CELLULOSE-SPLITTING ENZYMES .6. DIFFERENCE IN THE SPECIFICITIES OF CELLULASE AND BETA-GLUCOSIDASE FROM IRPEX-LACTEUS
CELLULOSE-SPLITTING ENZYMES .6. DIFFERENCE IN THE SPECIFICITIES OF CELLULASE AND BETA-GLUCOSIDASE FROM IRPEX-LACTEUS
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DOI：
10.1016/0003-9861(59)90191-2
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发表时间：
1959-01-01
影响因子：
3.9
通讯作者：
HASHIMOTO, Y
中科院分区：
文献类型：
--
作者：
NISIZAWA, K;HASHIMOTO, Y
Several [beta]-D-glucosides and [beta]-D-cellobiosides having different aglycons were employed for a study of the specificities of [beta]-glucosidase and cellulase obtained from the culture solution of Irpex lacteus (Polyporus tulipiferae). Cellobiose, ordinary hetero [beta]-D-glucosides, and aryl and alkyl [beta]-D-cellobiosides were all hydrolyzed easily by the B-glucosidase, but hydroquinone bis-B-B-D-glucoside was not hydrolyzed. These hetero [beta]-D-glucosides, cellobiose, and alkyl [beta]-D-cellobiosides were not or were only slightly hydrolyzed by the cellulase, whereas the aryl [beta]-D-cellobiosides were good substrates. It was confirmed by paper chromatography that the aglycon linkage of p-nitrophenyl [beta]-D-cellobioside was preferentially split by the cellulase, whereas the [beta]-glucosidase hydrolyzed the holoside linkage somewhat easier than the aglycon bond. Irpex cellulase was found, by the use of paper chromatography, to transfer the cellobiosyl residue of p-nitrophenyl [beta]-D-cellobioside to methanol. However, it appeared also to have a very slight ability of splitting off and transferring the terminal glucosyl residue. In contrast, the [beta]-glucosidase transferred the terminal glucosyl residue more easily than the cellobiosyl residue.
