基质(水族馆)
葡萄糖-6-磷酸异构酶
酶
异构酶
化学
动力学
固定化酶
底物特异性
生物化学
组合化学
生物
生态学
量子力学
物理
作者
Kuo‐Cheng Chen,Juan‐Yih Wu
标识
DOI:10.1002/bit.260300703
摘要
Abstract Using commercial immobilized glucose isomerase (SWETASE®, Nagase Co.), the effect of substrate protection on enzyme deactivation has been studied in a batch manner. The data analysis was carried out based on Briggs‐Haldane kinetics in which enzyme deactivation accompanying the protection of substrates was also considered. The protection factor was proposed to elucidate the dependence of the degree of substrate protection. The existence of the protection of glucose isomerase by the substrates has been verified experimentally. Also, the enzyme‐substrate complex deactivates with a decay constant which is one‐half that of the free enzyme. Theoretical analysis of enzyme deactivation with substrate protection offers an effective understanding which is essential for enzyme replacement and process optimization.
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