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谷氨酰胺转胺酶的分离纯化及酶学性质的研究 被引量:8

谷氨酰胺转胺酶的分离纯化及酶学性质的研究
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摘要 对灰轮丝链轮丝菌ZC60所产生的谷氨酰胺转胺酶采用(NH4)2SO4盐析、透析脱盐、冷冻浓缩和SephadexG-100凝胶过滤层析进行纯化,经SDS-PAGE检测,样品达到电泳级纯。对冷冻浓缩后得到的粗酶的酶学性质进行研究,得到该酶的最适反应温度为50℃,最适pH为7.0;酶的温度稳定范围为0~50℃,pH稳定范围为6.0~7.5;K+、Na+、Ca2+、Ba2+、Mg2+对MTG的活性几乎没有影响,而Pb2+,Cu2+抑制酶活。 The crude enzyme of transgulaminase from streptoverticillium griseoverticillatum was purified using saturation of ammonium sulfate, dialyzing. freeze concentrating and sepHadex G-100,The apparent purity was examined by SDS-PAGE. The properties of the crude enzyme were studied. The optimal temperature and pH were 50℃ and 7,0.respectively. The crude enzyme was stable below 50℃ and within pH 6.0-7.5. Metal ions of K+,Na+,Ca2+,Ba2+ and Mg2+ had little effect on the activity of MTG. but Pb2+ and Cu2+ can inhibit the activity of the enzvme,
出处 《食品工业科技》 CAS CSCD 北大核心 2007年第1期60-62,共3页 Science and Technology of Food Industry
基金 辽宁省科技厅科技攻关项目(2004205001) 辽宁省教育厅项目(2005369) 沈阳农业大学中 青年硕士导师项目资助
关键词 谷氨酰胺转胺酶 分离纯化 酶学性质 transgulaminase purification enzymologyproperties
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参考文献7

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二级参考文献10

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