欧姆加热诱导鳗鱼皮胶原蛋白热变性、结构改变及变应原性丧失。
Alteration of collagen thermal denaturation, structural and the abrogation of allergenicity in eel skin induced by ohmic heating.
机构信息
Engineering Research Center of Food Thermal-Processing Technology, College of Food Science and Technology, Shanghai Ocean University, Hucheng Huan Road 999, Pudong, Shanghai 201306, China.
Department of Food Science and Technology, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai 200240, China.
出版信息
Food Chem. 2022 Oct 15;391:133272. doi: 10.1016/j.foodchem.2022.133272. Epub 2022 May 20.
This study aimed to evaluate the effect of ohmic heating (OH) on the thermal denaturation, structure, and allergenicity of collagen in fresh eel skin. The allergenicity of collagen decreased by approximately 70% at 50 °C as measured by simulated gastric fluid (SGF), simulated intestinal fluid (SIF) and ELISA in vitro. SDS-PAGE analysis showed that the molecular weight of collagen did not decrease, but the band strength decreased with an increase in the processing temperature. FTIR and SEM analyses showed that the secondary structure and microstructure of collagen also changed. The water retention, dielectric properties and amino acid content of collagen also decreased with increasing temperature. Compared to water bath heating (WH), OH required significantly less time and energy and reduced the allergenicity of fish skin collagen through protein unfolding and secondary structure changes, thus potentially reducing the allergenicity of eel.
本研究旨在评估欧姆加热（OH）对鲜鳗鱼皮胶原的热变性、结构和变应原性的影响。体外模拟胃液（SGF）、模拟肠液（SIF）和 ELISA 检测结果表明，胶原的变应原性在 50°C 时降低了约 70%。SDS-PAGE 分析表明，胶原的分子量没有降低，但是随着处理温度的升高，条带强度降低。傅里叶变换红外光谱（FTIR）和扫描电子显微镜（SEM）分析表明，胶原的二级结构和微观结构也发生了变化。胶原的保水率、介电性能和氨基酸含量也随温度的升高而降低。与水浴加热（WH）相比，OH 所需的时间和能量显著减少，通过蛋白质展开和二级结构变化降低了鱼皮胶原的变应原性，从而潜在降低了鳗鱼的变应原性。
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