| 芽孢杆菌（Bacillus subtilis No.16A）苎麻脱胶聚半乳糖醛酸裂解酶的纯化及酶学性质 |
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| 引用本文： | 颜涛,苏静,李德舜.芽孢杆菌（Bacillus subtilis No.16A）苎麻脱胶聚半乳糖醛酸裂解酶的纯化及酶学性质[J].山东大学学报(理学版),2006,41(5):161-165. |
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| 作者姓名： | 颜涛 苏静 李德舜 |
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| 作者单位： | 1. 山东大学,微生物技术国家重点实验室,山东,济南,250100;杭州杭曼香精有限公司,浙江,杭州,310002
2. 山东大学,微生物技术国家重点实验室,山东,济南,250100 |
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| 摘 要： | 通过丙酮沉淀,阳离子交换层析,凝胶过滤,从苎麻脱胶菌Bacillus subtilis No.16A发酵液中纯化了聚半乳糖醛酸酶（PGase）.结果表明该酶分子量为30.2?ｋu,最适作用pH为9.0,最适作用温度为50?℃,在55?℃以下、中性pH（6.0～8.0）范围内稳定, Ca2+、Mg2+对该酶有激活作用, Cu2+、Mn2+、Co2+、Hg2+有抑制作用,酶解产物在235 nm处有强吸收峰,说明该酶是聚半乳糖醛酸裂解酶.
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| 关 键 词： | 苎麻脱胶菌Bacillus subtilis No.16A 聚半乳糖醛酸酶 纯化 性质 |
| 文章编号： | 1671-9352(2006)05-0161-05 |
| 收稿时间： | 2006-02-10 |
| 修稿时间： | 2006年5月17日 |
Purification and properties of Polygalacturonic acid lyase fromramie degumming Bacillus subtilis No.16A |
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| YAN Tao,SU Jing,LI De-shun.Purification and properties of Polygalacturonic acid lyase fromramie degumming Bacillus subtilis No.16A[J].Journal of Shandong University,2006,41(5):161-165. |
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| Authors: | YAN Tao SU Jing LI De-shun |
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| Institution: | 1．State Key Lab. of Microbial Technology, Shangdong Univ., Jinan 250100, Shandong, China;2.Hangmai Flavors Co.,LTD, Hangzhou 310002, Zhejiang, China |
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| Abstract: | Polygalacturonase produced by Bacillus subtilis No.16A was purified by three steps including acetone precipitation, CM Sepharose Fast Flow cation exchange chromatograph and Sephadex G 75 gel filtration chromatography. Its molecular weight is 30.2?kD by SDS PAGE. The optimal pH and temperature of the enzyme activity are 9.0 and 50?℃ respectively. This enzyme is stable under 55?℃ and in the neutral pH（6.0～8.0）. The enzyme activity was stimulated by Ca2+ and Mg2+, while inhibited by Cu2+, Mn2+, Co2+ and Hg2+. It's product has strong absorbtion around 235?nm, which show that it is Polygalacturonic acid lyase. |
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| Keywords: | Bacillus subtilis No 16A polygalacturonase purification property |
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