D-来苏糖异构酶的酶学性质研究

Characterization of Recombinant D-Lyxose Isomerase

DOI：10.3969/j.issn.1673-1689.2019.01.013

中文关键词: D-甘露糖 D-来苏糖异构酶 生物制备

英文关键词: D-mannose,D-lyxose isomerase,biological production

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中文摘要:

为探索D-甘露糖的高效酶法合成途径，作者克隆了来源于Peptococcaceae bacterium1109的D-来苏糖异构酶基因，将其导入到E. coliBL21（DE3）中进行表达。该酶的最适底物为D-来苏糖，并可以高效催化D-果糖与D-甘露糖之间的差向异构反应。以D-果糖为底物时，重组表达的D-来苏糖异构酶的比酶活可达2.5 U/mg，该酶的最适pH为7.5，最适温度为70 ℃，Co2+可以显著提高该酶的活力。在最适条件下以500 g/L的果糖为底物，反应8 h达到平衡，平衡转化率达19.17%，生产D-甘露糖95.85 g/L。

英文摘要:

In this study，the D-lyxose isomerase gene derived fromPeptococcaceae bacterium1109 was cloned and introduced intoE. coliBL21（DE3） for expression. The optimal substrate for the recombinant D-LI is D-lyxose，and it can efficiently catalyze the epimerization reaction between D-fructose and D-mannose. The specific activity of recombinantly expressed D-lysose isomerase can reach 2.544 U/mg when used D-fructose as substrate. It displayed maximal activity in presence of 1 mM Co2+ at pH 7.0 and 70 ℃. Under optimum conditions，95.85 g/L D-mannose was produced from 500 g/L D-fructose after reaction for 5 h，giving a conversion yield of 19.17%.

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