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- W2014052728 abstract "Endo β-1,3-glucanase IV (E.C. 3.2.1.6, endo-1,3(4)-β-d-glucanase) from Flav. dormitator var. glucanolyticae FA-5 was shown to be a glycoprotein by gel filtration and sodium dodecyl sulfate gel electrophoresis. The carbohydrate moiety was composed of 17 hexose units. The enzyme had an apparent molecular weight of 3.3 x 104, determined by gel filtration, sodium dodecyl sulfate 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 laminaripen-taose from a variety of linear β-1,3-glucans and showed transglucanosylation activity. The amino acid composition of the enzyme and some of its physicochemical and enzymatic properties are described." @default.
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- W2014052728 date "1981-01-01" @default.
- W2014052728 modified "2023-10-03" @default.
- W2014052728 title "Characterization of endo .BETA.-1,3-glucanase IV from Flavobacterium dormitator var. glucanolyticae FA-5." @default.
- W2014052728 cites W2132068224 @default.
- W2014052728 doi "https://doi.org/10.1271/bbb1961.45.2689" @default.
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