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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제25권 제10호
- 발행연도
- 2015.1
- 수록면
- 1,660 - 1,669 (10page)
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The present study describes the gene cloning, overexpression and characterization of a novel nitrilase from hyperthermophilic bacterium Thermotoga maritima MSB8. The nitrilase gene consisted of 804 base pairs, encoding a protein of 268 amino acid residues with a molecular mass of 30.07 kDa after SDS-PAGE analysis. The optimal temperature and pH of the purified enzyme were 45°C and 7.5, respectively. The enzyme demonstrated good temperature tolerance, with 40% residual activity after 60 min of heat treatment at 75°C. The kinetic constants Vmax and Km of this nitrilase toward 3-cyanopyridine were 3.12 μmol/min/mg and 7.63 mM, respectively. Furthermore, this novel nitrilase exhibited a broad spectrum toward the hydrolysis of the aliphatic nitriles among the tested substrates, and particularly was specific to aliphatic dinitriles like succinonitrile, which was distinguished from most nitrilases ever reported. The catalytic efficiency kcat/Km was 0.44 /mM/s toward succinonitrile. This distinct characteristic might enable this nitrilase to be a potential candidate for industrial applications for biosynthesis of carboxylic acid.
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참고문헌 (22)
참고문헌 신청
Banerjee A / 2002 / The nitriledegrading enzymes: current status and future prospects / Appl. Microbiol. Biotechnol 60 : 33 ~ 44
Banerjee A / 2006 / Purification and characterization of an enantioselective arylacetonitrilase from Pseudomonas putida. / Arch. Microbiol 184 : 407 ~ 418
Bayer S / 2011 / A nitrilase from a metagenomic library acts regioselectively on aliphatic dinitriles / Appl. Microbiol. Biotechnol 89 : 91 ~ 98
Black GW / 2015 / A high-throughput screening method for determining the substrate scope of nitrilases / Chem. Commun 51 : 2660 ~ 2662
Bradford MM / 1976 / A rapid and sensitiv emethod for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72 :
Banerjee A / 2006 / Purification and characterization of an enantioselective arylacetonitrilase from Pseudomonas putida. / Arch. Microbiol 184 : 407 ~ 418
Bayer S / 2011 / A nitrilase from a metagenomic library acts regioselectively on aliphatic dinitriles / Appl. Microbiol. Biotechnol 89 : 91 ~ 98
Black GW / 2015 / A high-throughput screening method for determining the substrate scope of nitrilases / Chem. Commun 51 : 2660 ~ 2662
Bradford MM / 1976 / A rapid and sensitiv emethod for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72 :
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