Title: Properties of thermostable α-amylase from Bacillus licheniformis strain WB-11
Abstract:An α amylase was isolated from Bacillus licheniformis and identified as electrophoretically homogeneous by means of PAGE and SDS PAGE The optimum temperature of the amylase was 95 ℃ and it was stable ...An α amylase was isolated from Bacillus licheniformis and identified as electrophoretically homogeneous by means of PAGE and SDS PAGE The optimum temperature of the amylase was 95 ℃ and it was stable at 50 ℃ as well as 70 ℃.After incubated at 90 ℃ for 30 minutes,the residual activity of the amylase decreased to 28 9%.The optimum pH of the amylase was 6 0 6 5 and its activity was stable at pH range of 5 08 0.The molecular weight of the enzyme was 65 900 and its isoelectric point was 6 94,and its K m to soluble starch was 0 41 mg·mL -1 .The amylase was activated by Ca 2+ ,Mn 2+ ,Cu 2+ ,Co 2+ and Ba 2+ ions,among which,Ca 2+ was the most remarkable with the optimum concentration of 48 mmol·L -1 .Besides,Ca 2+ can also enhance the thermal stability of the amylase.The residual activity of the enzyme increased from 28 9% to 83% after incubated at 90 ℃ for 30 minutes at the presence of 4 mmol·L -1 Ca 2+ .Read More
Publication Year: 2004
Publication Date: 2004-01-01
Language: en
Type: article
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