串扰
酶
化学
竞赛(生物学)
生物物理学
生物化学
纳米技术
生物
生态学
材料科学
工程类
电子工程
作者
Ahlem Meziadi,Victoria Bloquert,Andrea A. Greschner,Hendrick W. de Haan,Marc A. Gauthier
出处
期刊:Biomacromolecules
[American Chemical Society]
日期:2024-08-16
卷期号:25 (9): 6072-6081
标识
DOI:10.1021/acs.biomac.4c00727
摘要
In nature, enzymatic pathways often involve compartmentalization effects that can modify the intrinsic activity and specificity of the different enzymes involved. Consequently, extensive research has focused on replicating and studying the compartmentalization effects on individual enzymes and on multistep enzyme "cascade" reactions. This study explores the influence of compartmentalization achieved using molecular crowding on the glucose oxidase/horseradish peroxidase (GOx/HRP) cascade reaction. The crowder tested is methoxy poly(ethylene glycol) (mPEG) that can, depending on conditions, promote GOx and HRP coassociation at the nanoscale and extend their contact time. Low-molecular-weight mPEG (0.35 kDa), but not mPEG of higher molecular weights (5 or 20 kDa), significantly enhanced the cascade reaction where up to a 20-fold increase in the rate of the cascade reaction was observed under some conditions. The combined analyses emphasize the particularity of low-molecular-weight mPEG and point toward mPEG-induced coassociation of HRP and GOx, producing nearest crowded neighbor effects of HRP on GOx, and
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