Thermal stability and activity improvements of a Ca-independent α-amylase from Bacillus subtilis CN7 by C-terminal truncation and hexahistidine-tag fusion.
Biotechnol Appl Biochem
; 61(2): 93-100, 2014.
Article
em En
| MEDLINE
| ID: mdl-24033784
ABSTRACT
Simultaneous improvements of thermostability and activity of a Ca-independent α-amylase from Bacillus subtilis CN7 were achieved by C-terminal truncation and his6-tag fusion. C-terminal truncation, which eliminates C-terminal 194-amino-acid residues from the intact mature α-amylase, raised the turnover number by 35% and increased the thermostability in terms of half-life at 65 °C by threefold. A his6-tag fusion at either the C- or N-terminus of truncated α-amylase further enhanced its turnover number by 59% and 37%, respectively. Molecular modeling revealed that these improvements could be attributed to structural rearrangement and reorientation of the catalytic residues.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Estabilidade Enzimática
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Alfa-Amilases
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Aminoácidos
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Histidina
Idioma:
En
Revista:
Biotechnol Appl Biochem
Assunto da revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Ano de publicação:
2014
Tipo de documento:
Article