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Clostridium bolteae ATCC BAA-613 D-塔格糖3-差向异构酶的诱导表达、纯化及活性研究 被引量：2

Study on expression,purification and enzyme activity of Clostridium bolteae ATCC BAA-613 D-tagatose 3-epimerase
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摘要 D-塔格糖3-差向异构酶是生物法生产新型功能性因子D-阿洛酮糖最为有效的酶。一种新型的能够编码D-塔格糖3-差向异构酶的基因CLOBOL_00069被克隆,它来源于Clostridium bolteae ATCC BAA-613。以pUC57为克隆载体,以pET-22b(+)为载体质粒,E.coli BL21(DE3)为宿主细胞,构建了基因重组工程菌。IPTG诱导剂诱导目的蛋白的表达;通过镍柱亲和层析,杂蛋白与目的蛋白得到了很好的分离。对纯化的重组蛋白样品进行SDS-PAGE分析,在约32ku处出现明显的特征条带。通过活性研究表明,Clostridium bolteae ATCC BAA-613 DTEase属于DTEase家族,并具有较高的生物转化率,反应10h后转化率达到20%。 D-tagatose 3-epimerase is the most effective enzyme for the biological production of D-psicose from D-fructose,a novel functional factor.Gene CLOBOL_00069 encoding the D-tagatose 3-epimerase from Clostridium bolteae ATCC BAA-613 was cloned and expressed in Escherichia coli.E.coli BL21（DE3）were host cells with pUC57 as cloning vector and pET-22b（＋）as plasmid to construct recombinant strains.The bacterium was induced by IPTG;then the recombinant DTEase was purified to electrophoretical homogeneity with affinity chromatography.The recombinant DTEase was analyzed by SDS-PAGE,and approximately 32ku exogenous protein was observed on the SDS-PAGE.The activity of recombinant DTEase was also studied,indicating that Clostridium bolteae ATCC BAA-613 DTEase belonged to DTEase family enzymes and had a high rate of biological transformation.The conversion reached 20% after 10h reaction.
作者 储菲菲 沐万孟 邢庆超 周榴明 张涛 江波
机构地区 江南大学食品科学与技术国家重点实验室 罗盖特美国公司
出处 《食品工业科技》 CAS CSCD 北大核心 2012年第7期198-201,392,共5页 Science and Technology of Food Industry
基金 国家自然基金项目(20906040) 中央高校基本科研业务费专项资金(JUSRP31002) 江苏省社会发展科技支撑项目(BE2010626)
关键词 D-塔格糖3-差向异构酶 D-阿洛酮糖 基因重组 亲和层析 D-tagatose 3-epimerase D-psicose gene recombinant affinity chromatography
分类号 Q786 [生物学—分子生物学]
  • 相关文献

参考文献14

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二级参考文献11

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  • 2Matsuo T, Suzuki H, Hashiguchi M, et al. D-Psicose is a rare sugar that provides no energy to growing rats[J]. J Nutr Sci Vitaminol, 2002, 48(1) :77-80.
  • 3Matsuo T, Baba Y, Hashiguchi M, et al. Dietary D-psicose, a C 3 epimer of Dfructose, suppresses the activity of hepatic lipogenic enzymes in rats[J]. Asia Pac J Clin Nutr, 2001, 10(3) ..233-237.
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  • 5Izumori K, Khan A R, Okaya H, et al. A new enzyme, D-ketohexose 3-epimerase, from Pseudornonas sp. ST-24 [J]. Biosci Biotechnol Biochem, 1993, 57 : 1037- 1039.
  • 6Itoh H, Okaya H, Khan A R, et al. Purification and characterization of D-tagatose 3-epimerase from Pseudornonas sp. ST-24 [J]. Biosci Biotechnol Biochem, 1994, 58..2168-2171.
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共引文献153

同被引文献32

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  • 10Wanmeng Mu, Feifei Chu, Qiangchao Xing, et al. Cloning, expression,and characterization of a D-psicose 3-epimerase from Clostridium cellulolyticum H10 [ J ]. Journal of Agriculture and Food Chemistry,2011,59(14) :7785-7792.

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二级引证文献16

食品工业科技
2012年 第7期

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