High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution
High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution
复制标题
高压均质结合过氧化氢封闭巯基增强鸡胸肌原纤维蛋白水溶液的热稳定性
DOI：
10.1016/j.foodchem.2019.01.131
复制
发表时间：
2019-07-01
期刊：
影响因子：
8.8
通讯作者：
Xu, Xinglian
中科院分区：
文献类型：
--
作者：
Chen, Xing;Xiong, Youling L.;Xu, Xinglian
本研究测试了高压均质化（HPH，69 MPa）与过氧化氢（H2 O2，在0，40，80，160和320 μ mol/g蛋白质）相结合的潜力，对提高稳定性的肌原纤维蛋白（MP，15 mg/mL）对热聚集（95 ℃，10分钟）在水溶液中。H2 O2的加入阻断了巯基，抑制了二硫键的形成，并抑制了MP的热聚集。HPH通过破坏完整的肌原纤维结构和暴露埋藏的- SH基团，促进H2 O2的阻断作用，从而增强对热聚集的抑制作用，从而提高MP的溶解度。超过75%的加热MP与HPH和160 μ mol/g H2 O2处理后保持可溶性，而未处理的样品在加热时形成凝胶。结果表明，HPH与H2 O2的协同作用是提高MP热稳定性的有效策略。
This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (H2O2, at 0, 40, 80, 160 and 320 mu mol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 degrees C for 10 min) in aqueous solution. The addition of H2O2 blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of H2O2 by disrupting the intact myofibril structure and exposing buried - SH groups, and this resultedin stronger inhibition of thermal aggregation therefore improved solubility of MP. More than 75% of heated MP remained soluble after the treatment with HPH and 160 mu mol/g H2O2, while untreated samples formed a gel upon heating. These results proved that HPH combined with H2O2 is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.