Flavobacterium johnsoniae昆布多糖酶的分离纯化及其催化性质  

Purification and catalytic properties of a laminarinase from Flavobacterium johnsoniae

作　　者：周亮[1] 朱永涛[1] 陈冠军[1] 刘巍峰[1] 

机构地区：[1]山东大学微生物技术国家重点实验室,山东济南250100

出　　处：《微生物学通报》2011年第6期839-846,共8页Microbiology China

基　　金：国家863计划项目(No.2006AA10Z342)

摘　　要：约氏黄杆菌Flavobacterium johnsoniae具有分泌裂解酵母细胞壁酶系的能力,经初步分析发现其发酵液中具有葡聚糖酶、几丁质酶和蛋白酶等活性。通过离子交换层析、疏水层析和凝胶过滤层析,从该菌发酵液中分离纯化到一种昆布多糖酶。该酶分子量为35 kD左右,其最适反应温度为50°C,最适反应pH为5.0。以昆布多糖和昆布寡糖为底物的反应表明,该酶以内切酶作用模式进行催化水解。Flavobacterium johnsoniae is capable of secreting enzymes which can efficiently hydrolyze yeast cell wall.Preliminary analysis revealed the presence of glucanase,chintinase and protease activi-ties in its culture supernatant.A laminarinase was purified from the extracellular components of F.johnsoniae through several isolation steps including ion exchange,hydrophobic interaction and gel ex-clusion chromatography.The molecular weight of the purified laminarinase is about 35 kD.The opti-mum temperature and pH of its catalyzed hydrolysis are 50 °C and 5.0,respectively.Laminarin and laminari-oligosaccharide were hydrolyzed by this laminarinase in an endoglucanase mode with lami-naritriose as the main product.

关 键 词：约氏黄杆菌 葡聚糖 酵母细胞壁 昆布多糖酶 纯化 

分 类 号：Q814.1[生物学—生物工程]