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细菌纤维素固定化酶的制备及其水解拆分性能

Preparation and Its Hydrolysis Resolution Properties of Nanofiber D-Lacs@BC-NH_(2)
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摘要 经D-泛解酸内酯酶(D-Lacs)催化水解拆分是制备医药中间体D-泛解酸的绿色催化新技术,但游离酶存在价格昂贵、易失活、难分离等问题。利用椰果源细菌纤维素(BC)的三维纳米纤维网络为支架,以二乙烯三胺将其改性成BC-NH2,吸附纳米酶后,以戊二醛稳定D-泛解酸内酯水解酶固定于BC网络中。结果表明,氨基化修饰改性提高了BC固定化酶的活性,BC-NH2固定化D-Lacs的酶固载量高达372.5 mg/g,约4.5 h即可完成D,L-泛解酸内酯的水解拆分,均高于未改性BC。经过10次回收循环水解拆分实验,均可保证每批次2 h即可达到一半水解率,是一种有前景的全生物基酶固定化技术。 D-Lactonohydrolase(D-Lacs)catalyzed hydrolysis and resolution is a new green catalytic technology for the preparation of pharmaceutical intermediate D-Lacs.However,free enzymes have problems such as high cost,easy deactivation,and difficulty in separation.This article uses a three-dimensional nanofiber network of coconut derived bacterial cellulose(BC)as a scaffold,modified with diethylenetriamine to BC-NH_(2),adsorbed with nanoenzymes,and immobilized with glutaraldehyde stabilized D-Lactonohydrolase in the BC network.The results showed that the amination modification improved the activity of BC immobilized enzyme.The enzyme load of BC-NH_(2)immobilized D-Lacs was up to 372.5 mg/g,and the hydrolysis and resolution of DL-pantolactone could be completed in about 4.5 hours,which were higher than unmodified BC.After 10 cycles of recycling,hydrolysis and separation experiments,it can be ensured that each batch reaches half of the hydrolysis rate within 2 hours,it has been proven to have good cycling stability and is a promising technology for immobilization of all bio-based enzymes.
作者 元佳丽 周晓悦 向忠润 王慧庆 YUAN Jia-li;ZHOU Xiao-yue;XIANG Zhong-run;WANG Hui-qing(School of Chemistry and Chemical Engineering,Hefei University of Technology,Hefei 230009,China)
出处 《安徽化工》 CAS 2024年第3期49-53,共5页 Anhui Chemical Industry
基金 安徽省重点研究与开发计划“VB5内酯酶绿色稳定高效固载关键技术研究及应用”(2022a05020059)。
关键词 D-泛解酸内酯水解酶 细菌纤维素 酶固定化 水解 D-Lactonohydrolase bacterial cellulose immobilization hydrolysis
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