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Journal of dairy science v.100 no.2, 2017년, pp.975 - 980   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Short communication: Improving the activity of bile salt hydrolases in Lactobacillus casei based on in silico molecular docking and heterologous expression

Xiong, Zhi-Qiang (Shanghai Engineering Research Center of Food Microbiology, School of Medical Instruments and Food Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China ); Wang, Qiao-Hui (Shanghai Engineering Research Center of Food Microbiology, School of Medical Instruments and Food Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China ); Kong, Ling-Hui (Shanghai Engineering Research Center of Food Microbiology, School of Medical Instruments and Food Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China ); Song, Xin (Shanghai Engineering Research Center of Food Microbiology, School of Medical Instruments and Food Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China ); Wang, Guang-Qiang (Shanghai Engineering Research Center of Food Microbiology, School of Medical Instruments and Food Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China ); Xia, Yong-Jun (Shanghai Engineering Research Center of Food Microbiology, School ); Zhang, Hui ( ); Sun, Yong ( ); Ai, Lian-Zhong ( );
  • 초록  

    ABSTRACT Bile salt hydrolase (BSH) plays an essential role in the cholesterol-removing effect of lactic acid bacteria, which hydrolyze conjugated bile salts to amino acid and deconjugated bile salts. However, Lactobacillus casei lacks the bsh gene, which may make it highly sensitive to bile salt stress. We wanted to improve the BSH activity of L. casei for various food-industry applications (e.g., milk fermentation). Plate assay testing indicated that Lactobacillus plantarum AR113 has the highest BSH activity. We cloned and sequenced 4 bsh genes from the genome of L. plantarum AR113. Structure modeling and molecular docking of BSH indicated that BSH1 and BSH3 could react efficiently with bile salts, so we selected BSH1 and BSH3 for heterologous expression in L. casei . Compared with single expression of BSH1 or BSH3, co-expression of both protein sequences showed the highest hydrolysis activity by HPLC analysis. Our results suggested that heterologous expression of BSH in L. casei can significantly improve host activity against bile salts, and in silico molecular docking could be an efficient method of rapid screening for BSH with high activity.


  • 주제어

    bile salt hydrolase .   Lactobacillus casei .   molecular docking .   heterologous expression.  

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