玉米细菌性枯萎病菌EGase内切葡聚糖酶蛋白纯化研究初探

目的研究玉米细菌性枯萎病菌EGase内切葡聚糖酶蛋白纯化的方法。方法以玉米细菌性枯萎病菌（Pantoea stewartii subsp.stewartii）菌株为材料,分离纯化其内切葡聚糖酶Egase。制备EGase浓缩液,浓缩液经SephradexTMG-75凝胶过滤层析和DEAE-Sephorose Fast Flow阴离子交换柱层析等提纯步骤,获得了凝胶电泳均一的内切葡聚糖酶。结果经变性聚丙烯酰胺凝胶电泳检测为一条电泳带,纯化后的EGase是单体蛋白,分子量约为72.3 k Da。Egase酶反应的最适温度是60℃,最适pH为5.0。结论本研究从玉米细菌性枯萎病菌中分离得到了一种新的内...

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Bibliographic Details
Published in食品安全质量检测学报 Vol. 7; no. 4; pp. 1392 - 1396
Main Author 厉艳 邵秀玲 张京宣 王英超 封立平 王简
Format Journal Article
LanguageChinese
Published 山东出入境检验检疫局检验检疫技术中心,青岛,266002 2016
Subjects
内切葡聚糖酶
玉米细菌性枯萎病菌
蛋白纯化
endoglucanase
protein purification
蛋白纯化
内切葡聚糖酶
玉米细菌性枯萎病菌
Pantoea stewartii subsp.stewartii
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ISSN2095-0381

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Summary:目的研究玉米细菌性枯萎病菌EGase内切葡聚糖酶蛋白纯化的方法。方法以玉米细菌性枯萎病菌（Pantoea stewartii subsp.stewartii）菌株为材料,分离纯化其内切葡聚糖酶Egase。制备EGase浓缩液,浓缩液经SephradexTMG-75凝胶过滤层析和DEAE-Sephorose Fast Flow阴离子交换柱层析等提纯步骤,获得了凝胶电泳均一的内切葡聚糖酶。结果经变性聚丙烯酰胺凝胶电泳检测为一条电泳带,纯化后的EGase是单体蛋白,分子量约为72.3 k Da。Egase酶反应的最适温度是60℃,最适pH为5.0。结论本研究从玉米细菌性枯萎病菌中分离得到了一种新的内切葡聚合糖酶,对其部分性质进行了表述,为后续EGase基因的克隆及表达研究提供了研究基础。
Bibliography:11-5956/TS
Pantoea stewartii subsp.stewartii; endoglucanase; protein purification
LI Yan;SHAO Xiu-Ling;ZHANG Jing-Xuan;WANG Ying-Chao;FENG Li-Ping;WANG Jian;Technical Center of Shandong Entry-Exit Inspection and Quarantine Bureau; Qingdao 266002, China
Objective To investigate the purification method of endoglucanase（EGase） from Pantoea stewartii subsp. stewartii. Methods With the material of Pantoea stewartii subsp. stewartii. strain, EGase fermented liquid was prepared, and then eluted using Sephadex~（TM）G-75 and on DEAE-Sepharose Fast Flow anion exchange. SDS-PAGE was used to determine the EGase activity after purification. Results Endoglucanase was purified from Pantoea stewartii subsp. stewartii. It was monomer protein and its molecular size was 72.3 k Da. The optimum reaction temperature of endoglucanase was 60 ℃ and the optimum pH was 5.0. Conclusion Endoglucanase was purified firstly from Pantoea stewartii subsp. stewartii and its properties were described. This study will provide an important base for c
ISSN:2095-0381