Mulenga D K, Berry D R
Department of Bioscience and Biotechnology, University of Strathclyde, Glasgow, Scotland.
Microbios. 1994;80(324):143-54.
A beta-glucanase enzyme has been described which has beta-1,6 activity but no beta-1,3 activity. It was isolated and purified from cell free extract and culture free medium of Saccharomycopsis fibuligera by a combination of techniques that included adsorption on DEAE-Sepharose and gel filtration through a Sephacryl S-300 column. The extracellular endo-beta-1,6-glucanase had similar physicochemical properties to those of the intracellular one. The intracellular enzyme behaved as an acidic protein with pI 3.95. It had an optimum pH of 5.5 and optimum temperature of 50 degrees C. The enzyme was specific for beta-1,6-glucosidic linkages by an endo-acting mechanism. The molecular weight of the intracellular enzyme was estimated at 51 kD from gel filtration compared with 43 kD for the extracellular enzyme.
已描述了一种具有β-1,6活性但无β-1,3活性的β-葡聚糖酶。它是通过包括在DEAE-琼脂糖上吸附和通过Sephacryl S-300柱进行凝胶过滤在内的一系列技术组合，从产朊假丝酵母的无细胞提取物和无培养基中分离纯化得到的。细胞外内切β-1,6-葡聚糖酶具有与细胞内酶相似的物理化学性质。细胞内酶表现为一种酸性蛋白，其pI为3.95。它的最适pH为5.5，最适温度为50℃。该酶通过内切作用机制对β-1,6-糖苷键具有特异性。通过凝胶过滤估计细胞内酶的分子量为51kD，而细胞外酶为43kD。
