Thermostable liquefying α-amylase from bacillus amyloliquefaciens

An extracellular alpha -amylase is purified to homogeneity with 62% recovery of the enzyme activity using heat treatment, ion-exchange and gel filtration chromatographies. The purified enzyme has a molecular weight of 68,000, isoelectric point 6.25, optimal activity at pH 6 and temperature 65 degree...

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Bibliographic Details
Published in:Biotechnology letters 1990-05, Vol.12 (5), p.393-396
Main Authors: KOCHHAR, S, DUA, R. D
Format: Article
Language:English
Subjects:
alpha -amylase
Bacillus amyloliquefaciens
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Fundamental and applied biological sciences. Psychology
Mission oriented research
Physiology and metabolism
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Summary:An extracellular alpha -amylase is purified to homogeneity with 62% recovery of the enzyme activity using heat treatment, ion-exchange and gel filtration chromatographies. The purified enzyme has a molecular weight of 68,000, isoelectric point 6.25, optimal activity at pH 6 and temperature 65 degree C, K sub(cat) 8.8 x 10 super(8) s super(-1) liquefying amylase units, and K sub(m) for starch 2.9 mg ml super(-1). The enzyme is further characterized for its endo action on the starch and related polymers. Calcium stabilizes the active conformation of the enzyme during prolonged exposure to the extremes of pH and temperature. The enzyme retains 100% activity for 24 h at 65 degree C and exhibits a half-life of 9, 3, and 0.5 h at 80 degree , 85 degree and 90 degree C, respectively.
ISSN:0141-5492
1573-6776
DOI:10.1007/BF01024438