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肉类烹饪对肌原纤维蛋白理化状态及体外消化率的影响。

Effect of meat cooking on physicochemical state and in vitro digestibility of myofibrillar proteins.

作者信息

Santé-Lhoutellier Veronique, Astruc Thierry, Marinova Penka, Greve Eleonore, Gatellier Philippe

机构信息

INRA, UR370 QuaPA, F-63122 Saint-Genès Champanelle, France.

出版信息

J Agric Food Chem. 2008 Feb 27;56(4):1488-94. doi: 10.1021/jf072999g. Epub 2008 Feb 1.

DOI:10.1021/jf072999g
PMID:18237130
Abstract

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 alpha-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 alpha-chymotrypsin.

摘要

测定了肉类烹饪对牛腹直肌肌原纤维蛋白的影响。加热处理采用了两个温度(5分钟、15分钟、30分钟和45分钟时为100℃,1分钟时为270℃)。通过羰基和游离巯基水平评估烹饪诱导的蛋白质氧化。通过测量蛋白质的表面疏水性及其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,随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)中。肉类烹饪影响了肌原纤维蛋白对蛋白酶的敏感性,其速率增加或降低,这取决于蛋白酶的性质以及时间/温度参数。结果表明,烹饪诱导的蛋白质羰基化(p<0.01)和聚集(p<0.05)与对胃蛋白酶的蛋白水解敏感性之间存在直接的定量关系。然而,对于胰蛋白酶和α-胰凝乳蛋白酶,未观察到此类相关性。

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