The effect of high pressure on the functional properties of pork myofibrillar proteins
The effect of high pressure on the functional properties of pork myofibrillar proteins
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DOI：
10.1016/j.foodchem.2015.10.062
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发表时间：
2016-04-01
期刊：
影响因子：
8.8
通讯作者：
Orlien, Vibeke
中科院分区：
文献类型：
--
作者：
Grossi, Alberto;Olsen, Karsten;Orlien, Vibeke
使用补充方法来分析在 200、400、600 或 800 MPa（10 分钟、5 或 20 摄氏度）加压下猪肉中肌原纤维蛋白的压力诱导修饰和功能。研究发现 400 MPa 的压力是溶解度丧失的阈值，结构蛋白、肌球蛋白和肌动蛋白会因聚集而丧失其天然溶解度。使用针对破坏特定分子相互作用的不同试剂提取蛋白质的结果表明，压力诱导的聚集主要是由加压过程中的氢键引起的，而不是疏水相互作用或二硫键交联。此外，可溶性蛋白质在 200 MPa 的压力下已经发生了显着的结构变化，并失去了其天然功能。加压肉中蛋白质的修饰影响了肌原纤维蛋白质的水结合位点，从而影响了蛋白质和水分子之间的相互作用，以及肌原纤维和肌原纤维外区室之间的分布。 (C) 2015 Elsevier Ltd. 保留所有权利。
Complementary methodologies were used to analyse the pressure-induced modification and functionality of myofibrillar proteins from pork meat pressurised at 200, 400, 600, or 800 MPa (10 min, 5 or 20 degrees C). Pressure at 400 MPa was found to be the threshold for loss of solubility, and the structural proteins, myosin and actin, lost their native solubility due to aggregation. The results from the extraction of proteins with different reagents targeting the disruption of specific molecular interactions suggested that pressure-induced aggregation was caused mainly by hydrogen bonding during pressurisation and not hydrophobic interactions nor disulphide cross-links. Furthermore, the soluble proteins were exposed to remarkable structural changes already at 200 MPa and lost their native functionality. The modification of the proteins in pressurised meat affected the water binding sites of the myofibrillar proteins and, thereby, the interactions between proteins and water molecules, and distribution between myofibrillar and extra-myofibrillar compartments. (C) 2015 Elsevier Ltd. All rights reserved.