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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제22권 제11호
- 발행연도
- 2012.1
- 수록면
- 1,532 - 1,539 (8page)
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초록· 키워드
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The α-galactosidase-coding gene agaAJB13 was cloned from Sphingomonas sp. JB13 showing 16S rDNA (1,343 bp)identities of ≤97.2% with other identified Sphingomonas strains. agaAJB13 (2,217 bp; 64.9% GC content) encodes a 738-residue polypeptide (AgaAJB13) with a calculated mass of 82.3 kDa. AgaAJB13 showed the highest identity of 61.4% with the putative glycosyl hydrolase family 36α-galactosidase from Granulicella mallensis MP5ACTX8(EFI56085). AgaAJB13 also showed <37% identities with reported protease-resistant or Sphingomonas α-galactosidases.
A sequence analysis revealed different catalytic motifs between reported Sphingomonas α-galactosidases (KXD and RXXXD) and AgaAJB13 (KWD and SDXXDXXXR).
Recombinant AgaAJB13 (rAgaAJB13) was expressed in Escherichia coli BL21 (DE3). The purified rAgaAJB13was characterized using p-nitrophenyl-α-D-galactopyranoside as the substrate and showed an apparent optimum at pH 5.0 and 60oC and strong resistance to trypsin and proteinase K digestion. Compared with reported proteaseresistant α-galactosidases showing thermolability at 50oC or 60oC and specific activities of <71 U/mg with or without protease treatments, rAgaAJB13 exhibited a better thermal stability (half-life of >60 min at 60oC) and higher specific activities (225.0-256.5 U/mg). These sequence and enzymatic properties suggest AgaAJB13 is the first identified and characterized Sphingomonas α-galactosidase, and shows novel protease resistance with a potential value for basic research and industrial applications.
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참고문헌 (21)
참고문헌 신청
Baik, S. H. / 2000 / Molecular cloning and high-level expression in Escherichia coli of fungal α-galactosidase from Absidia corymbifera IFO8084 / J. Biosci. Bioeng 90 : 168
Bradford, M. M. / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 7
Buja, L. M. / 2009 / Evaluation of recombinant α-galactosidase A therapy for amelioration of the cardiovascular manifestations of Fabry disease: An important role for endomy
Cantarel, B. L. / 2009 / The Carbohydrate-Active EnZymes database (CAZy): An expert resource for glycogenomics / Nucleic Acids Res 37 : D233 ~ D238
Cao, Y. / 2009 / A novel protease-resistant α-galactosidase with high hydrolytic activity from Gibberella sp. F75: Gene cloning, expression, and enzymatic characterization /
Bradford, M. M. / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 7
Buja, L. M. / 2009 / Evaluation of recombinant α-galactosidase A therapy for amelioration of the cardiovascular manifestations of Fabry disease: An important role for endomy
Cantarel, B. L. / 2009 / The Carbohydrate-Active EnZymes database (CAZy): An expert resource for glycogenomics / Nucleic Acids Res 37 : D233 ~ D238
Cao, Y. / 2009 / A novel protease-resistant α-galactosidase with high hydrolytic activity from Gibberella sp. F75: Gene cloning, expression, and enzymatic characterization /
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