果糖
葡萄糖-6-磷酸异构酶
化学
生物催化
基质(水族馆)
异构酶
异构化
固定化酶
催化作用
高果糖玉米糖浆
有机化学
酶
生物化学
色谱法
反应机理
生物
生态学
作者
Xinnan Ma,Wenrui Huang,Yongqing Song,Juan Han,Jiacong Wu,Lei Wang,Yun Wang
标识
DOI:10.1021/acs.jafc.2c05667
摘要
The development of a suitable immobilization strategy to improve the performance of immobilized glucose isomerase for the isomerization of glucose to fructose is crucial to promoting the industrial production of high-fructose syrup. In this work, a novel recyclable upper critical solution temperature (UCST)-type mVBA-b-P(AAm-co-AN)@glucose isomerase biocatalyst (PVAA@GI) was prepared, and the immobilized glucose isomerase could capture the glucose substrate through the affinity of 4-vinylbenzeneboronic acid (4-VBA) and the glucose substrate, which led to the enhanced substrate affinity and catalytic efficiency of the PVAA@GI. The biocatalyst exhibited excellent stability in pH, thermal, storage, and recycling compared to the free enzyme. The mVBA-b-P(AAm-co-AN)@glucose isomerase biocatalyst displayed reversibly soluble-insoluble characteristics with temperature change, which was in the soluble state during the enzyme reaction process but could be recovered in an insoluble form by lowering the temperature after the reaction. The highest fructose production rate reached 62.79%, which would have potential application in the industrial production of high-fructose syrup.
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