Purification and characterization of laminaran hydrolases from Trichoderma viride
Purification and characterization of laminaran hydrolases from Trichoderma viride
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DOI：
10.1271/bbb.67.1349
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发表时间：
2003-06-01
影响因子：
1.6
通讯作者：
Suiko, M
中科院分区：
文献类型：
--
作者：
Nobe, R;Sakakibara, Y;Suiko, M
绿色木霉U-1在麦麸固体培养基中分泌至少三种胞外昆布多糖水解酶，水解来自双环爱胜蚓的昆布多糖（β-1,3:1,6-葡聚糖）。这三种酶，lam AI、All 和 B，被纯化至电泳均质。通过 SDS-PAGE 估计 lam AI、All 和 B 的分子量分别为 70.1、70.4 和 45.0 kDa。虽然 lam AI 和 All 都可以水解指状海带中的海带多糖，但 lam All 对海带多糖的活性高于昆布爱胜蚓。另一方面，lam B 优先水解 pustulan（一种 β-1,6-葡聚糖）。海带寡糖被lam AI和All水解，但B不被水解，而龙胆低聚糖仅被lam B水解。这表明lam AI和All对β-1,3-连接具有特异性，而lam B对β-1,6-连接具有特异性。这些结果表明T. viride U-1具有多种葡聚糖分解酶系统。
At least three extracellular laminaran hydrolases which hydrolyzed laminaran (beta-1,3:1,6-glucan) from Eisenia bicyclis were secreted in wheat bran solid medium by Trichoderma viride U-1. These three enzymes, lam AI, All, and B, were purified to electrophoretic homogeneity. Their molecular masses were estimated to be 70.1, 70.4, and 45.0 kDa for lam AI, All, and B, respectively, by SDS-PAGE. Whereas both lam AI and All could hydrolyze laminarin from Laminaria digitata, lam All showed higher activity against Laminaria laminarin rather than Eisenia laminaran. On the other hand, lam B preferentially hydrolyzed pustulan, a beta-1,6-glucan. Laminarioligosaccharide was hydrolyzed by lam AI and All but not B, whereas gentiooligosaccharide was hydrolyzed by only lam B. It showed that lam AI and All were specific for beta-1,3-linkages, but lam B was specific for beta-1,6-linkages. These results indicated that T. viride U-1 has a multiple glucanolytic enzyme system.