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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제29권 제6호
- 발행연도
- 2019.1
- 수록면
- 944 - 951 (8page)
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초록· 키워드
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Lipases are industrial enzymes that catalyze both triglyceride hydrolysis and ester synthesis. The overexpression of lipase genes is considered one of the best approaches to increase the enzymatic production for industrial applications. Subfamily I.2. lipases require a chaperone or foldase in order to become a fully-activated enzyme. The goal of this research was to isolate, clone, and co-express genes that encode lipase and foldase from Burkholderia territorii GP3, a lipolytic bacterial isolate obtained from Mount Papandayan soil via growth on Soil Extract Rhodamine Agar. Genes that encode for lipase (lipBT) and foldase (lifBT) were successfully cloned from this isolate and co-expressed in the E. coli BL21 background. The highest expression was shown in E. coli BL21 (DE3) pLysS, using pET15b expression vector. LipBT was particulary unique as it showed highest activity with optimum temperature of 80°C at pH 11.0. The optimum substrate for enzyme activity was C10, which is highly stable in methanol solvent. The enzyme was strongly activated by Ca2+, Mg2+, and strongly inhibited by Fe2+ and Zn2+. In addition, the enzyme was stable and compatible in non-ionic surfactant, and was strongly incompatible in ionic surfactant.
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참고문헌 (30)
참고문헌 신청
Hasan F / 2006 / Industrial application of microbial lipases / Enzyme. Microbiol. Technol 39:235~251
Yang J / 2007 / Cloning, expression and characterization of a novel thermal stable and short-chain alcohol tolerant lipase from Burkholderia cepacia strain G63 / J. Mol. Catal. B 45:91~96
Sebastian J / 2016 / A comparative study between chemical and enzymatic transesterification of high free fatty acid contained rubber seed oil for biodiesel production / Cog. Eng 3:1~12
Wang X / 2009 / Homologous expression, purification and characterization of a novel high-alkaline and thermal stable lipase from Burkholderia cepacia ATCC 25416 / Enzyme. Microb. Technol 45:94~102
Alnoch RC / 2018 / Co-expression, purification and characterization of the lipase and foldase of Burkholderia contaminans LTEB11 / Int. J. Biol. Macromol 116:1222~1231
Yang J / 2007 / Cloning, expression and characterization of a novel thermal stable and short-chain alcohol tolerant lipase from Burkholderia cepacia strain G63 / J. Mol. Catal. B 45:91~96
Sebastian J / 2016 / A comparative study between chemical and enzymatic transesterification of high free fatty acid contained rubber seed oil for biodiesel production / Cog. Eng 3:1~12
Wang X / 2009 / Homologous expression, purification and characterization of a novel high-alkaline and thermal stable lipase from Burkholderia cepacia ATCC 25416 / Enzyme. Microb. Technol 45:94~102
Alnoch RC / 2018 / Co-expression, purification and characterization of the lipase and foldase of Burkholderia contaminans LTEB11 / Int. J. Biol. Macromol 116:1222~1231
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