微生物转谷氨酰胺酶的纯化方法和酶学性质研究

Purification and enzymatic characteristics of microbial transglutaminase

由Streptoverticilliummobaraense发酵生产的转谷氨酰胺酶经过除菌体、超滤浓缩、乙醇沉淀、干燥后得到粗酶产品 ,其活力回收率约 70 %。又经Superdex 75凝胶过滤和Source 30S阳离子交换两步纯化后得到纯酶 ,最终酶活力收率约 37%。酶最适温度为 5 0℃ ,在 4 0℃以下稳定性良好 ;最适 pH为 6 .0 ,pH4 .0～ 8.0时比较稳定。离子强度对酶影响很小。

Transglutaminase from Streptoverticillium mobaraense was primarily purified after fermentation. After removing mycelia, ultrafiltration, precipitation and lyophilization, transglutaminase was potential to use in food industry. The recovery of activity was about 70% after separation. And then the enzyme was further purified through gel filtration on Superdex75 and cation exchange on Source 30S. The final recovery of activity was about 37%. The optimal temperature of transglutaminase was 52℃ and it was stable below 40℃. The optimal pH was about 6.0 and the enzyme was most stable between pH 4.0～8.0. Ionic strength gave little effect on enzyme activity.