生物转化
异构酶
突变体
酶
阿拉伯糖
嗜热脂肪地芽孢杆菌
生物化学
化学
芽孢杆菌(形态)
杆菌科
生物
嗜热菌
细菌
微生物学
发酵
木糖
遗传学
枯草芽孢杆菌
基因
作者
Moez Rhimi,Nushin Aghajari,Michel Juy,Hichem Chouayekh,Emmanuelle Maguin,R. Haser,Samír Béjar
出处
期刊:Biochimie
[Elsevier]
日期:2009-05-01
卷期号:91 (5): 650-653
被引量:44
标识
DOI:10.1016/j.biochi.2009.01.014
摘要
l-Arabinose isomerases catalyze the bioconversion of d-galactose into d-tagatose. With the aim of producing an enzyme optimized for d-tagatose production, three Bacillus stearothermophilus US100 l-arabinose isomerase mutants were constructed, purified and characterized. Our results indicate that mutant Q268K was significantly more acidotolerant and more stable at acidic pH than the wild-type enzyme. The N175H mutant has a broad optimal temperature range from 50 to 65 °C. With the aim of constructing an acidotolerant mutant working at relatively low temperatures we generated the Q268K/N175H construct. This double mutant displays an optimal pH in the range 6.0–7.0 and an optimal activity around 50–65 °C, temperatures at which the enzyme was stable without addition of metal ions.
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