Synergistic action of an X-prolyl dipeptidyl aminopeptidase and a non-specific aminopeptidase in protein hydrolysis

J Agric Food Chem. 2001 Apr;49(4):2061-3. doi: 10.1021/jf001091m.

Abstract

Non-specific monoaminopeptidase (AP; E.C. 3.4.11) and X-prolyl dipeptidyl aminopeptidase (X-PDAP; E.C. 3.4.14.5), both from Aspergillus oryzae, demonstrate strong synergism in hydrolyzing proline-containing peptides. Incubation of AP alone with the peptide Ala-Pro-Gly-Asp-Arg-Ile-Tyr-Val-His-Pro-Phe does not generate free amino acids. However, when AP and X-PDAP are added in combination, complete and immediate hydrolysis of all peptide bonds, other than X-Pro bonds, is observed. In the enzymatic hydrolysis of casein, soy, and gluten, degree of hydrolysis (DH) values of 54, 54, and 47% were achieved, respectively, when subtilisin (E.C. 3.4.21.62) was supplemented with AP. Addition of a third enzyme, X-PDAP, resulted in significantly higher DH values of 69, 72, and 64%, respectively, establishing the utility of this synergism in protein hydrolysis.

MeSH terms

  • Amino Acids / analysis
  • Aminopeptidases / metabolism*
  • Aspergillus oryzae / enzymology
  • Caseins / metabolism
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / metabolism*
  • Drug Synergism
  • Glutens / metabolism
  • Hydrolysis
  • Peptides / metabolism*
  • Soybean Proteins / metabolism

Substances

  • Amino Acids
  • Caseins
  • Peptides
  • Soybean Proteins
  • Glutens
  • Aminopeptidases
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases