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- W1723361719 abstract "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 Km of approximately 0.5 mg ml-1 for starch. The enzyme activity was stimulated by Ca2+ and Mg2+ 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." @default.
- W1723361719 created "2016-06-24" @default.
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- W1723361719 date "1990-01-01" @default.
- W1723361719 modified "2023-09-24" @default.
- W1723361719 title "Purification and properties ofα-amylase fromMicrococcus varians" @default.
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- W1723361719 doi "https://doi.org/10.1002/jobm.3620301003" @default.
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