Purification and properties of amylase produced by a moderately halophilic Acinetobacter sp.

Abstract:

: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.

journal_name

Can J Microbiol

authors

Onishi H,Hidaka O

doi

10.1139/m78-169

subject

Has Abstract

pub_date

1978-09-01 00:00:00

pages

1017-23

issue

9

eissn

0008-4166

issn

1480-3275

journal_volume

24

pub_type

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