Partial purification and some properties of alpha-amylase from Bacillus subtilis KIBGE-HAS.
An extracellular alpha-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 degrees C for 15 min. alpha-Amylase was highly stable at -18 degrees 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 a-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.
Bano
Saeeda
S
Pharmaceutical Research Centre, PCSIR Laboratories Complex, Karachi, Pakistan.
Ul Qader
Shah Ali
SA
Aman
Afsheen
A
Azhar
Abid
A
D001412:Bacillus subtilis / Q000201:enzymology*; D008670:Metals / Q000494:pharmacology; D013501:Surface-Active Agents / Q000494:pharmacology; D013696:Temperature; D000516:alpha-Amylases / Q000302:isolation & purification* / Q000378:metabolism*
D008670:Metals; D013501:Surface-Active Agents; D000516:alpha-Amylases