摘要
研究不同盐浓度下肌原纤维蛋白的氧化对后继的微生物谷氨酰胺转移酶(MTG)交联反应及凝胶能力的影响。分散在三种盐浓度(0.15、0.45和0.6mol/L NaCl)下的肌原纤维蛋白在4℃分别氧化2h和24h,然后在0.6mol/L NaCl条件下加入MTG于30℃交联2h。通过电泳和溶解度研究蛋白的氧化对MTG交联反应的影响,通过凝胶强度研究蛋白的氧化对MTG交联反应后凝胶性的影响。研究表明,三种盐浓度下的氧化都会促进MTG交联反应,特别是高盐条件下的氧化(提高量达47.8%)。所有样品经MTG交联后凝胶强度均显著增加(p<0.05),高盐条件下氧化的蛋白其凝胶强度明显高于低盐条件,然而在所有盐浓度下,氧化蛋白的凝胶强度增幅均小于未氧化的。结果表明过多的交联反应反而不利于蛋白成胶性。
The effect of protein oxidation in different salt concentrations on subsequent microbial transglutaminase （MTG）-catalyzed cross-linking reaction and gelation was studied. Myofibrillar proteins dispersed in three salt concentrations （0.15,0.45 and 0.6mol/L NaCI） were oxidized at 4℃ for 2h and 24h, respectively,then treated with MTG in 0.6mol/L NaCI at 30℃ for 2h. Electrophoresis and solubility were used to study the effect of protein oxidation on MTG cross-linking reaction,and gel strength was used to study the effect of protein oxidation on gel properties when treated with MTG. The results showed that oxidation of myofibrillar proteins at three salt concentrations all promoted MTG-mediated cross-linking reaction,especially in high salt concentrations （relative increase induced by MTG was up to 47.8%）. The gel strength of all samples significantly increased after MTG treatment（p〈0.05）. Compared with myofibrilar protein oxidized in low salt concentration,the protein oxidized in high salt concentration formed much stronger gels. Moreover,the relative increase of gel strength for oxidized protein induced by MTG in all salt concentrations was higher than that of the nonoxidized. As a conclusion,excessive cross-linking was found undesirable for protein gelation.
出处
《食品工业科技》
CAS
CSCD
北大核心
2013年第12期141-144,共4页
Science and Technology of Food Industry
基金
美国农业部(2008-35503-18790)资助项目
国家自然科学基金委(30972290)资助项目
关键词
谷氨酰胺转移酶
蛋白氧化
交联反应
凝胶
transglutaminase
protein oxidation
cross-linking reaction
gelation
