Improving thermostability of Aspergillus niger phytase by elongation mutation / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 983-987, 2005.
Artículo
en Chino
| WPRIM
| ID: wpr-237038
ABSTRACT
The phytase gene phyA(m) from Aspergillus niger N25 was recombined into E. coli expression vector pET-30b(+). Recombined at expression vectors pET30b-FphyA(m) was served as a template to amplify phytase gene, and the PCR product named elongation mutation gene phyA(e) was expanded with a 13 amino acid sequence from pET-30b-FphyA(m) vector at C-terminal of phytase gene phyA(m). Furthermore, phyA(e) gene was recombined into expression vector pPIC9k and expressed in Pichia pastoris. The comparison experiment of mutant phytase PP-NP0 with wild-type phytase PP-NP(m)-8 showed that the optimum temperature of PP-NPe was increased by 3 degrees C, and its thermostability was increased by 21% when it was exposed to 10 min at 75 degrees C. Its effective reaction pH range with catalysis efficiency above 70% was pH 4.6 - pH 6.6, and wider 0.4 pH value than that of wild-type phytase.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Aspergillus niger
/
Estabilidad de Enzimas
/
Proteínas Fúngicas
/
Datos de Secuencia Molecular
/
Secuencia de Aminoácidos
/
6-Fitasa
/
Escherichia coli
/
Genética
/
Calor
/
Mutación
Idioma:
Chino
Revista:
Chinese Journal of Biotechnology
Año:
2005
Tipo del documento:
Artículo
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