Trichoderma pseudokoningii TM37株の生産するエキソ型β-1,3-グルカナーゼのβ-グルカンに対する作用

概要

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Two or three different β-1,3-glucanases are present in Trichoderma pseudokoningii TM37 culture broth. One of these enzymes, EP-1,was purified from a crude enzyme preparation. It seemed to be a single polypeptide with a high molecular weight(>200 kDa by SDS-PAGE)and a pI of 7.0. The optimum pH and temperature for laminarin degradation were 5.0 and 60℃, respectively. EP-1 hydrolyzed β-1,3-glucans such as pachyman and laminarin to produce almost only glucose. From these results and the hydrolysis patterns of laminarioligosaccharides, EP-1 appeared to be a typical exo-β-1,3-glucanase releasing only glucose from the non-reducing end of β-1,3-glucans. However, EP-1 also hydrolyzed β-glucans containing β-1,3- and β-1,4-linkages such as barley glucan, or β-1,3-and β-1,6-linkages such as yeast glucan and laminarin, and besides glucose produced various mixed oligosaccharides with different linkages from these substrates. In this respect, though EP-1 is an exo-enzyme, it could hydrolyze internal glycosydic linkages in the main polysaccharide chain of mixed glucans with different linkages.
社団法人日本生物工学会の論文
1996-07-25