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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >A novel thermostable and efficient Class II glucose isomerase from the thermophilic Caldicoprobacter algeriensis: Biochemical characterization, molecular investigation, and application in High Fructose Syrup production
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A novel thermostable and efficient Class II glucose isomerase from the thermophilic Caldicoprobacter algeriensis: Biochemical characterization, molecular investigation, and application in High Fructose Syrup production

机译：一种新的热稳定和有效的II类葡萄糖异构酶，来自嗜热钙霉菌阿尔及利氏菌：生物化学表征，分子调查和高果糖糖浆生产中的应用

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摘要

A novel glucose isomerase gene from the thermophilic Caldicoprobacter algeriensis, encoding a polypeptide of 438 residues, was identified, cloned and successfully expressed in E. coli. The purified enzyme (GICA) was a homotetramer of about 200 kDa displaying the highest activity at pH 7.0 and 90 degrees C and retaining 97% of its maximum activity at pH 6.5. The enzyme showed an excellent thermostability with a half-life of 6 min at 100 degrees C. Interestingly, GICA had a very high affinity of 40 mM and catalytic efficiency of 194 min(-1) mM(-1) toward D-glucose at 90 degrees C. A maximum of 54.7% D-glucose to D-fructose conversion was achieved by GICA at 85 degrees C making it an attractive candidate for HFCS-55 production. The primary sequence inspection and molecular modeling studies revealed that the thermal stability of GICA could be attributed to the presence of extra charged residues at the surface like E108 and Q408 increasing surface charge interactions. Moreover, a serine at position 56 near to P58 could establish hydrogen bond strengthening the dimer attachment. The high catalytic efficiency and affinity of GICA could be ascribed to the presence of amino add like E108 and K62 that created more charges around the catalytic site entry. (C) 2019 Elsevier B.V. All rights reserved.
机译：鉴定，在大肠杆菌中鉴定了来自嗜热钙霉菌的嗜热性钙霉菌杆菌的新葡萄糖异构酶基因，编码438个残基的多肽。纯化的酶（GICA）是大约200kDa的同源体，在pH 7.0和90℃下显示最高活性，并在pH6.5下保留其最大活性的97％。酶显示出优异的热稳定性，在100摄氏度下半衰期为6分钟。有趣的是，GICA在D-葡萄糖的194 min（-1）mm（-1）中具有40mm和催化效率的非常高的亲和力在85℃下，GICA在85摄氏度下，最大为54.7％的D-果糖转化率为D-果糖转化，使其成为HFCS-55生产的有吸引力的候选者。主要序列检测和分子建模研究表明，GICA的热稳定性可归因于在E108和Q408的表面上存在额外的带电残基，增加表面电荷相互作用。此外，靠近P58的位置56处的丝氨酸可以建立强化二聚体附着的氢键。 GICA的高催化效率和亲和力可以归因于氨基的存在，如E108和K62，在催化位点围绕催化位点产生更多的电荷。 （c）2019 Elsevier B.v.保留所有权利。

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