title: Synergistic action of an X-prolyl dipeptidyl aminopeptidase and a non-specific aminopeptidase in protein hydrolysis.
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.
authors: Novozymes Biotech, Incorporated, 1445 Drew Avenue, Davis, California 95616, USA.
authors: T
authors: T
authors: Byun
authors: L
authors: L
authors: Kofod
authors: A
authors: A
authors: Blinkovsky
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases / Q000378:metabolism*; D001236:Aspergillus oryzae / Q000201:enzymology; D002364:Caseins / Q000378:metabolism; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000378:metabolism*; D004357:Drug Synergism; D005983:Glutens / Q000378:metabolism; D006868:Hydrolysis; D010455:Peptides / Q000378:metabolism*; D030262:Soybean Proteins / Q000378:metabolism
chemical_list: D000596:Amino Acids; D002364:Caseins; D010455:Peptides; D030262:Soybean Proteins; D005983:Glutens; D000626:Aminopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases