Please use this identifier to cite or link to this item:
|Title:||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|
Qader, Shah Ali Ul
|Abstract:||<smarttagtype namespaceuri="urn:schemas-microsoft-com:office:smarttags" name="metricconverter"> An extracellular <img src='/image/spc_char/alpha.gif'>-amylase from <i>Bacillus</i> <i style="">subtilis </i>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. <img src='/image/spc_char/alpha.gif'>-Amylase was highly stable at -18°C and loss of activity was very low during stability study. Metal ions like Mn<sup>2+</sup>, Ca<sup>2+</sup>,<sup> </sup>Co<sup>2+</sup>, K<sup>+</sup>, Mg<sup>2+</sup>, and Fe<sup>3+</sup> activated the enzyme, while Hg<sup>2+</sup> Ba<sup>2+</sup>, Cu<sup>2+</sup>, Na<sup>+</sup> and Al<sup>3+</sup> 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.</smarttagtype>|
|ISSN:||0975-0959 (Online); 0301-1208 (Print)|
|Appears in Collections:||IJBB Vol.46(5) [October 2009]|
Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.