Improving the organic solvent resistance of lipase a from Bacillus subtilis in water-ethanol solvent through rational surface engineering
- 주제(키워드) Stability inwater-ethanol cosolvent , Engineering ethanol-interacting residues , Rational surface design , Bacillus subtilis lipase A
- 주제(기타) Agricultural Engineering
- 주제(기타) Biotechnology & Applied Microbiology
- 주제(기타) Energy & Fuels
- 설명문(일반) [Min, Kyoungseon; Lee, Jin-Suk] Korea Inst Energy Res KIER, Gwangju BioEnergy R&D Ctr, Gwangju 61003, South Korea; [Kim, Hee Taek] Chungnam Natl Univ, Coll Agr & Life Sci, Dept Food Sci & Technol, Daejeon 34134, South Korea; [Park, Si Jae] Ewha Womans Univ, Dept Chem Engn & Mat Sci, Grad Program Syst Hlth Sci & Engn, Seoul 03760, South Korea; [Lee, Siseon; Jung, Ye Jean; Joo, Jeong Chan] Catholic Univ Korea, Dept Biotechnol, Bucheon Si 14662, Gyeonggi Do, South Korea; [Yoo, Young Je] Seoul Natl Univ, Sch Chem & Biol Engn, Seoul 08826, South Korea
- 관리정보기술 faculty
- 등재 SCIE, SCOPUS
- 발행기관 ELSEVIER SCI LTD
- 발행년도 2021
- URI http://www.dcollection.net/handler/ewha/000000182336
- 본문언어 영어
- Published As http://dx.doi.org/10.1016/j.biortech.2021.125394
초록/요약
Given that lipase is an enzyme applicable in various industrial fields and water-miscible organic solvents are important reaction media for developing industrial-scale biocatalysis, a structure-based strategy was explored to stabilize lipase A from Bacillus subtilis in a water-ethanol cosolvent. Site-directed mutagenesis of ethanolinteracting sites resulted in 4 mutants, i.e., Ser16Gly, Ala38Gly, Ala38Thr, and Leu108Asn, which were stable in 50% ethanol and had up to 1.8-fold higher stability than the wild-type. In addition, Leu108Asn was more thermostable at 45 degrees C than the wild type. The results discussed in this study not only provide insights into strategies for enzyme engineering to improve organic solvent resistance but also suggest perspectives on pioneering routes for constructing enzyme-based biorefineries to produce value-added fuels and chemicals.
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