κ-casein. Figure 7 depicts direct
and indirect genetic effects on MCP. Milk
from different ruminant species has different curd
firmness pattern. For example, milk from
smaller ruminants such as goat and sheep
coagulates earlier than cow milk. This
means that RCT from the formagraph is
longer, and, thus, k
might not be
measurable. For bovine breeds, milk from
Holstein-Friesian and some Scandinavian
breeds is considered to be non-coagulating
milk (De Marchi et al., 2013), which is milk that
has longer RCT, lower a
, and immeasurable
than does milk from Brown Swiss,
Simmental and other local alpine breeds
(Bittante et al., 2012). Genetic variation of
κ-casein in the degree of glycosylation (GD)
Koch ChaSarn Journal of Science Vol.37 No.1 11
has direct effect on MCP. It has been
recently reported that GD of milk from
Simmental breed ranged from 22 to 76%,
and milk with higher GD had shorter RCT than
milk with lower GD. Thus, the association
between RCT and κ-casein content mainly
owes the glycosylated fraction of the protein
(Bonfatti et al., 2014).
Other factors that affect MCP include
drug residues in milk and coagulation
temperature. In order to prevent the occurrence
of disease in milk production, drug treatment
might be used. Thus, milk might contain
residual drugs, which can pose problem for
the cheese manufacture. It has been reported
that milk samples containing trimethoprim
had longer RCT, lower a
, and immeasurable
, while the presence of sulfamides did
not alter MCP (Dreassi et al., 2007). Lastly,
coagulation temperature poses direct impact
on cheese microstructure, which consequently
influences cheese and flavor. Ong et al. (2011)
studied effect of coagulation temperature on the
microstructure and composition of full fat
Cheddar cheese. They reported that the
microstructure of milk gel coagulated at
27°C consisted of a fine interconnected
protein network, whereas gel coagulated
at 36°C consisted of a coarse, irregular and
more discontinuous protein network. At a
higher coagulation temperature, hydrophobic
and ionic interactions increased, which caused
rearrangement of casein micelles and an
increasing the size casein aggregates and the
size of protein strands, as shown in Figure 8.
Figure 7 Direct and indirect genetic effects on milk coagulation properties.
Adapted from Bittante et al., 2012.
12 37 1
Figure 8 Cryo SEM micrographs of rennet milk gel coagulated at (A1) 27°C and (A2) 36°C.
Adapted from Ong et al., 2011.
Cheddaring and salting steps
Traditionally, Cheddar cheese utilizes the
cheddaring process, where the curd is allowed
to fuse into slabs, which are turned, piled,
and re-piled at regular intervals for 1 to 2 hr
until reaching the desired pH. This process
causes the curd granules to fuse together
under gravity, which leads to a close-knit
and fibrous cheese structure. The cheddared
curds are followed by milling, which involves
mechanically cutting curds into small pieces.
The milling process facilitates uniform salt
distribution into the curds and promotes
whey drainage from the curds. However,
because of the development of hooping
and pressing of salted granular curd under
vacuum, the stirred-curd method has become
more commonly accepted. In this method,
drained curds are continuously stirred until
reaching the desired pH. Although the
constant agitating does not allow knitting of
curds, the use of ‘block former’ hooping and
vacuum pressing system yields Cheddar
cheese with a close-texture characteristic.
Thus, the stirred-curd method facilitating by
hooping and vacuum pressing eliminate the
need for cheddaring and milling. The stirred-
curd method requires shorter time than the
traditional method; thus this is the method
of choice in highly mechanized cheese plants
(Lawrence et al., 2004; Serrano et al., 2004;
Rehman et al., 2008).
Salt plays an important role in the
quality of Cheddar cheese, which include 1)
controlling the growth of lactic acid bacteria
and undesirable bacteria such as coliforms,
staphylococci and clostridia, 2) controlling
the final pH of Cheddar cheese as a result
of starter culture activity retardation, and
3) controlling overall flavor and texture of
the cheese. The main method of salting Cheddar
cheese curd is directly mixing dry salt crystals
into milled or stirred curd pieces after whey
removal. After dry salt is distributed over
the surface of cheese curd, some salt dissolves
and slowly move inwards the curd. This
causes a counter flow of whey from the curd to
Koch ChaSarn Journal of Science Vol.37 No.1 13
the surface and dissolves the remaining salt
crystals, creating a supersaturated brine
solution around each curd particle. The rate
of the salt uptake by the cheese curds
highly depends on the initial moisture in the
curd and the amount of the salt added. An
increase in salting level results in an increase in
the rate of both salt absorption by the cheese
curd and whey drainage from the cheese
curd (Guinee and Fox, 2004; Lawrence et
Cheddar cheese composition
According to USDA standard of identity,
Cheddar cheese is required to have the minimum
of 50% milk fat and the maximum of 39%
moisture content (Office of the Federal Register,
2006). Typically, Cheddar cheese composition
contains approximately 37% moisture, 25%
protein, 33% fat, 1% carbohydrate, and 4%
ash (Canadian Dairy Commission, 2011).
Since Cheddar cheese can be eaten fresh
or aged for up to 2 years, some chemical
composition of Cheddar cheese might change
over time. In order to produce a commercial
first-grade Cheddar cheese, a diagram (Figure 9)
with suggested ranges of moisture in the non-
fat substance (MNFS), salt-to-moisture ratio
(S/M), fat-in-dry matter (FDM), and pH has
been widely used. This useful diagram can
be a method for deciding which cheese should
be further ripened and which should be
sold more quickly (Lawrence et al., 2004).
Figure 9 Suggested range of salt-to-moisture ratio (S/M), moisture in the non-fat substance (MNFS), fat-in-dry
matter (FDM), and pH for first grade and second grade Cheddar cheese. Analyses 14 days after cheese
Adapted from Lawrence et al., 2004.
14 37 1
Cheddar cheese is a complex and
dynamic food system. Although there has
been quite extensive research about Cheddar
cheese for several decades, with an increase in
the global cheese consumption, more
research on this subject is needed in order to
meet continually changes in consumer demands.
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