Lectin Agglutinated Multienzyme Catalyst with Enhanced Substrate Affinity and Activity

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• 作者：Yifei Zhang ; You Yong ; Jun Ge ; Zheng Liu
• 刊名：ACS Catalysis
• 出版年：2016
• 出版时间：June 3, 2016
• 年：2016
• 卷：6
• 期：6
• 页码：3789-3795
• 全文大小：468K
• 年卷期：0
• ISSN：2155-5435

文摘

A method based on biological recognition was proposed to prepare cross-linked multiple glycoenzyme aggregates. With Concanavalin A (ConA) as a molecular glue, horseradish peroxidase (HRP) and glucose oxidase (GOx) were agglutinated and then cross-linked by glutaraldehyde, forming a GOx-ConA-HRP catalyst. The affinity of ConA to glucose enhanced the uptake of the substrate, reducing the K_m of cross-linked GOx-ConA-HRP aggregates for glucose from 51 mM to 8.8 mM. The colocalization and clustering of cascade enzymes at nanoscale facilitated the intermediate consumption. These effects significantly improved the catalytic performance of the GOx-HRP cascade with a 1.5-fold increased specificity constant. The use of ConA as a molecular glue provides a facile way to construct a multienzyme catalyst with enhanced stability and activity.