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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제17권 제9호
- 발행연도
- 2007.1
- 수록면
- 1,460 - 1,468 (9page)
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In this study, an aprox. 2.5-kb gene fragmentincluding the catalase gene from Rhodospirillum rubrum S1was cloned and characterized. The determination of thefragment was organized into three open reading frames,designated as ORF1, catalase, and ORF3 in that order. Thecatalase gene consisted of 1,455 nucleotides and 484 aminoacids, including the initiation and stop codons, and waslocated 326 bp upstream in the opposite direction of ORF1.The catalase was overproduced in Escherichia coli UM255, acatalase-deficient mutant, and then purified for the biochemicalcharacterization of the enzyme. The purified catalase had anestimated molecular mas of 189 kDa, consisting of fouridentical subunits of 61 kDa. The enzyme exhibited activityover a broad pH range from pH 5.0 to pH 1.0 andtemperature range from 20oC to 60oC. The catalase activitywas inhibited by 3-amino-1,2,4-triazole, cyanide, azide, andhydroxylamine. The enzyme’s Km value and Vmax of the catalasefor H2O2 were 21.8 mM and 39,960 U/mg, respectively.Spectrophotometric analysis revealed that the ratio of A406 toA280 for the catalase was 0.97, indicating the presence of a ferrica Soret band at 406 nm, which is typical of a heme-containingcatalase. Treatment of the enzyme with dithionite did not alterthe spectral shape and revealed no peroxidase activity. Thecombined results of the gene sequence and biochemicalcharacterization proved that the catalase cloned from strainS1 in this study was a typical monofunctional catalase, whichdifered from the other types of catalases found in strain S1.
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참고문헌 (23)
참고문헌 신청
/ 1970 / U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 : 680 ~ 685
Beers / 1952 / R. F. Jr. and I. W. Sizer. 1952. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195 : 133 ~ 140
Bose / 1962 / and J. G. Ormerod. 1962. Lightactivated hydrogenase activity in photosynthetic bacterium : 13 ~ 14
Chiu / 1989 / and R. Timkovich. 1989. Proposed structure for the prosthetic group of the catalase HPII from Escherichia coli. J. Am. Chem. Soc. 111 : 7046 ~ 7050
Claiborne / 1979 / A. and I. Fridovich. 1979. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual
Beers / 1952 / R. F. Jr. and I. W. Sizer. 1952. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195 : 133 ~ 140
Bose / 1962 / and J. G. Ormerod. 1962. Lightactivated hydrogenase activity in photosynthetic bacterium : 13 ~ 14
Chiu / 1989 / and R. Timkovich. 1989. Proposed structure for the prosthetic group of the catalase HPII from Escherichia coli. J. Am. Chem. Soc. 111 : 7046 ~ 7050
Claiborne / 1979 / A. and I. Fridovich. 1979. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual
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