NOTES Partial purification and some properties of α-amylase from Bacillus subtilis KIBGE-HAS
نویسندگان
چکیده
An extracellular α-amylase from Bacillus subtilis KIBGEHAS 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. α -Amylase was highly stable at −18°C and loss of activity was very low during stability study. Metal ions like Mn, Ca, Co, K, Mg, and Fe activated the enzyme, while Hg Ba, Cu, Na and Al 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.
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