裸麦F-1β-グルカンの酵素水解, 特にlaminarinase, cellulase水解について

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F-1 β-glucan from naked barley endosperm, a main component of water soluble β-glucan, has been subjected to degradation with laminarinase from Bacillus circulans and cellulases from Trichoderma viride and Trametes sanguinea. Laminarinase converts F-1 β-glucan in to a trisaccharide, 3-O-β-cellobiosyl-_D-glucose, and a tetrasaccharide, 3-O-β-cellotriosyl- _D-glucose, as the main products. Overall data show that F-1 β-glucan consists mainly of two types of structural sequences; one is the trimeric unit in which a single β-(1-3) linkage alternates with two consecutive β-(1-4) linkages, and the other is the tetrameric unit in which a single β-(1-3) linkage alternates with three consecutive β-(1-4) linkages. It is shown that this laminarinase from B. circulans hydrolyzes the glucoside bond of the reducing side of 1,3-linked β- _D-glucophranose residues.Trichoderma viride cellulase converted F-1 β-glucan to _D-glucose, cellobiose, 4-O-β-laminaribiosyl- _D-glucose and 4^2-O-β-laminaribiosyl-cellobiose as the main products. From T. sanguinea four fractions of cellulase were separated. Their hydrolyzing mechanisms against F-1 β-glucan differed from each other. Thus, it was suggested that the hydrolyzing mechanism of cellulase was different when its orgin or its fraction in the same origin differed.
社団法人日本生物工学会の論文
1969-07-25

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