Comparison of Protein Hydrolysis Catalyzed by Bovine, Porcine, and Human Trypsins

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3 Citations (Scopus)

Abstract

Based on trypsin specificity (for lysines and arginines), trypsins from different sources are expected to hydrolyze a given protein to the same theoretical maximum degree of hydrolysis (DHmax,theo). This is in contrast with experiments. Using α-lactalbumin and β-casein, this study aims to reveal if the differences among experimental DHmax (DHmax,exp) by bovine, porcine, and human trypsins are due to their secondary specificity. Peptide analysis showed that ∼78% of all the cleavage sites were efficiently hydrolyzed by porcine trypsin, and ∼47 and ∼53% were efficiently hydrolyzed by bovine and human trypsins, respectively. These differences were explained by the enzyme secondary specificity, that is, their sensitivities to the amino acids around the cleavage sites. The DHmax predictions based on the secondary specificity were 4 times closer to the DHmax,exp than the predictions based on trypsin specificity alone (DHmax,theo). Proposed preliminary relations between binding sites and trypsin secondary specificity allow DHmax,exp estimations of tryptic hydrolysis of other proteins.
Original languageEnglish
Pages (from-to)4219-4232
JournalJournal of Agricultural and Food Chemistry
Volume66
Issue number16
DOIs
Publication statusPublished - 25 Apr 2018

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Trypsin
trypsin
Hydrolysis
Swine
hydrolysis
swine
cattle
Proteins
proteins
Lactalbumin
prediction
lactalbumin
Caseins
Lysine
arginine
Arginine
binding sites
casein
lysine
Binding Sites

Keywords

  • LC-MS
  • peptide release kinetics
  • protein digestibility
  • secondary specificity
  • tryptic hydrolysis

Cite this

@article{39f7d2ae61e541f8bb96c889d0ffc8fd,
title = "Comparison of Protein Hydrolysis Catalyzed by Bovine, Porcine, and Human Trypsins",
abstract = "Based on trypsin specificity (for lysines and arginines), trypsins from different sources are expected to hydrolyze a given protein to the same theoretical maximum degree of hydrolysis (DHmax,theo). This is in contrast with experiments. Using α-lactalbumin and β-casein, this study aims to reveal if the differences among experimental DHmax (DHmax,exp) by bovine, porcine, and human trypsins are due to their secondary specificity. Peptide analysis showed that ∼78{\%} of all the cleavage sites were efficiently hydrolyzed by porcine trypsin, and ∼47 and ∼53{\%} were efficiently hydrolyzed by bovine and human trypsins, respectively. These differences were explained by the enzyme secondary specificity, that is, their sensitivities to the amino acids around the cleavage sites. The DHmax predictions based on the secondary specificity were 4 times closer to the DHmax,exp than the predictions based on trypsin specificity alone (DHmax,theo). Proposed preliminary relations between binding sites and trypsin secondary specificity allow DHmax,exp estimations of tryptic hydrolysis of other proteins.",
keywords = "LC-MS, peptide release kinetics, protein digestibility, secondary specificity, tryptic hydrolysis",
author = "Yuxi Deng and Harry Gruppen and Wierenga, {Peter A.}",
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language = "English",
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Comparison of Protein Hydrolysis Catalyzed by Bovine, Porcine, and Human Trypsins. / Deng, Yuxi; Gruppen, Harry; Wierenga, Peter A.

In: Journal of Agricultural and Food Chemistry, Vol. 66, No. 16, 25.04.2018, p. 4219-4232.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Comparison of Protein Hydrolysis Catalyzed by Bovine, Porcine, and Human Trypsins

AU - Deng, Yuxi

AU - Gruppen, Harry

AU - Wierenga, Peter A.

PY - 2018/4/25

Y1 - 2018/4/25

N2 - Based on trypsin specificity (for lysines and arginines), trypsins from different sources are expected to hydrolyze a given protein to the same theoretical maximum degree of hydrolysis (DHmax,theo). This is in contrast with experiments. Using α-lactalbumin and β-casein, this study aims to reveal if the differences among experimental DHmax (DHmax,exp) by bovine, porcine, and human trypsins are due to their secondary specificity. Peptide analysis showed that ∼78% of all the cleavage sites were efficiently hydrolyzed by porcine trypsin, and ∼47 and ∼53% were efficiently hydrolyzed by bovine and human trypsins, respectively. These differences were explained by the enzyme secondary specificity, that is, their sensitivities to the amino acids around the cleavage sites. The DHmax predictions based on the secondary specificity were 4 times closer to the DHmax,exp than the predictions based on trypsin specificity alone (DHmax,theo). Proposed preliminary relations between binding sites and trypsin secondary specificity allow DHmax,exp estimations of tryptic hydrolysis of other proteins.

AB - Based on trypsin specificity (for lysines and arginines), trypsins from different sources are expected to hydrolyze a given protein to the same theoretical maximum degree of hydrolysis (DHmax,theo). This is in contrast with experiments. Using α-lactalbumin and β-casein, this study aims to reveal if the differences among experimental DHmax (DHmax,exp) by bovine, porcine, and human trypsins are due to their secondary specificity. Peptide analysis showed that ∼78% of all the cleavage sites were efficiently hydrolyzed by porcine trypsin, and ∼47 and ∼53% were efficiently hydrolyzed by bovine and human trypsins, respectively. These differences were explained by the enzyme secondary specificity, that is, their sensitivities to the amino acids around the cleavage sites. The DHmax predictions based on the secondary specificity were 4 times closer to the DHmax,exp than the predictions based on trypsin specificity alone (DHmax,theo). Proposed preliminary relations between binding sites and trypsin secondary specificity allow DHmax,exp estimations of tryptic hydrolysis of other proteins.

KW - LC-MS

KW - peptide release kinetics

KW - protein digestibility

KW - secondary specificity

KW - tryptic hydrolysis

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