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从嗜热栖热菌中纯化和鉴定一种对甘油具有特殊专一性的醇脱氢酶。

Purification and characterization of an alcohol dehydrogenase with an unusual specificity towards glycerol from Thermus thermophilus.

机构信息

Chemistry Department, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110 016, India.

出版信息

Bioresour Technol. 2010 Apr;101(7):2554-7. doi: 10.1016/j.biortech.2009.10.063. Epub 2009 Nov 24.

Abstract

The purification and characterization of an NAD(+)-dependent and zinc containing alcohol dehydrogenase (ADH) from Thermus thermophilus (TTHADH) is described. The enzyme could be purified with 25-fold purification and 68% yield using a single chromatographic step. The enzyme was found to be a tetramer (170 kDa) of identical subunits. The pH optimum of the purified enzyme was 8.8 and the temperature optimum was found to be 80 degrees C. Thermal denaturation curves were determined by monitoring the CD values at 222 nm and the T(m) was found to be 89 degrees C. The enzyme showed much higher activity towards glycerol as compared to short chain primary and secondary alcohols. This thermostable enzyme was also highly stereospecific in oxidation of glycerol and converted glycerol into d-glyceraldehyde. The enzyme which converts glycerol into a chiral molecule like d-glyceraldehyde opens up several synthetic opportunities.

摘要

从嗜热栖热菌(Thermus thermophilus)中纯化并鉴定出一种依赖 NAD(+)和锌的醇脱氢酶(ADH)(TTHADH)。该酶可以通过单一的色谱步骤进行纯化,获得 25 倍的纯化和 68%的收率。研究发现该酶为四聚体(170 kDa),由相同的亚基组成。纯化酶的最适 pH 值为 8.8,最适温度为 80°C。通过监测 222nm 处的 CD 值来确定热变性曲线,发现 T(m)为 89°C。与短链伯醇和仲醇相比,该酶对甘油的活性更高。这种热稳定的酶在甘油的氧化中也具有很高的立体特异性,将甘油转化为 d-甘油醛。将甘油转化为类似 d-甘油醛的手性分子的酶为多种合成方法提供了可能。

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