Effect of meat cooking on physicochemical state and in vitro digestibility of myofibrillar proteins
Effect of meat cooking on physicochemical state and in vitro digestibility of myofibrillar proteins
复制标题
DOI：
10.1021/jf072999g
复制
发表时间：
2008-02-27
影响因子：
6.1
通讯作者：
Gatellier, Philippe
中科院分区：
文献类型：
--
作者：
Sante-Lhoijtellier, Veronique;Astrijc, Thierry;Gatellier, Philippe
测定了肉类烹调对牛M.腹直肌加热处理涉及两个温度（在5、15、30和45分钟期间为100 ° C，在1分钟期间为270 ° C）。蛋白质氧化诱导的烹饪进行了评估的羰基和游离巯基的水平。通过测量蛋白质的表面疏水性和聚集状态来评估蛋白质的结构修饰。为了评估热处理对消化过程的影响，然后将肌原纤维蛋白在模拟胃和十二指肠消化的pH和温度条件下暴露于消化道蛋白酶（胃蛋白酶、胰蛋白酶和α-胰凝乳蛋白酶）。肉类烹饪影响肌原纤维蛋白对蛋白酶的敏感性，根据蛋白酶的性质和时间/温度参数，速率增加或减少。结果表明，蛋白质羰基化（p < 0.01）和聚集（p < 0.05）之间的直接和定量的关系诱导烹饪和蛋白水解敏感性胃蛋白酶。然而，胰蛋白酶和α-胰凝乳蛋白酶没有观察到这种相关性。
The effect of meat cooking was measured on myofibrillar proteins from bovine M. Rectus abdominis. The heating treatment involved two temperatures (100 degrees C during 5, 15, 30, and 45 min and 270 degrees C during 1 min). Protein oxidation induced by cooking was evaluated by the level of carbonyl and free thiol groups. Structural modifications of proteins were assessed by the measurement of their surface hydrophobicity and by their aggregation state. With the aim of evaluating the impact of heat treatment on the digestive process, myofibrillar proteins were then exposed to proteases of the digestive tract (pepsin, trypsin, and a-chymotrypsin) in conditions of pH and temperature that simulate stomach and duodenal digestion. Meat cooking affected myofibrillar protein susceptibility to proteases, with increased or decreased rates, depending on the nature of the protease and the time/temperature parameters. Results showed a direct and quantitative relationship between protein carbonylation (p < 0.01) and aggregation (p < 0.05) induced by cooking and proteolytic susceptibility to pepsin. However, no such correlations have been observed with trypsin and a-chymotrypsin.