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Improving the Acid Resistance of Tannase TanBLp (AB379685) from Lactobacillus plantarum ATCC14917(T) by Site-Specific Mutagenesis

文献类型： 外文期刊

作者： Pan, Hu 1 ; Zhan, Jingjing 1 ; Yang, Hui 1 ; Wang, Chong 1 ; Liu, Huhu 1 ; Zhou, Hui 3 ; Zhou, Haiyan 1 ; Lu, Xiangyang 1 ; Su, Xiaojun 3 ; Tian, Yun 1 ;

作者机构： 1.Hunan Agr Univ, Coll Biosci & Biotechnol, Changsha, Hunan, Peoples R China

2.Inst Agr Product Qual Standard & Testing Res, Tibet Acad Agr & Anim Husb Sci, Lhasa, Peoples R China

3.Hunan Agr Univ, Coll Food Sci & Technol, Changsha, Hunan, Peoples R China

关键词： Tannase; TanBLp; Acid resistance; Catalytic activity; Site-specific mutagenesis

期刊名称：INDIAN JOURNAL OF MICROBIOLOGY （ 影响因子：2.461； 五年影响因子：2.259 ）

ISSN： 0046-8991

年卷期：

页码：

收录情况： SCI

摘要： Tannin acyl hydrolase referred commonly as tannase catalyzes the hydrolysis of the galloyl ester bond of tannin to release gallic acid. The tannase TanBLp which cloned from Lactobacillus plantarum ATCC14917(T) has high activity in the pH range (7.0-9.0) at 40 degrees C, it would be detrimental to the utilization at acidic environment. The catalytic sites and stability of TanBLp were analyzed using bioinformatics and site-specific mutagenesis. The results reiterated that the amino acid residues Ala164, Lys343, Glu357, Asp421 and His451 had played an important role in maintaining the activity. The optimum pH of mutants V75A, G77A, N94A, A164S and F243A were shifted from 8.0 to 6.0, and mutant V75A has the highest pH stability and activity at acidic conditions than other mutants, which was more suitable for industrial application to manufacture gallic acid. This study was of great significance to promote the industrialization and efficient utilization of tannase TanBLp.

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