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Lookup NU author(s): Dr Kheng-Lim GohORCiD
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© 2023 Elsevier B.V.Enzymatic hydrolysis is a promising approach for protein and food processing. However, the efficiency of this approach is constrained by the self-hydrolysis, self-agglomeration of free enzymes and the limited applicability resulted from enzymes' selectivityt. Here, novel organic-inorganic hybrid nanoflowers (AY-10@AXH-HNFs) were prepared by coordinating Cu2+ with both endopeptidase of PROTIN SD-AY10 and exopeptidase of Prote AXH. The results indicate that the AY-10@AXH-HNFs exhibited 4.1 and 9.6 times higher catalytic activity than free Prote AXH and PROTIN SD-AY10, respectively, for the enzymatic hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE). The kinetic parameters of Km, Vmax and Kcat/Km by AY-10@AXH-HNFs were determined to be 0.6 mg/mL, 6.8 mL·min/mg and 6.1 mL/(min·mg), respectively, surpassing the values obtained from free endopeptidase and exopeptidase. Furthermore, the ability of AY-10@AXH-HNFs to retain 41 % of their initial catalytic activity after undergoing 5 cycles of repeated use confirmed their stability and reusability. This study introduces a novel approach of co-immobilizing endopeptidase and exopeptidase on nanoflowers, resulting in significantly enhanced stability and reusability of the protease in catalytic applications.
Author(s): Zhu H, Chen J, Zhang Y, Goh K-L, Wan C, Zheng D, Zheng M
Publication type: Article
Publication status: Published
Journal: International Journal of Biological Macromolecules
Print publication date: 15/08/2023
Online publication date: 29/06/2023
Acceptance date: 28/06/2023
ISSN (print): 0141-8130
ISSN (electronic): 1879-0003
Publisher: Elsevier B.V.
PubMed id: 37392925
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