Constanza Liggieri

Constanza Liggieri
Universidad Nacional de La Plata | UNLP · Centro de Investigación de proteínas vegetales (CIPROVE)

About

24
Publications
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397
Citations
Citations since 2017
9 Research Items
210 Citations
2017201820192020202120222023010203040
2017201820192020202120222023010203040
2017201820192020202120222023010203040
2017201820192020202120222023010203040
Introduction
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Publications

Publications (24)
Article
Full-text available
Helicobacter pylori is a Gram negative bacterium most frequently associated with human gastrointestinal infections worldwide. The increasing occurrence of antibiotic-resistant isolates of H. pylori constitutes a challenge. The eradication of the microorganism is currently being considered a “high priority” by the World Health Organization (WHO). In...
Article
Full-text available
A crude extract with proteolytic activity was prepared from edible fruits of Bromelia serra, containing cysteine peptidases with molecular masses between 24.1 and 25.9 kDa. The extract presented an optimal pH range of 6.03‒9.05, retained more than 80% of activity after thermal pre-treatments at 23, 37, and 45°C (120 min), but it was rapidly inactiv...
Article
Full-text available
Our objective was to isolate peptidases from the latex of Maclura pomifera fruits and use them to hydrolyze food proteins, as well as to purify and characterize the main peptidase. Two partially purified proteolytic extracts were prepared by ethanol (EE) and acetone (AE) precipitation from an aqueous suspension of exuded fruit latex. EE was used to...
Article
BACKGROUND The most common milk‐clotting enzymes in the cheese industry are recombinant chymosins. Food naturalness is a factor underpinning consumers’ food choice. For consumers that avoid food with GMO‐derived ingredients, the use of vegetable‐based rennet substitute in the cheese formulation may be a suitable solution. Artichokes that deviate fr...
Article
•The aim of this work was to study different immobilization strategies on silica supports in order to obtain robust biocatalysts from latex proteases of Asclepias curassavica L., a South American native plant. Immobilized enzyme performance was evaluated under harsh reaction conditions such as the synthesis of the antihypertensive peptide N-α-CBZ-V...
Article
Full-text available
In this study we report the enzymatic synthesis of N‐α‐[Carbobenzyloxy]‐Tyr‐Gln‐Gln (Z‐YQQ), a new anticoagulant tripeptide. It was obtained using phytoproteases from the stems and petioles of Asclepias curassavica L. as catalyst in an aqueous–organic biphasic system formed by 50% (v/v) ethyl acetate and 0.1 M Tris – HCl buffer pH 8. The resulting...
Article
Binary blends of S. marianum–flower extract and chymosin, as coagulant preparations, enabled the manufacture of miniature cheeses with distinctive characteristics compared to those of chymosin-renneted cheeses. The physicochemical parameters, sensory attributes of the cheeses, and in-vitro water-soluble antioxidant activity were analyzed and compar...
Article
A partially purified proteolytic extract prepared from Maclura pomifera latex was employed in hydrolyzing a soybean-protein isolate (4.2 mg/mL). The hydrolysis-product formation, monitored by tricine–sodium-dodecyl-sulfate–polyacrylamyde-gel electrophoresis and reverse-phase high-performance liquid chromatography, indicated that after 10 min of rea...
Article
In work reported here, a proteolytic extract prepared from Maclura pomifera latex was employed to hydrolyze bovine caseins. Densitograms of Tricine–sodium-dodecyl-sulfate–polyacrylamide-gel electrophoresis (SDS-PAGE) indicated that the caseins were considerably degraded after a 10-min reaction. The degree of hydrolysis determined by the 2,4,6-trini...
Article
Abstract In this article, we report the cloning of an aspartic protease (AP) from flowers of Arctium minus (Hill) Bernh. (Asteraceae) along with the use of depigmented aqueous flower extracts, as a source of APs, for the hydrolysis of whey proteins. The isolated cDNA encoded a protein product with 509 amino acids called arctiumisin, with the charac...
Article
Full-text available
Background: Proteases constitute the largest product segment in the global industrial enzymes market; they are used in food, pharmaceutical, leather, textile, wood and detergent industries. Alkaline proteases improve the cleaning efficiency of detergents and represent one of the most successful applications of modern industrial biotechnology. The a...
Article
Full-text available
A crude extract named pomiferin was obtained from latex of fruits of Maclura pomifera (Raf.) Schneid. (Moraceae), containing serine endopeptidases. The caseinolytic activity was 14.1 ± 0.8 Ucas/mL and the protein concentration was 1.5 ± 0.1 mg/mL. Isoelectrofocusing of pomiferin followed by zymogram analysis showed several bands (pI 3.7–9.2) of whi...
Article
Full-text available
Araujiain aII, the protease with highest specific activity purified from latex of Araujia angustifolia (Apocynaceae), shows optimum proteolytic activity at alkaline pH, and it is completely inhibited by the irreversible inhibitor of cysteine proteases trans-epoxysucciny-L: -leucyl-amido(4-guanidino) butane. It exhibits esterolytic activity on sever...
Article
Food proteins encrypt bioactive peptides that can be released during gastrointestinal digestion or food processing by enzymatic proteolysis. Flowers of Carduae tribe, family Asteraceae, contain aspartic proteinases with milk clotting activity. Crude enzyme extracts with proteolytic activity were prepared from flowers of Arctium minus at pH 7.0, and...
Article
Full-text available
Two cysteine endopeptidases from latex of Araujia angustifolia (araujiain aI and araujiain aIII) were purified and characterized by means of conventional and proteomics techniques (MALDI-TOF). N-terminal sequences showed a high percentage of identity with cysteine proteinases belonging to the papain family. The peptide mass fingerprint analysis dem...
Article
Latices from Asclepias spp are used in wound healing and the treatment of some digestive disorders. These pharmacological actions have been attributed to the presence of cysteine proteases in these milky latices. Asclepias curassavica (Asclepiadaceae), "scarlet milkweed" is a perennial subshrub native to South America. In the current paper we repor...
Article
Partially purified preparations with proteolytic activity, obtained from South American native plants, were used as biocatalysts in condensation reactions of N-protected arginine alkyl ester derivatives with decylamine and dodecylamine in low-water content systems. The final products are cationic surfactants with potential application as emulsifier...
Article
Full-text available
Most of the species belonging to Asclepiadaceae family usually secrete an endogenous milk-like fluid in a network of laticifer cells in which sub-cellular organelles intensively synthesize proteins and secondary metabolites. A new papain-like endopeptidase (asclepain c-II) has been isolated and characterized from the latex extracted from petioles o...
Article
To get a better insight into the ligninolytic system of Grammothele subargentea, extracellular ligninolytic enzyme activities and ability to degrade synthetic dyes as well as Eucalyptus globulus wood were assayed in cultures grown on an agar medium with Cu2+ or dyes and on E. globulus wood chips. Laccase was the only ligninolytic enzyme detected. T...
Article
In this work we report the isolation, purification and characterization of a new protease from latex of Asclepias curassavica L. Crude extract (CE) was obtained by gathering latex on 0.1 M citric-phosphate buffer with EDTA and cysteine with subsequent ultracentrifugation. Proteolytic assays were made on casein or azocasein as substrates. Caseinolyt...
Article
Two new endopeptidases were purified to homogeneity from the latex of Araujia hortorum fruits by a simple purification procedure involving ultracentrifugation and ion exchange chromatography. Molecular weights of araujiain h II and araujiain h III were 23,718 and 23546 (mass spectrometry), respectively. The isoelectric point of araujiain h II was 8...

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