The purification of a novel amylase from Bacillus subtilis and its inhibition by wheat proteins
Keyword(s):
A new alpha-amylase (EC 3.2.1.1) from Bacillus subtilis was purified by affinity chromatography. The molecular weight of the purified enzyme, estimated from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, was 93000, which is very different from the molecular weights of two well-characterized amylases from B. subtilis. Electrofocusing showed an isoelectric point of 5. Amylase shows a broad maximum of activity between pH 6 and 7; maximal inhibition of enzyme by wheat-protein alpha-amylase inhibitors is displayed at pH 7.
1982 ◽
Vol 47
(01)
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pp. 014-018
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1997 ◽
Vol 34
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pp. 681-687
1992 ◽
Vol 38
(11)
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pp. 1162-1166
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1983 ◽
Vol 29
(10)
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pp. 1361-1368
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1976 ◽
Vol 54
(12)
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pp. 1029-1033
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