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Purification and characterization of the amylase of B. subtilis NRRL B3411

✍ Scribed by Martha H. Moseley; Leonard Keay

Publisher: John Wiley and Sons
Year: 1970
Tongue: English
Weight: 732 KB
Volume: 12
Category: Article
ISSN: 0006-3592
DOI: 10.1002/bit.260120207

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✦ Synopsis

The amylase of Bacillus sublilis NRRL B3411 has been purified and partially characterized. The specific activity can be increased from 300,000 units/g to 6,000,000 units/g with a 607, recovery of total units. The purified material consists of one major and one trace anodic component as determined by disc gel electrophoresis. The molecular weight was 48,000 as determined by bio-gel filtration; the molecular weight was 44,900 f 2400 as determined by sedimentation equilibrium methods. This purified enzyme is stable at 70°C in the presence of 0.01M Ca++ and 0.1 R;I NaCl over a broad pH range from 5.5-9.5. The pH activity profile indicates optimum activity at pH 6.0. This amylase exhibits maximum activity at 60°C. The enzyme is a liquefying a-amylase as determined by analysis of hydrolysis products and immunological studies.

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