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Partial purification and some properties of <img src='/image/spc_char/alpha.gif'>-amylase from <i style="">Bacillus</i> <i style="">subtilis</i> KIBGE-HAS

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Title Partial purification and some properties of -amylase from Bacillus subtilis KIBGE-HAS
 
Creator Bano, Saeeda
Qader, Shah Ali Ul
Aman, Afsheen
Azhar, Abid
 
Subject -Amylase
Bacillus sp.
Surfactant
Metal ions
Thermal stability
 
Description 401-404


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.
 
Date 2009-10-28T04:06:14Z
2009-10-28T04:06:14Z
2009-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/6299
 
Language en_US
 
Publisher CSIR
 
Source IJBB Vol.46(5) [October 2009]