State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Key Laboratory of Meat Processing and Quality Control, Ministry of Education and College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, United States.
Food Chem. 2019 Jul 1;285:31-38. doi: 10.1016/j.foodchem.2019.01.131. Epub 2019 Jan 31.
This study tested the potential of high-pressure homogenization (HPH, 69 MPa) combined with hydrogen peroxide (HO, at 0, 40, 80, 160 and 320 μmol/g protein) on enhancing the stability of myofibrillar protein (MP, 15 mg/mL) against thermal aggregation (95 °C for 10 min) in aqueous solution. The addition of HO blocked the sulfhydryl (SH) groups, inhibited the formation of disulfide bonds, and suppressed thermal aggregation of MP. HPH facilitated the blockage effect of HO 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 μmol/g HO, while untreated samples formed a gel upon heating. These results proved that HPH combined with HO is an effective strategy to promote heat stability of MP in the development of muscle protein-based beverages.
本研究测试了高压均质（HPH，69 MPa）与过氧化氢（HO，0、40、80、160 和 320 μmol/g 蛋白）联合处理对增强肌原纤维蛋白（MP，15 mg/mL）在水溶液中热聚集稳定性（95°C 10 min）的潜力。HO 的添加阻止了巯基（SH）基团的形成，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出埋藏的 -SH 基团来促进 HO 的阻断作用，从而更有效地抑制热聚集，因此提高了 MP 的溶解度。经 HPH 和 160 μmol/g HO 处理后，超过 75%的加热 MP 保持可溶，而未经处理的样品在加热时形成凝胶。这些结果证明，HPH 与 HO 联合处理是提高肌肉蛋白基饮料中 MP 热稳定性的有效策略。
