Controlled Hydrolysis of Cheese Whey Proteins Using Trypsin and α-Chymotrypsin

Galvão, Célia M.A.; Silva, Astréa F. Souza; Custódio, Marcos Franqui; Monti, Rubens; Giordano, Raquel de Lima Camargo

doi:10.1385/abab:91-93:1-9:761

Cited by 25 publications

(8 citation statements)

References 13 publications

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“…Trypsin cleaves on the C-side of basic residues (Arg and Lys) whilst chymotrypsin requires an aromatic or bulky nonpolar side-chain (Phe, Tyr, Trp, Leu, Met) on the carboxyl side of the scissible bond [31]. Thus, previous studies demonstrated that ␤-LG can be hydrolyzed to a large extent following a trypsin/chymotrypsin digestion [30,32,33]. To determine the complex peptide mapping of both digestion mixtures, MALDI-MS and LC-ESI-MS analyses were carried out.…”

Section: Identification Of ␤-Lg Peptides Resulting From the In Vitro mentioning

confidence: 99%

Mass spectrometric characterization of glycated β-lactoglobulin peptides derived from galacto-oligosaccharides surviving the in vitro gastrointestinal digestion

Moreno

Quintanilla-López

Lebrón-Aguilar

et al. 2008

J. Am. Soc. Mass Spectrom.

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A mass spectrometric study has been carried out to elucidate the structures of glycated peptides obtained after in vitro gastrointestinal digestion of bovine {3-lactoglobulin ({3-LG) glycated with prebiotic galacto-oligosaccharides (GOS). The digests of both native and glycated {3-LG were analyzed by MALDI-MS, LC-ESI-MS, and LC-ESI-MS/MS. MALDI-MS profiles showed marked differences mainly related to the lower intensity of ions corresponding to the digest of glycated {3-LG. Overall, 58 and 23 unglycated peptides covering 97% and 63% of the mature {3-LG sequence could be identified in the digests of native and glycated samples, respectively. The LC-ESI-MS analyses corroborated the MALDI-MS results regarding the unglycated peptides but they also enabled an extensive investigation into the digest of glycated {3-LG. Thus, a total of 19 peptides glycated with GOS from two to seven hexose units could be identified. The tandem mass spectra of glycated peptides were mostly characterized by two neutral losses of 1026/1056, 864/894, 702/732, 540/570, 378/408, and 216/246 u, corresponding to the formation of the furylium ion and its subsequent "CHOH" loss, indicative of the peptide glycation with hepta-, hexa-, penta-, tetra-, tri-, and disaccharides, respectively. Also, other minor ionic species containing the furylium ring linked to different galactose units could be also detected, showing the diversity of the fragmentation pattern of peptides glycated with larger size carbohydrates. Finally, the putative GOS glycation sites could be determined at the NHz-terminal Leu residue and at Lys residues located in positions

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Section: Identification Of ␤-Lg Peptides Resulting From the In Vitro mentioning

confidence: 99%

Mass spectrometric characterization of glycated β-lactoglobulin peptides derived from galacto-oligosaccharides surviving the in vitro gastrointestinal digestion

Moreno

Quintanilla-López

Lebrón-Aguilar

et al. 2008

J. Am. Soc. Mass Spectrom.

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“…Trypsin is an important proteolytic enzyme, already used in large-scale processes by the detergent and dairy industries [6]. The industrial use of this enzyme in the immobilized form is a trade-off between the reduction of the enzyme cost (since the catalyst can be reutilized) and the immobilization cost.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of trypsin on chitosan gels: Use of different activation protocols and comparison with other supports

Manrich

Galvão

Jesus

et al. 2008

International Journal of Biological Macromolecules

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“…Hydrolyzed by chymotrypsin, casein functional properties (such as antioxidant activity, angiotensin converting enzyme inhibition and antibacterial ability) are improved (Srinivas and Parksh, 2009). Chymotrypsin is used as an additive with trypsin to control hydrolysis of cheese whey proteins and β-lactoglobulin in the cheese production industry (Galvão et al, 2001). …”

Section: Food Industrymentioning

confidence: 99%

Extraction, Purification and Characterization of Fish Chymotrypsin: A Review

K.¹

2011

American Journal of Biochemistry and Biotechnology

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Problem statement: Solid fish waste is generated from the unwanted parts of fish including heads, tails, fins, frames, offal (guts, kidney and liver) and skin. It accounts for up to 80% of material from production of surimi, 66% from production of fillet and 27% from production of headed and gutted fish. Currently, fish wastes are disposed off in land-based waste disposal systems or at sea generating toxic byproducts during the decomposition process. However, fish processing waste can be used to produce commercially valuable by-products, such as chymotrypsin. Approach: A comperehensive review of the literature on the extraction, purification and characeterization of fish chymotrypsin was performed. Results: Chymotrypsin is an endopeptidase secreted by the pancreatic tissues of vertebrates and invertebrates. It has 3 different structures (chymotrypsin A, B and C) varying slightly in solubility, electrophoretic mobility, isoelectric point and cleavage specificity. Only chymotrypsin A and B are found in fish. Compared with mammal chymotrypsin, fish chymotrypsins have similar amino acid composition and molecular weights. Fish chymotrypsins have higher specific activity, especially those from cold-water fish, and low pH and temperature tolerance. The factors affecting the concentration and activity of chymotrypsin in fish are water temperature, fish species, fish age, fish weight and starvation. Chymotrypsin has application in various industries including the food industry, leather production industry chemical industry and medical industry. Conclusion: Extraction techniques for chymotrypsin include: ultra-filtration, ammonium sulphate fractionation precipitation or water-in-oil microemulsions. Purification can be carried out using recrystallization and gel-filtration, ion-exchange and hydrophobic interaction chromatography. Further studies should focus on the optimization of purifiying chymotrypsin from fish processing wastes.

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Controlled Hydrolysis of Cheese Whey Proteins Using Trypsin and α-Chymotrypsin

Cited by 25 publications

References 13 publications

Mass spectrometric characterization of glycated β-lactoglobulin peptides derived from galacto-oligosaccharides surviving the in vitro gastrointestinal digestion

Mass spectrometric characterization of glycated β-lactoglobulin peptides derived from galacto-oligosaccharides surviving the in vitro gastrointestinal digestion

Immobilization of trypsin on chitosan gels: Use of different activation protocols and comparison with other supports

Extraction, Purification and Characterization of Fish Chymotrypsin: A Review

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