Robillarda sp.のセルラーゼによるセルロースの分解

概要

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The fungus, Robillarda sp. Y-20,was isolated from soil a endo-type cellulase producer. The properties of this crude enzyme were studied.Microcrystalline cellulose hydrolyzing activity was most active at pH 4.6-5 and 40℃, and CM-cellulose hydrolyzing activity was most active at pH 5 and 45℃. The two activities were stable between pH 4.6 and 5.6. Microcrystalline cellulose hydrolyzing activity was stable below 37℃, and CM-cellulose hydrolyzing activity was stable below 40℃.Acid-treated cellulose with a little crystalline structure was hydrolyzed by crude enzymes from Aspergillus niger, Trichoderma viride, and Robillarda sp. Y-20. A niger cellulase was more strongly affected by the remaining crystalline structure than Robillarda sp. Y-20 cellulase. The saccharification rate of acid-treated cellulose by Robillarda sp. Y-20 cellulase was nearly equal to that of T. viride cellulase.On hydrolysis of pretreated agricultural hyproducts by the crude enzyme, rice straw had the highest saccharification rate; 5% rice straw suspension was hydrolyzed at 12 h up to 75%.The combined use of the crude enzyme with T. viride cellulase stimulated the hydrolysis of rice straw. Saccharification was nearly 100% at 16 h. The hydrolysate of rice straw consisted of xylose, glucose, and several oligosaccharides.
社団法人日本生物工学会の論文
1986-11-25