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Purification and properties of a major isoform of Beta-1,3-glucanase from pearl millet seedlings

Ramachandra Kini, K. and Vasanthi, N.S. and Umesh Kumar, S. and Shekar Shetty, H. (2000) Purification and properties of a major isoform of Beta-1,3-glucanase from pearl millet seedlings. Plant Science, 150. pp. 139-145.

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A major isoform of beta-1,3-glucanase from pearl millet seedlings was purified following ammonium sulfate precipitation,ion-exchange chromatography and gel filtration techniques. The enzyme had a molecular weight of 20.5 kDa on SDS–PAGE and was highly basic with a pI of 9.6. It was thermostable with a broad temperature optima for activity ranging from 37 to 70°C and had an optimum pH of 5.2. Mercuric chloride and para-chloromercuric benzoate inhibited completely the enzyme while manganese chloride activated it. Antibodies raised against the purified b-1,3-glucanase identified another protein with an apparent molecular weight of 30 kDa in western reactions. Significance of this enzyme in pearl millet–downy mildew host–pathogen interaction is discussed.

Item Type: Article
Uncontrolled Keywords: beta-1,3-Glucanase; Pearl millet; Downy mildew; Host–pathogen interaction
Subjects: 600 Technology > 08 Food technology > 21 Cereals
500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology
500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
Divisions: Fermentation Technology and Bioengineering
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 25 Sep 2007 11:55
Last Modified: 28 Dec 2011 09:30
URI: http://ir.cftri.com/id/eprint/1439

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