首页> 外文期刊>Applied biochemistry and biotechnology, Part A. enzyme engineering and biotechnology >Simultaneous enzymatic synthesis of gluconic acid and sorbitol - Production, purification, and application of glucose-fructose oxidoreductase and gluconolactonase
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Simultaneous enzymatic synthesis of gluconic acid and sorbitol - Production, purification, and application of glucose-fructose oxidoreductase and gluconolactonase

机译:葡萄糖酸和山梨醇的同时酶促合成-葡萄糖-果糖氧化还原酶和葡萄糖酸内酯酶的生产,纯化和应用

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摘要

With regard to the enzymatic synthesis of sorbitol and gluconic acid, a screening was carried out to identify promising producers of glucose-fructose oxidoreductase (GFOR) and gluconolactonase (GL). Zymomonas mobilis DSM 473 and Rhodotorula rubra DSM 70403 have been selected for the synthesis of GFOR and GL, respectively. Maximal enzyme production by these organisms has been achieved at D-glucose concentrations of 200 and 150 g/L, respectively. Both GFOR and GL were purified and characterized with respect to some of their catalytic properties. GL showed strict specificity for 1,5-(delta)-lactones and was activated by Mg2+ and Mn2+ ions. The potential use of soluble GFOR is limited by its inactivation during substrate conversion, and the effects of reaction temperature and pH on the ''catalytic'' stability of GFOR were evaluated. Exogenous adddition of auxiliary GL had no effect on oxidoreductase stability and did not improve productivities.
机译:关于山梨糖醇和葡萄糖酸的酶促合成,进行了筛选以鉴定有希望的葡萄糖-果糖氧化还原酶(GFOR)和葡糖酸内酯酶(GL)的生产者。分别选择了运动发酵单胞菌DSM 473和红红假单胞菌DSM 70403来合成GFOR和GL。这些生物分别在200和150 g / L的D-葡萄糖浓度下实现了最大的酶生产。 GFOR和GL均经过纯化,并就其某些催化性能进行了表征。 GL对1,5-δ-内酯显示出严格的特异性,并被Mg2 +和Mn2 +离子激活。可溶性GFOR的潜在用途受到其在底物转化过程中失活的限制,并且评估了反应温度和pH对GFOR的“催化”稳定性的影响。外源添加辅助GL对氧化还原酶的稳定性没有影响,也没有提高生产率。

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