caa a22 4500 397555504 CHVBK 20180308164800.0 cr unu---uuuuu 161202e199612 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021531 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021531 Fine Substrate Specificities of Four Exo-Type Cellulases Produced by Aspergillus niger, Trichoderma reesei, and Irpex lacteus on (1→3),(1→4)-β-D-Glucans and Xyloglucan [Elektronische Daten] [Yoshihiko Amano, Masahiro Shiroishi, Kazutosi Nisizawa, Eiichi Hoshino, Takahisa Kanda] To investigate the fine substrate specificities of four highly purified exo-type cellulases (Exo-A from Aspergillus niger, CBHI and CBHII from Trichoderma reesei, and Ex-1 from Irpex lacteus), water-soluble substrates such as barley glucan, xyloglucan from tamarind (Tamarindus indica L.), and their oligosaccharides were employed. Four exo-type cellu-lases immediately hydrolyzed 3-O-β-D-cellotriosylglucose to produce cellobiose and laminaribiose. In contrast, CBHII showed no hydrolytic activity towards 32-O-β-D-cello-biosylcellobiose, which was hydrolyzed to cellobiose by the other exo-type cellulases. These cellulases hydrolyzed the internal linkages of barley glucan and lichenan in an endo-type fashion to produce cellobiose and mix-linked oligosaccharides as main products. The lowering activities of the four exo-type cellulases on barley glucan were in the order of Ex-1, CBHIT, Exo-A, and CBHI. Based on gel permeation chromatography analysis of the hydrolysates, Ex-1 seemed to attack the internal cellobiosyl unit adjacent to β 1,3-glucosidic linkages in barley glucan molecule more frequently than did the other cellulases. Xyloglucan was hydrolyzed only by CBHI and CBHII, and produced hepta-, octa-, and nona-sacceharides. In addition, a xyloglucan tetradecasaccharide (XG14) was split only to heptasaccharide (XG7) by CBHI and CBHI. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence barley glucan nationallicence exo-cellulase nationallicence fungi nationallicence substrate specificity nationallicence xyloglucan nationallicence Amano Yoshihiko Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University Wakasato 500, Nagano 380 aut Shiroishi Masahiro Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University Wakasato 500, Nagano 380 aut Nisizawa Kazutosi College of Bioresource Sciences, Nihon University Setagaya-ku, Tokyo 154 aut Hoshino Eiichi Tochigi Research Laboratories, Kao Corporation 2606 Akabane, Ichikai Haga, Tochigi 321-34 aut Kanda Takahisa Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University Wakasato 500, Nagano 380 aut The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1123-1129 0021-924X 120:6<1123 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021531 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021531 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Amano Yoshihiko Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University Wakasato 500, Nagano 380 aut NATIONALLICENCE 700 1- Shiroishi Masahiro Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University Wakasato 500, Nagano 380 aut NATIONALLICENCE 700 1- Nisizawa Kazutosi College of Bioresource Sciences, Nihon University Setagaya-ku, Tokyo 154 aut NATIONALLICENCE 700 1- Hoshino Eiichi Tochigi Research Laboratories, Kao Corporation 2606 Akabane, Ichikai Haga, Tochigi 321-34 aut NATIONALLICENCE 700 1- Kanda Takahisa Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University Wakasato 500, Nagano 380 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1123-1129 0021-924X 120:6<1123 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford