| Literature DB >> 28285356 |
Li-Qun Jin1,2, Qi Xu1,2, Zhi-Qiang Liu1,2, Dong-Xu Jia1,2, Cheng-Jun Liao3, De-Shui Chen3, Yu-Guo Zheng4,5.
Abstract
Glucose isomerase is the important enzyme for the production of high fructose corn syrup (HFCS). One-step production of HFCS containing more than 55% fructose (HFCS-55) is receiving much attention for its industrial applications. In this work, the Escherichia coli harboring glucose isomerase mutant TEGI-W139F/V186T was immobilized for efficient production of HFCS-55. The immobilization conditions were optimized, and the maximum enzyme activity recovery of 92% was obtained. The immobilized glucose isomerase showed higher pH, temperature, and operational stabilities with a K m value of 272 mM and maximum reaction rate of 23.8 mM min-1. The fructose concentration still retained above 55% after the immobilized glucose isomerase was reused for 10 cycles, and more than 85% of its initial activity was reserved even after 15 recycles of usage at temperature of 90 °C. The results highlighted the immobilized glucose isomerase as a potential biocatalyst for HFCS-55 production.Entities:
Keywords: Activity; Fructose; Glucose isomerase; Immobilization; Stability
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Year: 2017 PMID: 28285356 DOI: 10.1007/s12010-017-2445-0
Source DB: PubMed Journal: Appl Biochem Biotechnol ISSN: 0273-2289 Impact factor: 2.926