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Characterization of endo beta 1 3 glucanase iv ec 3.2.1.6 from flavobacterium dormitator var glucanolyticae fa 5


Characterization of endo beta 1 3 glucanase iv ec 3.2.1.6 from flavobacterium dormitator var glucanolyticae fa 5



Agricultural and Biological Chemistry 45(12): 2689-2694



ISSN/ISBN: 0002-1369

Endo-.beta.-1,3-glucanase IV (endo-1,3(4)-.beta.-D-glucanase) from E. dormitator var. glucanolyticae FA-5 was shown to be a glycoprotein by gel filtration and sodium dodecyl sulfate [SDS] gel electrophoresis. The carbohydrate moeity was composed of 17 hexose units. The enzyme had an apparent MW of 3.3 .times. 104 as determined by gel filtration, SDS gel electrophoresis and ultracentrifugation. The enzyme showed maximum reactivity at pH 6.0 and 6.5 for living yeast cells and laminaran, respectively. The enzyme predominantly released laminaripentaose from a variety of linear .beta.-1,3-glucans and showed transglucanosylation activity. The amino acid composition of the enzyme and some of its physicochemical and enzymatic properties are described.

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Accession: 004927974

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Related references

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