Determination of amino acids and dipeptides is correlated significantly with optimum temperatures of microbial lipases

被引：2

作者：

Zhang, Hui-Min ^{[1
]}

Li, Jian-Fang ^{[1
]}

Wu, Min-Chen ^{[2
]}

Shi, Hong-Ling ^{[2
]}

Tang, Cun-Duo ^{[3
]}

机构：

[1] Jiangnan Univ, Sch Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China

[2] Jiangnan Univ, Sch Med & Pharmaceut, Wuxi 214122, Jiangsu, Peoples R China

[3] Jiangnan Univ, Sch Biotechnol, Minist Educ, Key Lab Ind Biotechnol, Wuxi 214122, Jiangsu, Peoples R China

来源：

ANNALS OF MICROBIOLOGY | 2013年 / 63卷 / 01期

基金：

中国国家自然科学基金;

关键词：

Microbial lipase; Dipeptide; Optimum temperature; Stepwise regression method; Thermostability; BACILLUS-SUBTILIS LIPASE; PROTEIN THERMOSTABILITY; STABILITY; PURIFICATION; SELECTION; ENZYMES; CLONING; SERINE;

D O I：

10.1007/s13213-012-0475-y

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Amino acids and dipeptides that are correlated significantly with lipase optimum temperatures were searched for in 34 microbial lipase sequences by a stepwise regression method. The positive dipeptides were found to be IR, KS, NY, SA, ST and YR, whereas negative ones were DK, DY, IS, KA, WS, YS and QI. The calculated optimum temperatures from an optimal regression equation of dipeptides fitted the corresponding experimental optimum temperatures of lipases very well, and the maximal absolute difference was only 3.43A degrees C. The spatial positions of the related dipeptides were searched for in two known crystal structures of a thermophilic and mesophilic lipase, respectively. Most of the positive dipeptides were sited in the alpha-helices, while the negative ones were located mainly in the beta-strands or coils and about half of them existed in the N- or C-terminii of the lipases. The results obtained will be very useful in lipase engineering for enhancing lipase thermostability.

引用

页码：307 / 313

页数：7

共 22 条

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