Partial purification and some properties of -amylase from Bacillus subtilis KIBGE-HAS.
Indian J Biochem Biophys
;
2009 Oct; 46(5): 401-404
Artigo
em Inglês
| IMSEAR
| ID: sea-135224
ABSTRACT
An extracellular -amylase from Bacillus subtilis KIBGE-HAS was partially purified by ultrafiltration and ammonium sulphate precipitation with 19.2-fold purification and specific activity of 4195 U/mg. The enzyme showed relatively high thermostability and retained 62% of its activity when kept at 70°C for 15 min. -Amylase was highly stable at -18°C and loss of activity was very low during stability study. Metal ions like Mn2+, Ca2+, Co2+, K+, Mg2+, and Fe3+ activated the enzyme, while Hg2+ Ba2+, Cu2+, Na+ and Al3+ strongly inhibited the activity. The α-amylase was highly stable in various surfactants and detergents. In the presence of surfactants such as SDS and Triton X-100 the enzyme activity was found 2.9 and 1.8-fold higher respectively than control. The non-ionic detergents (Tween 20 and Tween 80) exhibited slightly inhibitory effect on the enzyme activity.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Tensoativos
/
Temperatura
/
Bacillus subtilis
/
Alfa-Amilases
/
Metais
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
2009
Tipo de documento:
Artigo
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