Properties of thermosensitive extracellular alpha-amylases of Bacillus subtilis.
Enzymological properties of four thermosensitive alpha-amylases (M3, M9, M18, and M20) brought by different mutation sites in alpha-amylase structural gene of Bacillus subtilis were compared with those of the parental alpha-amylase NA64. Two thermosensitive alpha-amylases (M9 and M20) were altered not only in their thermosensitivity but also in their immunological properties, catalytic properties, molecular weights determined by the gel filtration on a Bio-Gel P-100 column, and others. The other two thermosensitive alpha-amylases (M3 and M18) were altered only in their thermosensitivity.
D000681:Amylases; D001407:Bacillus / Q000201:enzymology; D001412:Bacillus subtilis / Q000201:enzymology* / Q000276:immunology; D001426:Bacterial Proteins / Q000032:analysis; D002384:Catalysis; D002850:Chromatography, Gel; D003470:Culture Media; D004355:Drug Stability; D004492:Edetic Acid / Q000494:pharmacology; D004589:Electrophoresis, Disc; D006358:Hot Temperature; D008970:Molecular Weight; D009154:Mutation; D010447:Peptide Hydrolases / Q000302:isolation & purification
D001426:Bacterial Proteins; D003470:Culture Media; D004492:Edetic Acid; D000681:Amylases; D010447:Peptide Hydrolases