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

Yuxi Deng, Harry Gruppen, Peter A. Wierenga*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

9 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

Keywords

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

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