Preparation and investigation of novel endopeptidase-exopeptidase co-immobilized nanoflowers with improved cascade hydrolysis

文献类型： 外文期刊

第一作者： Zhu, Hao

作者： Zhu, Hao;Chen, Jinhang;Zhang, Yi;Wan, Chuyun;Zheng, Mingming;Zhu, Hao;Zheng, Dongyun;Goh, Kheng-Lim;Zhang, Yi;Zheng, Mingming

作者机构：

关键词： Hybrid nanoflowers; Protease immobilization; Catalytic stability; Reusability; Cascade reaction

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）

ISSN： 0141-8130

年卷期： 2023 年 246 卷

页码：

收录情况： SCI

摘要： 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 K-m, V-max and K-cat/K-m 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.

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