植物乳杆菌β-D-葡萄糖苷酶的定位及活性研究  

Localization and Activity of β-D-Glucosidase from Lactobacillus plantarum

作　　者：张哲[1] 樊明涛[1] 董梅[1] 李爱霞[1] 刘延琳[2] 

机构地区：[1]西北农林科技大学食品科学与工程学院,陕西杨凌712100 [2]西北农林科技大学葡萄酒学院,陕西杨凌712100

出　　处：《食品科学》2014年第15期161-165,共5页Food Science

基　　金：国家现代农业(葡萄)产业技术体系建设专项(nycytx-30-ch-03)

摘　　要：以对硝基苯基β-D-葡萄糖苷为底物,通过比色法从5株植物乳杆菌中筛选出2株有较高β-D-葡萄糖苷酶酶活力的菌株,并利用差速离心分级沉淀对其β-D-葡萄糖苷酶进行定位。根据对植物乳杆菌的生长状况的分析,测定其在不同生长条件下β-D-葡萄糖苷酶的酶活力。结果表明:目的菌株体内的β-D-葡萄糖苷酶为胞内酶,属于细胞膜结合酶;该酶在对数生长末期(培养至12 h)酶活力最高,最适产酶培养基为改良MRS培养基;以完整细胞为参照对象,植物乳杆菌520、XJ-25菌株所产的β-D-葡萄糖苷酶均受纤维二糖及熊果苷的诱导,熊果苷的诱导作用较强。In this study, two strains of Lactobacillus plantarum(L. plantarum) with the highest β-D-glucosidase activity were obtained from five L. plantarum strains with p-nitro-phenyl-β-D-glucopyranoside as the substrate and their cellular localization of β-D-glucosidase was studied by using fractional precipitation with differential centrifugation. In addition, the enzymatic act ivity of β-D-glucosidase was determined under different growth conditions, followed by analyzing the growth of L. plantarum. Our results supported the conclusion that β-D-glucosidase was membrane-associated and might be insoluble. The highest activity was displayed at the late exponential phase and an improved MRS was verified as the optimal medium. For whole cells, β-D-glucosidase was induced by cellobiose and arbutin, but arbutin played more important role in the enzymatic activity.

关 键 词：植物乳杆菌 β-D-葡萄糖苷酶 定位 酶活力 

分 类 号：TS201.3[轻工技术与工程—食品科学]