首页> 外文期刊>RSC Advances >Biochemical characterization and biocatalytic application of a novel d-tagatose 3-epimerase from Sinorhizobium sp.
【24h】

Biochemical characterization and biocatalytic application of a novel d-tagatose 3-epimerase from Sinorhizobium sp.

机译:SINORHIZOBIUM SP的新型D-Tagatose 3-eBimerase的生物化学表征及生物催化应用。

获取原文
获取原文并翻译 | 示例
           

摘要

Sinorhizobium sp. D-tagatose 3-epimerase (sDTE) catalyzes the conversion of D-tagatose to D-sorbose. It also recognizes D-fructose as a substrate for D-allulose production. The optimal temperature and pH of the purified sDTE was 50 degrees C and 8.0, respectively. Based on the sDTE homologous model, Glu154, Asp187, Gln213, and Glu248, form a hydrogen bond network with the active-site Mn2+ and constitute the catalytic tetrad. The amino acid residues around O-1, -2, and -3 atoms of the substrates (D-tagatose/D-fructose) are strictly conserved and thus likely regulate the catalytic reaction. However, the residues at O-4, -5, and -6, being responsible for the substrate-binding, are different. In particular, Arg65 and Met9 were found to form a unique interaction with O-4 of D-fructose and D-tagatose. The whole cells with recombinant sDTE showed a higher bioconversion rate of 42.5% in a fed-batch bioconversion using D-fructose as a substrate, corresponding to a production of 476 g L-1 D-allulose. These results suggest that sDTE is a potential industrial biocatalyst for the production of D-allulose in fed-batch mode.
机译:Sinorhizobium sp。 D-Tagatose 3-eBimerase(SDTE)催化D-Tagatose至D-山梨糖的转化。它还识别D-果糖作为D-甲型制备的基材。纯化的SDTE的最佳温度和pH分别为50℃和8.0。基于SDTE同源模型,GLU154,ASP187,GLN213和GLU248,形成具有有源部位MN2 +的氢键网络,并构成催化Tetrad。邻接O-1,-2和-3原子的氨基酸残基严格保守,因此可能调节催化反应。然而,O-4,-5和-6的残基对底物结合负责是不同的。特别地,发现Arg65和Met9形成与D-果糖和D-塔肽的O-4的独特相互作用。具有重组SDTE的整个细胞使用D-果糖作为基材的FED-批量生物转化率较高的生物转化率为42.5%,对应于476g L-1 D-甲壳的产生。这些结果表明,SDTE是潜在的工业生物催化剂,用于在氟批模式下生产D-甲型。

著录项

  • 来源
    《RSC Advances》 |2019年第6期|共9页
  • 作者单位

    Tianjin Univ Sci &

    Technol Key Lab Ind Fermentat Microbiol Tianjin Key Lab Ind Microbiol Minist Educ Coll Biotechnol Natl Engn Lab Ind Enz Tianjin 300457 Peoples R China;

    Tianjin Univ Sci &

    Technol Key Lab Ind Fermentat Microbiol Tianjin Key Lab Ind Microbiol Minist Educ Coll Biotechnol Natl Engn Lab Ind Enz Tianjin 300457 Peoples R China;

    Tianjin Univ Sci &

    Technol Key Lab Ind Fermentat Microbiol Tianjin Key Lab Ind Microbiol Minist Educ Coll Biotechnol Natl Engn Lab Ind Enz Tianjin 300457 Peoples R China;

    Tianjin Univ Sci &

    Technol Key Lab Ind Fermentat Microbiol Tianjin Key Lab Ind Microbiol Minist Educ Coll Biotechnol Natl Engn Lab Ind Enz Tianjin 300457 Peoples R China;

    Tianjin Univ Sci &

    Technol Key Lab Ind Fermentat Microbiol Tianjin Key Lab Ind Microbiol Minist Educ Coll Biotechnol Natl Engn Lab Ind Enz Tianjin 300457 Peoples R China;

    Tianjin Univ Sci &

    Technol Key Lab Ind Fermentat Microbiol Tianjin Key Lab Ind Microbiol Minist Educ Coll Biotechnol Natl Engn Lab Ind Enz Tianjin 300457 Peoples R China;

    Tianjin Univ Sci &

    Technol Key Lab Ind Fermentat Microbiol Tianjin Key Lab Ind Microbiol Minist Educ Coll Biotechnol Natl Engn Lab Ind Enz Tianjin 300457 Peoples R China;

    Tianjin Univ Sci &

    Technol Key Lab Ind Fermentat Microbiol Tianjin Key Lab Ind Microbiol Minist Educ Coll Biotechnol Natl Engn Lab Ind Enz Tianjin 300457 Peoples R China;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;
  • 关键词

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号