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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제20권 제12호
- 발행연도
- 2010.1
- 수록면
- 1,696 - 1,701 (6page)
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The α-amylases activity was improved by random mutagenesis and screening. A region comprising residues from the position 34-281 was randomly mutated in B.
licheniformis α-amylase (AmyL), and the library with mutations ranging from low, medium, and high frequencies was generated. The library was screened using an effective liquid-phase screening method to isolate mutants with an altered pH profile. The sequencing of improved variants indicated 2-5 amino acid changes. Among them, mutant TP8H5 showed an altered pH profile as compared with that of wild type. The sequencing of variant TP8H5indicated 2 amino acid changes, Ile157Ser and Trp193Arg,which were located in the solvent accessible flexible loop region in domain B.
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참고문헌 (25)
참고문헌 신청
Arnold, F. H / 1999 / Directed evolution of biocatalysts / Curr. Opin. Chemi Biol 3 : 54 ~ 59
Arnold, K. L / 2006 / The SWISS-MODEL Workspace: A Web-based environment for protein structure homology modelling / Bioinformatics 22 : 195 ~ 201
Bessler, C / 2003 / Directed evolution of a bacterial α-amylase: Towards enhanced pH-performance and higher specific activity / Prot. Sci 12 : 2141 ~ 2149
Bisgaard-Frantzen, H / 1999 / Development of industrially important α-amylases / J. Appl. Glycosci 46 : 199 ~ 206
Cadwell, R. C / 1994 / Mutagenic PCR / PCR Methods Appl 3 : 136 ~ 140
Arnold, K. L / 2006 / The SWISS-MODEL Workspace: A Web-based environment for protein structure homology modelling / Bioinformatics 22 : 195 ~ 201
Bessler, C / 2003 / Directed evolution of a bacterial α-amylase: Towards enhanced pH-performance and higher specific activity / Prot. Sci 12 : 2141 ~ 2149
Bisgaard-Frantzen, H / 1999 / Development of industrially important α-amylases / J. Appl. Glycosci 46 : 199 ~ 206
Cadwell, R. C / 1994 / Mutagenic PCR / PCR Methods Appl 3 : 136 ~ 140
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