@article{oai:nagano.repo.nii.ac.jp:00000675,
 author = {WAKABAYASHI, Kazumasa},
 issue = {1},
 journal = {長野大学紀要, ACADEMIC BULLETIN OF NACANO UNIVERSITY},
 month = {Jun},
 note = {application/pdf, An experimental investigation was made on action patterns of two highly purified β-1, 3-glucanase components (named L-I and-IV), obtained from Driselase, a commercial enzyme preparation from Irpex lacteus (Polyporus tulipiferae), on various substrates. L-I and-IV exhibited a high substrate specificity in hydrolyzing β-1, 3-gluco-oligosaccharides with a degree of polymerization higher than 3, although their action patterns were different from each other, but they were inactive toward laminaribiose. L-I did not attack modified pachyman in which the nonreducing terminal residue had been altered by periodate oxidation, whereas L-IV attacked the modified pachyman at a rate of hydrolysis comparable with that of the original pachyman. These facts indicate that L-I cleaves the substrate molecule in an exo-wise manner, successively removing the glucosyl residue from the nonreducing terminal, whereas L-IV cleaves it in a random fashion. L-I can also bypass the β-1, 6-linked branches to cleave β-1, 3-linkages, producing glucose and gentio-biose when scleroglucan was used as substrate, but cannot cleave mixed-linkage β-1, 3-; β-1, 4-glucans such as lichenan and reduced, pneumo-coccal polysaccharide RS III. On the other hand, L-IV can cleave preferentially the β-1, 4-linkages adjacent to the β-1, 3-linked glucose residue in the mixed-linkage β-glucans, but scarcely have action on β-1, 3-glucans containing β-1, 6-linked branch.},
 pages = {63--74},
 title = {Modes of Action of Exo-and Endo-β-1, 3-Glucanases from Irpex lacteus (Polyporus tulipiferae)},
 volume = {11},
 year = {1989}
}