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Properties and significance of an α‐amylase produced by Myxococcus coralloides D
Author(s) -
FárezVidal M. Esther,
FernándezVivas Antonia,
González F.,
Arias J.M.
Publication year - 1995
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1995.tb01667.x
Subject(s) - amylase , size exclusion chromatography , sephadex , hydrolysis , maltose , chemistry , chromatography , nuclear chemistry , enzyme , isoelectric point , biochemistry
M.E.FÁREZ‐VIDAL, A. FERNÁNDEZ‐VIVAS, F. GONZÁLEZ AND J.M. ARIAS. 1995. The extracellular amylase activity from Myxococcus coralloides D was purified by Sephacryl S‐200 gel filtration and by ion‐exchange chromatography on DEAE‐Sephadex A‐25. The molecular weight was estimated by SDS‐PAGE and by gel filtration as 22.5 kDa. The optimum temperature was 45°C. The pH range of high activity was between 6.5 and 8.5, with an optimum at pH 8.0. Activity was strongly inhibited by Hg 2+ , Zn 2+ , Cu 2+ , Ag + , Pb 2+ , Fe 2+ and Fe 3+ , EDTA and glutardialdehyde, but was less affected by Ni 2+ and Cd 2+ . Li + , Mg 2+ , Ba 2+ , Ca 2+ , N ‐ethylmaleimide, carbodiimide and phenyl methyl sulphonyl fluoride had almost no affect. The K m (45°C, pH 8) for starch hydrolysis was 2.0 times 10 ‐3 gl ‐1 . Comparison of the blue value‐reducing curves with the time of appearance of maltose identified the enzyme produced by M. coralloides D as an α‐amylase.