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Enzymic and physicochemical properties of an exo 1 3 beta d glucanase from rhizoctonia solani


Enzymic and physicochemical properties of an exo 1 3 beta d glucanase from rhizoctonia solani



Carbohydrate Research 194: 261-272



ISSN/ISBN: 0008-6215

An exo-(1 .fwdarw. 3)-.beta.-D-glucanase, isolated from a commercial lytic enzyme preparation "kitalase", had mol. wt. 74,000, isoelectric point pH 8.1, optimum pH 5.6, optimum temperatures 53.degree., pH stability 5.0-8.0, and temperature stability up to 65.degree. The enzyme contained 703 amino acids, including 10 Cys, 7 Trp, 11 His, 83 Asp (Asn), and 51 Glu (Gln). The activity was inhibited on modification of the tryptophan, histidine, or carboxyl residues. Oxidation of Trp was inhibited by the addition of substrate. The enzyme released only glucose from a (1 .fwdarw. 3)-.beta.-D-glucan, glucose and gentiobiose from a 6-branched (1 .fwdarw. 3)-.beta.-D-glucan, and had no effect on gentiobiose and methyl .alpha.- and .beta.-D-glucopyranosides. For the series of laminarioligosaccharides G3-G7, the relative velocities of reaction compared to that of laminarin were G7:G6:G5:G4:G3 = 77:65:54:34:3. The enzyme acted on the glucan that had the reducing end modified but not that with the non-reducing end modified. The glucose residues liberated were .alpha. The enzyme is suitable for use in the structural characterization of (1 .fwdarw. 3)-.beta.-D-glucans.

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Accession: 007307240

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