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Purification and properties of α-amylase from Micrococcus varians

✍ Scribed by Dr. Adeyemi I. Adeleye

Publisher
John Wiley and Sons
Year
1990
Tongue
English
Weight
348 KB
Volume
30
Category
Article
ISSN
0233-111X

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✦ Synopsis

Purification and properties of a-amylase from Micrococcus variuns ADEYEMI I . ADELEYE i Rcc?ird I 0 .4u</i~s/ 19cYYiArccy,tetl 6 FdJruciry I9901

An extraccllular cx-amylase from Micrococcus ivxinns 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 apparcnt Kin of approximately 0.5 mg ml for starch. The enzyme activity was stimulated by CaZt and MgZ ' ions. Optimum temperature was 45 C while there was a complete absence ofactivity at 70 C in 20 min. Ethylene diaminetetra acetic acid (EDTA) and iodoacetic acid (IA) inhibited the activity of the enzyme.

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