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Purification and characterization of the amylase of B. subtilis NRRL B3411
Author(s) -
Moseley Martha H.,
Keay Leonard
Publication year - 1970
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260120207
Subject(s) - bacillus subtilis , size exclusion chromatography , amylase , chemistry , hydrolysis , chromatography , molecular mass , enzyme , specific activity , enzyme assay , biochemistry , bacteria , biology , genetics
The amylase of Bacillus subtilis 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 60% 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 ± 2400 as determined by sedimentation equilibrium methods. This purified enzyme is stable at, 70°C in the presence of 0.01 M Ca ++ and 0.1 M 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 α‐amylase as determined by analysis of hydrolysis products and immunological studies.