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  • Title: [beta-1,3-1,4-glucanase in sporeforming microorganisms. III. Substrate specificity and action patterns of some Bacillus-beta-glucan-hydrolases (author's transl)].
    Author: Borriss R, Zemek J.
    Journal: Zentralbl Bakteriol Naturwiss; 1980; 135(8):696-703. PubMed ID: 6784376.
    Abstract:
    Comparative investigations were carried out concerning substrate specificity and action patterns of seven Bacillus-endo-beta-glucanases produced by the species, B. subtilis, B. macerans, B. amyloliquefaciens, B. circulans, B. laterosporus, B. pumilus and B. polymyxa. All enzymes with the exception of beta-glucanase from B. macerans hydrolyze lichenan and barley-beta-glucan only and were without action on laminaran and CM-cellulose. It was suggested that hydrolysis products of beta-glucanase produced by B. macerans were markedly different from the products of the other enzymes. We conclude that B. macerans enzyme, which cleaves laminaran and beta-1,3-1,4-glucans, represents "laminarinase" type (1-3-beta-D-glucan glucanohydrolase, E.C. 3.2.1.6). On the other hand the glucanases produced by the other Bacillus strains belong to "licheninases" 1-3,1-4-beta-D-glucan glucanohydrolases, E.C. 3.2.1.73).
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