谷氨酰胺转胺酶对酪蛋白的改性效应  

Modification Study on Goat Milk Casein by Transglutaminase

作　　者：蔡慧农[1] 李亚玲[2] 陈发河[1] 

机构地区：[1]集美大学生物工程学院,福建厦门361021 [2]新疆农业大学食品科技系,新疆乌鲁木齐830052

出　　处：《食品科学》2004年第2期107-111,共5页Food Science

基　　金：福建省科技厅科技计划项目(闽财指:2001Z006)

摘　　要：羊乳中的酪蛋白经商品级谷氨酰胺转胺酶作用后,产物经SDS-PAGE检测,发现生成了相对分子量较大的聚合物。聚合的最佳条件为:酶量/酪蛋白=15U/g;最适pH:6.0～8.0;最适反应温度:50℃;反应时间:120min。其中β-酪蛋白最易被催化,其次为αs-1酷蛋白,αs-2酷蛋白,k-酪蛋类白不易被催化。经谷氨酰胺转胺酶改性后的酪蛋白溶液,其粘度增加,乳化能力提高,起泡性下降。The casein of goat milk modified by transgluatminase was studied.SDS-PAGE assay showed that high-molecular-weight biopolymers were formed.The appropriate conditions to form the biopolymers were as follows:ezyme/protein=15U/g:pH 60～8.0; appropriate temperature 50℃and appropriate time 120min.The result, also showed that β- casein and α-casein were more easily polymerized by TGase than k-casein.After polymerization,the emulsifying stability and theviscosity of casein were increased.,while the foaming property of casein was decreased.

关 键 词：谷氨酰胺转胺酶 酪蛋白 羊乳 改性 SDS-PAGE检测 粘度 乳化能力 

分 类 号：TS201.21[轻工技术与工程—食品科学]