期刊
ACS CATALYSIS
卷 6, 期 6, 页码 3789-3795出版社
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.6b01047
关键词
multienzyme systems; Concanavalin A; glycoenzyme aggregates; substrate affinity; enhanced activity
资金
- National Natural Science Foundation of China [21036003]
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.
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