β-甘露聚糖酶的结构生物学研究现状和展望

Recent advances and prospect on structural biology of β-mannanase-A review

摘要:

摘要：β-甘露聚糖酶是一种半纤维素水解酶，广泛存在于动植物和微生物中，在造纸，纺织印染，洗涤，食品，饲料，医药和石油开采等工业中有着广阔的应用前景。β-甘露聚糖酶往往由催化域和非催化域两部分组成的。催化域折叠成TIM桶状结构，参与底物的结合和催化；碳水化合物结合域,作为最常见的一种非催化域，采用经典的β三明治结构，可以增强结合有纤维素的甘露糖水解能力。本文主要对组成β-甘露聚糖酶的各个模块三维结构特征和功能进行了系统的综述。

Abstract:

Abstract: β-mannanases (β-1, 4-D-mannanase, EC 3.2.1.78), as a hemicellulose hydrolase, are widely distributed in bacteria, fungi, plants and even animals. They can randomly hydrolyze the β-1,4-mannosidic linkages in mannan and heteromannan and have great potential in the food/feed, pulp/paper, medicine, oil exploitation and detergent industries. Most β-mannanases often display a modular organization and usually contain structurally discrete catalytic and non-catalytic modules. Catalytic domains of these enzymes share a (β/α)8 –barrel fold, which play important roles in substrate binding and catalysis. Carbohydrate binding modules, as the most common non-catalytic modules, fold as β-sandwich and facilitate the targeting of these enzymes to polysaccharide. In this review, a brief introduction is given concerning structural characteristics and function of these β-mannanase modules.