Purification and properties of amylase produced by a moderately halophilic Acinetobacter sp.
A moderately halophilic Acinetobacter sp., capable of producing dextrinogenic amylase, was isolated from sea-sands. Maximum enzyme production was obtained when the bacterium was cultivated aerobically in media containing 1 to 2M NaCl or 1M KCl. Two kinds of amylase, amylases I and II were purified from the culture filtrate to an electrophoretically homogenous state by glycogen-complex formation, DEAE-Sephadex A-50 chromatography, and Sephadex G-200 gel filtration. Both enzymes had maximal activity at pH 7.0 in 0.2 to 0.6 M NaCl or KCl at 50 to 55 degrees C. The activities were lost by dialysis against distilled water. Molecular weights for amylases I and II were estimated to be 55 000 and 65 000 respectively by SDS-gel electrophoresis. The action pattern on amylose, soluble starch, and glycogen showed that the products were maltose and maltotriose.
D000150:Acinetobacter / Q000201:enzymology*; D000681:Amylases / Q000302:isolation & purification / Q000378:metabolism*; D003470:Culture Media; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011189:Potassium Chloride / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature
D003470:Culture Media; D012965:Sodium Chloride; D011189:Potassium Chloride; D000681:Amylases