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Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.46 [2009] >
IJBB Vol.46(5) [October 2009] >
| Title: | Partial purification and some properties of  -amylase from Bacillus subtilis KIBGE-HAS |
| Authors: | Bano, Saeeda
Qader, Shah Ali Ul
Aman, Afsheen
Azhar, Abid |
| Keywords: | -Amylase
Bacillus sp.
Surfactant
Metal ions
Thermal stability |
| Issue Date: | Oct-2009 |
| Publisher: | CSIR |
| 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. |
| Page(s): | 401-404 |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Source: | IJBB Vol.46(5) [October 2009]
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