【作者】 刘红彦；

【导师】 张坤生；

【作者基本信息】 天津商业大学 ， 食品科学， 2012， 硕士

【摘要】 鲤鱼肌原纤维蛋白（Common Carp Myofibrillar Protein，CCMP）是鲤鱼肌肉中蛋白质的主要成分，鱼制品的加工技术都与其密切相关。目前，国内外对CCMP的性质研究尚少，使得鲤鱼制品的深加工受限。因此本实验以鲤鱼为原料，提取肌原纤维蛋白，研究不同实验条件下CCMP的功能特性，如溶解性、乳化性、起泡性及凝胶特性，确定转谷氨酰胺酶（TG）改善CCMP凝胶性的最佳工艺条件，并采用优化酶解CCMP技术制备具有较强抗氧化活性的酶解物，并对其功能性质进行研究。具体研究内容如下：1、试验所采用鲤鱼粗蛋白含量为17.72%，测得肌原纤维蛋白平均含量约为9.86g（每100g肌肉中），占总蛋白含量为55.64%，SDS-PAGE电泳分析表明，肌原纤维蛋白主要由肌球蛋白、肌动蛋白、原肌球蛋白等其他小分子蛋白组成，肌球蛋白是肌原纤维蛋白的主要成分。2、研究了CCMP的功能性质，结果表明CCMP在溶液pH偏离蛋白等电点时溶解性较好，且易溶于0.6~1.0mol/L NaCl溶液中；CCMP乳化性和起泡性受溶液pH、NaCl浓度、蛋白浓度、温度条件变化的影响显著，且不同因素条件对CCMP的乳化性和起泡性影响效果不同。3、对CCMP的凝胶特性进行了研究，结果表明其适宜的凝胶条件为pH6，NaCl浓度为0.6mol/L，制胶温度升至80℃。向CCMP中添加TG，发现TG可以显著改善CCMP的凝胶强度，通过单因素和响应面实验，得到最佳的工艺条件为：pH为6，反应温度为42.5℃，反应时间为2.25h，TG添加量为0.66%，此条件下实验得到的实际凝胶强度为179.461g，凝胶强度较好。4、研究了CCMP的酶解工艺，结果显示木瓜蛋白酶作为水解CCMP的优选蛋白酶，其酶解产物的抗氧化活性较高。经单因素和响应面优化实验，当酶解工艺条件为温度55.6℃，酶的添加量为1118U/g，水解时间为2.1h，在pH为7，底物浓度为4%条件下，此时酶解产物的最大还原力为0.861。对酶解产物的功能性测定结果显示酶解产物在不同pH、NaCl浓度条件下均有很高的溶解性，且pH、NaCl浓度、酶解物浓度、温度条件变化对其乳化性和起泡性影响较大。综合比较CCMP与其酶解产物，发现CCMP的乳化性和泡沫稳定性均高于酶解产物，但起泡能力低于酶解产物。更多还原

【Abstract】 As an important part of Common Carp meat, Common Carp Myofibrillar Protein (CCMP)is closely related to many processing properties. For now, few papers investigated properties ofCCMP, the futher processing of Common Carp is limited. Therefore, this paper studied on theproperties of the myofibrillar proteins extracted from Common Carp in different experimentalconditions, such as solubility, emulsifying, foaming and gel properties. In order to improve gelproperties, the research on the optimal process of transglutaminase (TG) and CCMP wasdiscussed. Hydrolysates with strong antioxidant activity were prepared by means of enzymatichydrolysis technology on CCMP. The main work in this paper was concluded as follows:1. Common Carp protein content is17.72%, and myofibrillar protein content is9.86g (100gmuscle) accounting for55.64%of total protein. The results of myofibrillar protein bySDS-polyacrylamide showed that myosin, actin, tropomyosin and other small molecular proteinconstituted myofibrillar protein. Myosin was the major protein of myofibrillar protein.2. Studying on the functional properties of CCMP, the results showed that solubility ofCCMP had higher capability with deviation isoelectric. And CCMP is easy to be dissolved in0.6~1.0mol/L NaCl solution. Emulsifying and foaming properties of CCMP was changedsignificantly by changes of pH, NaCl concentration, protein concentration and temperature.Different factors conditions had different effect on emulsifying and foaming properties ofCCMP.3. Studying on Gel properties of CCMP, the results showed that the optimal process ofCCMP gel strength was at80℃, pH6,0.6mol/L NaCl concentration. Gel strength of CCMP wasimproved significantly by addition of TG. By single factor experiment and response surfaceexperiment, results showed that the optimal process of CCMP gel strength as follows: pH6,reaction temperature at42.5℃, reaction time for2.25h, and TG content with0.66%. Gel strengthwas better under the optimum condition, up to179.461g.4. Studying on enzymatic hydrolysis process of CCMP, the results showed that higherantioxidant activity of hydrolysates obtained by papain. By single factor experiment andresponse surface experiment, the best condition of the enzyme hydrolysis process was:hydrolysis temperature was55.6℃, enzyme addition was1118U/g and hydrolysis time is2.1h. Then, the biggest reduction power is0.861, in the condition of pH7and4%substrate. The studyon functional properties of hydrolysates showed that hydrolysates of CCMP had better solubilityat different conditions of pH and NaCl concentration. And emulsifying and foaming properties ofhydrolysates was changed significantly by changes of pH, NaCl concentration, hydrolysatesconcentration and temperature. Comprehensive comparison with the emulsifying and foaming ofCCMP and hydrolysates, it demonstrated that emulsifying properties and foam stability ofCCMP was higher than hydrolysates. But foaming capacity was inferior to hydrolysates.更多还原