ISSN:
1432-0614
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Abstract Acetone fractionation of Bacillus lentus culture filtrate yielded the highest α-amylase activity and the 66.6% fraction reached 13-fold that of the crude enzyme preparation. Gel filtration and ion exchange chromatography afforded a pure α-amylase (relative molecular mass, 42 000). The pure enzyme was highly active on starch and dextrin. It produced a mixture of oligosaccharides as major products of starch hydrolysis. Maximal activity was reached at 70° C and pH 6.1. Ca2+, Na+, K+ and Sr2+ ions stabilized or slightly stimulated the enzyme whereas Ag+, Co2+, Hg2+, Zn2+, Cd2+ and Fe3+ ions strongly inhibited the activity. The enzyme contained 16 amino acids, of which aspartic and glutamic acids were present in the highest proportions.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00170078
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