L-arabinose isomerase from Lactobacillus fermentum C6: Enzymatic characteristics and its recombinant Bacillus subtilis whole cells achieving a significantly increased production of D-tagatose
文献类型： 外文期刊
作者： Ma, Donglin 1 ; Qiu, Lu 2 ; Wang, Xiaofang 3 ; Li, Lilang 1 ; Peng, Shuaiying 2 ; Liao, Yan 1 ; Li, Kuntai 1 ;
作者机构： 1.Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China
2.Jiangxi Agr Univ, Jiangxi Engn Lab Dev & Utilizat Agr Microbial Reso, Nanchang 330045, Peoples R China
3.Chinese Acad Trop Agr Sci, Agr Prod Proc Res Inst, Zhanjiang 524001, Peoples R China
关键词： Lactobacillus fermentum; L-arabinose isomerase; Whole-cell biotransformation of D-tagatose
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：7.7； 五年影响因子：7.7 ）
ISSN： 0141-8130
年卷期： 2024 年 278 卷
页码：
收录情况： SCI
摘要： L-arabinose isomerase (L-AI) is a functional enzyme for the isomerizing of D-galactose to produce D-tagatose. In this study, L-AI-C6-encoding gene from the probiotic Lactobacillus fermentum C6 was cloned and expressed in Bacillus subtilis WB600 for investigating enzymatic characteristics and bioconverting D-tagatose by means of whole-cell catalysis. Results showed that the engineered B. subtilis WB600-pMA5-LAI achieved a maximum specific activity of L-AI-C6 (232.65 f 15.54 U/mg protein) under cultivation in LB medium at 28 degrees C for 40 h. The recombinant L-AI-C6 was purified, and enzymatic characteristics test showed its optimum reaction temperature and pH at 60 degrees C and 8.0, respectively. In addition, L-AI-C6 exhibited good stability within the pH range of 5.5-9.0. By using B. subtilis WB600-pMA5-LAI cells as whole-cell catalyst, the highest D-tagatose yield reached 42.91 f 0.28 % with D-galactose as substrate, which was 2.41 times that of L. fermentum C6 (17.79 f 0.11 %). This suggested that the cloning and heterologous expression of L-AI-C6 was an effective strategy for improving Dtagatose conversion by whole-cell catalysis. In brief, the present study demonstrated that the reaction temperature, pH, and stability of L-AI-C6 from L. fermentum C6 meet the demands of industrial application, and the constructed B. subtilis WB600-pMA5-LAI shows promising potential for the whole-cell biotransformation of Dtagatose.
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