Properties and applications of phytepsins from thistle flowers

Cavalli, Sandra Vairo; Lufrano, Daniela; Colombo, María Laura; Priolo, Nora

doi:10.1016/j.phytochem.2013.04.013

Cited by 32 publications

(30 citation statements)

References 105 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Action specificity of cardosin A and cardosin B from Cynara cardunculus upon isolated bovine, caprine, and ovine caseins (α s1 -, β-, and κ). [52] Bovine caseins…”

Section: Evaluation Of Enzymatic Activities Of Plant Rennetsmentioning

confidence: 99%

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Amira

Besbes

Attia

et al. 2017

International Journal of Food Properties

View full text Add to dashboard Cite

Plant rennets hold an important position among various coagulants used in cheese technology. The selection of a suitable plant coagulant is important due to the increasing global demands of cheese alongside reduced supply of calf rennet. Thus, a literature synthesis is presented to investigate recent achievements on their functional properties and enzymatic role in cheese making. Efforts have also been done to compare certain rheological and sensory properties of final products, arising from some plant-and animalbased rennets. In fact, some coagulants such as actinidin or dubiumin produce cheeses with sensory qualities similar to those produced by animal rennet. Others, like ginger, cucumisin, or hieronymain proteases contribute to develop very different textures and flavours, due to excessive proteolytic activity and production of bitter peptides. For milk-clotting enzymes with high non-specific action, several improved strategies have been developed to produce cheeses with sensory properties close to those of animal rennet. For example, the mixture of coagulants (cardosins/chymosin), the selection of appropriate milk or its ultrafiltration, as well as the increase of salting time of cheese during ripening could be efficient ways to improve texture and reduce bitterness. Concerning cheeses with high yield loss, the whey could be used for a traditional production of whey cheese. To conclude, the selection of appropriate plant rennet with high milk-clotting activity/proteolytic activity ratio and the optimisation of all coagulation parameters play a central role in manufacturing cheese with superior rheological and sensory properties.

show abstract

“…Action specificity of cardosin A and cardosin B from Cynara cardunculus upon isolated bovine, caprine, and ovine caseins (α s1 -, β-, and κ). [52] Bovine caseins…”

Section: Evaluation Of Enzymatic Activities Of Plant Rennetsmentioning

confidence: 99%

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Amira

Besbes

Attia

et al. 2017

International Journal of Food Properties

View full text Add to dashboard Cite

show abstract

“…In fact, it has been shown that cardosins E and G have proteolytic activities upper than that of cardosin A [8]. This was mainly explained by the presence of several residue substitutions in these enzymes, which were found close to the active site, and some of these substitutions may be the cause of this increased activity [10].…”

Section: Protein Separation On 2d-e and Maldi-tof-ms Identificationmentioning

confidence: 93%

“…The milk clotting enzymes, which are known as cardosins, have been found previously in all C. cardunculus cells and tissues, but particularly with high quantity in the flowers' pistils (styles and stigmas) [6]. Cardosin A is a glycosylated aspartic protease (AP) that has been studied in detail and was shown to be similar to chymosin, in terms of kinetic parameters and specificity, by cleaving the same peptide bond (Phe105-Met106) of the casein kappa [7,8]. The most abundant proteolytic activity corresponds to that of cardosin A [9] and at acidic pH, it represents from 75 to 90 % of total extracted enzyme activity [8].…”

Section: Introductionmentioning

confidence: 99%

“…Cardosin A is a glycosylated aspartic protease (AP) that has been studied in detail and was shown to be similar to chymosin, in terms of kinetic parameters and specificity, by cleaving the same peptide bond (Phe105-Met106) of the casein kappa [7,8]. The most abundant proteolytic activity corresponds to that of cardosin A [9] and at acidic pH, it represents from 75 to 90 % of total extracted enzyme activity [8]. The second aspartic protease studied was cardosin B, which is similar to pepsin, in terms of activity and specificity [7].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of proteins from wild cardoon flowers (Cynara cardunculus L.) by a proteomic approach

et al. 2016

View full text Add to dashboard Cite

Proteomic approach was applied to identify total proteins, particularly the enzymatic content, from wild cardoon flowers. As the selection of an appropriate sample preparation method is the key for getting reliable results, two different extraction/precipitation methods (trichloroacetic acid and phenol/ammonium acetate) were tested on fresh and lyophilized flowers. After two-dimensional electrophoresis (2D-E) separations, a better protein pattern was obtained after phenol extraction from lyophilized flowers. Only 46 % of the total analyzed spots resulted in a protein identification by mass spectrometry MALDI-TOF. Four proteases (cardosins A, E, G, and H), which have become a subject of great interest in dairy technology, were identified. They presented molecular weights and isoelectric points very close and high levels of homology between matched peptides sequences. The absence of the other cardosins (B, C, D, and F) could be an advantage, as it reduces the excessive proteolytic activity that causes bitter flavors and texture defects, during cheese making.

show abstract

“…2 Bovine whey protein concentrates, as well as purified proteins from whey after hydrolysis by the proteases from cardoon flowers (Cynara cardunculus), release highly potent ACE-inhibitory peptides. 2,3 Active fragments generated from a-lactalbumin and b-lactoglobulin were different from previously reported peptides obtained by enzymatic digestion of the same substrate with other peptidases. 2,4 The ACE-inhibitory activity was also reported by Cimino et al 5 upon hydrolysis of whey protein with flower aqueous extracts of Arctium minus, another member of the Asteraceae family.…”

Section: Introductionmentioning

confidence: 99%

Partial Molecular Characterization ofArctium minusAspartylendopeptidase and Preparation of Bioactive Peptides by Whey Protein Hydrolysis

Cimino

Colombo

Liggieri

et al. 2015

Journal of Medicinal Food

Self Cite

View full text Add to dashboard Cite

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 characteristic primary structure organization of typical plant APs. Bovine whey protein hydrolysates, obtained employing the enzyme extracts of A. minus flowers, displayed inhibitory angiotensin-converting enzyme (ACE) and antioxidant activities. Hydrolysates after 3 and 5 h of reaction (degree of hydrolysis 2.4 and 5.6, respectively) and the associated peptide fraction with molecular weight below 3 kDa were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, matrix-assisted laser desorption ionization/time of flight mass spectrometry, and reverse phase-high-performance liquid chromatography. The results obtained in this study demonstrate the viability of using proteases from A. minus to increase the antioxidant and inhibitory ACE capacity of whey proteins.

show abstract

Properties and applications of phytepsins from thistle flowers

Cited by 32 publications

References 105 publications

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

Identification of proteins from wild cardoon flowers (Cynara cardunculus L.) by a proteomic approach

Partial Molecular Characterization ofArctium minusAspartylendopeptidase and Preparation of Bioactive Peptides by Whey Protein Hydrolysis

Contact Info

Product

Resources

About