Purification and some properties of endopolygalacturonase from Rhizopus sp. LKN

An endopolygalacturonase of Rhizopus sp. strain LKN, one of several isolates from tempe starter (ragi), was purified 235-fold by CM-Sephadex C-50, DEAE-Sephadex A-50 ion exchange chromatographies and Sephadex G-75 gel filtration. The purified enzyme was homogeneous by SDS-PAGE with a M r of 38.5 kDa...

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Bibliographic Details
Published in:World journal of microbiology & biotechnology 1994-05, Vol.10 (3), p.256-259
Main Authors: Elegado, F.B, Fujio, Y
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biotechnology
Eleusine coracana subsp. coracana
enzyme activity
Enzyme engineering
Fundamental and applied biological sciences. Psychology
Improved methods for extraction and purification of enzymes
Methods. Procedures. Technologies
physicochemical properties
polygalacturonase
purification
Rhizopus
starter cultures
tempeh
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Summary:An endopolygalacturonase of Rhizopus sp. strain LKN, one of several isolates from tempe starter (ragi), was purified 235-fold by CM-Sephadex C-50, DEAE-Sephadex A-50 ion exchange chromatographies and Sephadex G-75 gel filtration. The purified enzyme was homogeneous by SDS-PAGE with a M r of 38.5 kDa. Its K m value for pectic acid was 2 mg/ml. It was stable at pH 4.5 to 11 and up to 50°C, with optimum activity at pH 4.5 to 4.75 and 55 to 60°C. Some ionic compounds enhanced the enzyme activity, whereas tannic acid at 0.5 mM caused about 90% inhibition.
ISSN:0959-3993
1573-0972
DOI:10.1007/BF00414857