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Purification and Characterization of Thermostable α-Amylase from Soil Bacterium Bacillus sp
1Veterinary Health Department, Vocational School of Food, Agriculture and Livestock, Bingöl University, Bingöl, Turkey.
Background:
Amylases are used in several industrial and biotechnological sectors, including those producing textiles, detergents, paper and bakery products.
Objective:
This study aimed to purify an industrially important α-amylase from Bacillus sp. For this purpose, a single and rapid α-amylase purification was performed using the starch affinity method.
Methods:
Characterization of the purified enzyme was determined by investigating temperature, pH stability, detergents, and metal ions.
Results:
The purification coefficient of 29.8-fold with a yield of 9.2% was found. The molecular weight of the purified α-amylase was determined to be 53 kDa by SDS-PAGE, and thermostability was confirmed with 100% activity at 30ºC and 40ºC after 1 h. The purified enzyme was stable over a wide range of pH values, with optimum activity at pH 6.0, 7.0 and 8.0 after 2 h. The study also investigated the effects of the metal ions and detergents on the purified amylase and found that Mg2+ and Ca2+ ions were the activators of the enzyme, while Zn2+, Co2+ and Na+ ions decreased the activity. Furthermore, Hg2+; indicated complete inhibition of amylase activity. The detergents Triton X-100 and Tween 20 increased the α-amylase activity, while sodium dodecyl sulfate inhibited the activity.
Conclusion:
The purified α-amylase obtained from Bacillus sp. is considered to be environmentally friendly, can be processed in a short time, and has a low cost.
