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논문 기본 정보
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- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제30권 제2호
- 발행연도
- 2020.1
- 수록면
- 216 - 225 (10page)
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An esterase gene, estA1, was cloned from Alteromonas sp. 39-G1 isolated from the Beaufort Sea. The gene is composed of 1,140 nucleotides and codes for a 41,190 Da protein containing 379 amino acids. As a result of a BLAST search, the protein sequence of esterase EstA1 was found to be identical to Alteromonas sp. esterase (GenBank: PHS53692). As far as we know, no research on this enzyme has yet been conducted. Phylogenetic analysis showed that esterase EstA1 was a member of the bacterial lipolytic enzyme family IV (hormone sensitive lipases). Two deletion mutants (Δ20 and Δ54) of the esterase EstA1 were produced in Escherichia coli BL21 (DE3) cells with part of the N-terminal of the protein removed and His-tag attached to the C-terminal. These enzymes exhibited the highest activity toward p-nitrophenyl (pNP) acetate (C2) and had little or no activity towards pNP-esters with acyl chains longer than C6. Their optimum temperature and pH of the catalytic activity were 45°C and pH 8.0, respectively. As the NaCl concentration increased, their enzyme activities continued to increase and the highest enzyme activities were measured in 5 M NaCl. These enzymes were found to be stable for up to 8 h in the concentration of 3-5 M NaCl. Moreover, they have been found to be stable for various metal ions, detergents and organic solvents. These salt-tolerant and chemical-resistant properties suggest that the enzyme esterase EstA1 is both academically and industrially useful.
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참고문헌 (37)
참고문헌 신청
Anthonsen HW / 1995 / Lipases and esterases : a review of their sequences, structure and evolution, Biotechnol / Annu. Rev 1:315~371
Nardini M / 1999 / α/β Hydrolase fold enzymes : the family keeps growing / Curr. Opin. Struct. Biol 9:732~737
Bornscheuer UT / 2002 / Microbial carboxyl esterases : classification, properties and application in biocatalysis / FEMS Microbiol. Rev 26:73~81
Fu J / 2013 / Functional and structural studies of a novel cold-adapted esterase from an Arctic intertidal metagenomic library / Appl. Microbiol. Biotechnol 97:3965~3978
Kim HJ / 2015 / Characterization of novel family IV esterase and family I. 3 lipase from an oil-polluted mud flat metagenome / Mol. Biotechnol. 57:781~792
Nardini M / 1999 / α/β Hydrolase fold enzymes : the family keeps growing / Curr. Opin. Struct. Biol 9:732~737
Bornscheuer UT / 2002 / Microbial carboxyl esterases : classification, properties and application in biocatalysis / FEMS Microbiol. Rev 26:73~81
Fu J / 2013 / Functional and structural studies of a novel cold-adapted esterase from an Arctic intertidal metagenomic library / Appl. Microbiol. Biotechnol 97:3965~3978
Kim HJ / 2015 / Characterization of novel family IV esterase and family I. 3 lipase from an oil-polluted mud flat metagenome / Mol. Biotechnol. 57:781~792
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