A Novel Glucose Isomerase from Caldicellulosiruptor bescii with Great Potentials in the Production of High-Fructose Corn Syrup

A Novel Glucose Isomerase from Caldicellulosiruptor bescii with Great Potentials in the Production of High-Fructose Corn Syrup
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来自贝斯卡迪纤维素酶的新型葡萄糖异构酶在高果糖玉米糖浆生产中具有巨大潜力

DOI:
10.1155/2020/1871934
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发表时间:
2020-04-14
影响因子:
--
通讯作者:
Xu, Bo
Xu, Bo
中科院分区:
生物学3区
文献类型:
--
作者:
Dai, Chenxia;Miao, Tingting;Xu, Bo

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葡萄糖异构酶(glucose isomerase,GI)催化D-葡萄糖转化为D-果糖,是生产高果糖玉米糖浆(high-fructose corn syrup,HFCS)的重要工业酶。在这项研究中,一个新的GI(CbGI)的克隆从热纤维素酶,并在大肠杆菌中表达。纯化的重组CbGI(rCbGI)显示中性和嗜热性质。该酶在pH7.0和80°C下具有最佳活性,在85°C下保持稳定。与其他报道的GI相比,rCbGI表现出更高的底物亲和力(Km = 42.61 mM)和更高的转化效率(以3 M D-葡萄糖为底物时高达57.3%)。该CbGI的高催化效率和亲和力对于HFCS的成本有效的生产非常有价值。
Glucose isomerase (GI) that catalyzes the conversion of D-glucose to D-fructose is one of the most important industrial enzymes for the production of high-fructose corn syrup (HFCS). In this study, a novel GI (CbGI) was cloned from Caldicellulosiruptor bescii and expressed in Escherichia coli. The purified recombinant CbGI (rCbGI) showed neutral and thermophilic properties. It had optimal activities at pH 7.0 and 80°C and retained stability at 85°C. In comparison with other reported GIs, rCbGI exhibited higher substrate affinity (Km = 42.61 mM) and greater conversion efficiency (up to 57.3% with 3M D-glucose as the substrate). The high catalytic efficiency and affinity of this CbGI is much valuable for the cost-effective production of HFCS.