Activity and action pattern of Bacillus licheniformis α‐amylase in aqueous ethanol

FEBS Letters

Stone, Bruce A.¹  Blakeney, Anthony B.¹ 

[1] Department of Biochemistry, La Trobe University, Bundoora, Victoria 3083, Australia

关键词: Bacillus licheniformis;    α-Amylase;    Enzyme activity;    Ethanol-aqueous buffer mixture;    Action pattern;   

DOI  :  10.1016/0014-5793(85)80714-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A purified B. licheniformis α-amylase in a mixture of ethanol-aqueous buffer (1:1, ) retains half the activity shown in water alone. In ethanol-aqueous buffer (7:3, ) about 20% of the activity is retained. The pattern of oligosaccharides produced from amylose changed with ethanol concentration; in aqueous buffer the products are: DP 1 and 2, 33.7%; DP 3, 28.5%; DP 4, 4.4% and DP 5, 33.4%. Whereas in ethanolaqueous buffer (7:3, ) the products are DP 1 and 2, 66.8%; DP 3, 17.3%; DP 4, 4.1 % and DP 5, 11.8%. These results suggest that a change in substrate affinity at the active centre subsites is induced in the ethanolaqueous buffer medium.

【 授权许可】

Unknown