A study of the pattern of action of endo-(1→3)-β- d-glucanases from marine bivalves on a polymer substrate labelled at the reducing end

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The pattern of action of L-IV and L-O endo-laminarinases (EC 3.2.1.6) from the crystalline style of the marine bivalves Spisula sachalinensis and Chlamys albidus, respectively, on Smith-degraded laminarin labelled with 3H at the reducing end has been studied. The average d.p. of the substrate was 25. On the basis of relative bond-cleavage frequencies. The L-IV enzyme was shown to attack the substrate molecule more than once per encounter. The degree of this repetitive attack and the subsite affinities of the aglycon part of the active centre of both (1→3)-β- d-glucanases have been evaluated.