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Purification and properties of α ‐amylase from Micrococcus varians
Author(s) -
Adeleye Adeyemi I.
Publication year - 1990
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620301003
Subject(s) - iodoacetic acid , amylase , chemistry , micrococcus , enzyme , molecular mass , starch , ammonium , enzyme assay , chromatography , extracellular , biochemistry , nuclear chemistry , bacteria , biology , organic chemistry , genetics
An extracellular α‐amylase from Micrococcus varians was partially purified (63 fold) by ammonium sulphate precipitation followed by dialysis and separated by molecular exclusion into three components with molecular weights ranging from approximately 14,000 to 56,000. The amylase had a pH optimum of 7.0 and apparent K m of approximately 0.5 mg ml ‐1 for starch. The enzyme activity was stimulated by Ca 2+ and Mg 2+ ions. Optimum temperature was 45 °C while there was a complete absence of activity at 70 °C in 20 min. Ethylene diaminetetra acetic acid (EDTA) and iodoacetic acid (IA) inhibited the activity of the enzyme.