求把下面的英文翻译成中文,非常感谢。

Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions

Based on sequence alignments and homology modeling, Gly 312 and Lys 436 of the maltogenic amylase from Bacillus sp. US149 (MAUS149) were selected as targets for site-directed mutagenesis to improve the thermostability of the enzyme. Variants of MAUS149 with amino acid substitutions G312A, K436R and G312A–K436R had substrate specificities, kinetic parameters and pH optima similar to those of the wild-type enzyme; however, the enzymes with substitutions K436R and G312A–K436R, had an optimal temperature of 45℃ instead of the 40℃ for the wild-type enzyme. The half-life time at 55℃ increased from 15 to 25 min for the double mutant. Molecular modeling suggests that the increase in thermostability was due to new hydrophobic interactions and the formation of a salt bridge and hydrogen bond in the G312A and K436R variants, respectively. The double mutant could be a potential candidate for application in the bread industry.
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第1个回答  2011-03-15
提高耐高温的maltogenic由Gly312Ala Lys436Arg淀粉酶MAUS149代替,

摘要根据层序的路线及建模、Gly同源的表现436 312和芽孢杆菌产淀粉酶maltogenic sp。MAUS149 US149(目标)被选为定点诱变提高耐高温的酶。MAUS149的变体中的氨基酸G312A基质,K436R和G312A-K436R行情,动力学参数有相似和pH的最优野生酶;然而,这种酶和G312A-K436R K436R与代替,最佳温度45℃40℃,而不是为野生的酶。55℃的半衰期增加时间从15到25分钟为自己所犯下的双重突变体。分子模拟表明,增加的耐盐性是由于新疏水相互作用而形成的盐桥、氢键和K436R在G312A变异体,分别。双变异可能是一个潜在的候选人面包中的工业应用。
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