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 (DH_max,theo). This is in contrast with experiments. Using α-lactalbumin and β-casein, this study aims to reveal if the differences among experimental DH_max (DH_max,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

SUBMITTER: Deng Y 

PROVIDER: S-EPMC5920921 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature