Byun T, Kofod L, Blinkovsky A
Novozymes Biotech, Incorporated, 1445 Drew Avenue, Davis, California 95616, USA.
J Agric Food Chem. 2001 Apr;49(4):2061-3. doi: 10.1021/jf001091m.
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.
来自米曲霉的非特异性单胺肽酶（AP；酶委员会编号3.4.11）和X-脯氨酰二肽基氨基肽酶（X-PDAP；酶委员会编号3.4.14.5）在水解含脯氨酸的肽时表现出强烈的协同作用。单独将AP与肽Ala-Pro-Gly-Asp-Arg-Ile-Tyr-Val-His-Pro-Phe一起孵育不会产生游离氨基酸。然而，当将AP和X-PDAP组合添加时，除X-脯氨酸键外，所有肽键都能立即完全水解。在酪蛋白、大豆和麸质的酶促水解中，当枯草杆菌蛋白酶（酶委员会编号3.4.21.62）与AP一起使用时，水解度（DH）值分别达到54%、54%和47%。添加第三种酶X-PDAP后，DH值分别显著提高到69%、72%和64%，这证明了这种协同作用在蛋白质水解中的实用性。
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