摘要
利用亲和色谱Affi-gel和离子交换色谱SP-Toyopearl从绿豆种子中分离纯化出几丁质酶.纯化的蛋白通过SDS-聚丙烯酰胺凝胶电泳鉴定达到电泳纯,分子质量为30.8kDa.还原和非还原状态下的几丁质酶蛋白均显示单一区带,说明该几丁质酶为单倍体蛋白.通过等点聚焦法测得pI为6.3.该酶的最适pH为5.4,最适反应温度为40～50℃.
A chitinase was isolated from the seeds of mung bean (Phaseolus mungo) by the procedure containing aqueous extraction, affinity chromatography Affi-gel and ion exchange chromatography on SP-Toyopearl. The purified enzyme exhibited a single band on SDS-PAGE with a molecular weight of 30.8?kDa both in reduced and oxidized conditions, indicating it is monomeric protein. The pI was measured to be 6.3 by isoelectric focusing. This enzyme showed its optimum activity at pH?5.4, and a temperature between 40?℃ and 50?℃. These results demonstrated the purified protein was a kind of new chitinase.
出处
《福州大学学报（自然科学版）》
CAS
CSCD
2004年第6期769-772,共4页
Journal of Fuzhou University(Natural Science Edition)
基金
福建省青年科技人才创新重点项目(2001J40)
福州大学科技发展基金资助项目(2003-XY-07)
关键词
绿豆
几丁质酶
蛋白质
纯化
酶
表征
mung bean
chitinase
protein
purification
enzyme
characterization
