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调节肌原纤维蛋白聚集以减轻高温下蛋白质凝胶的质构劣化:疏水相互作用的影响。

Modulating the aggregation of myofibrillar protein to alleviate the textural deterioration of protein gels at high temperature: The effect of hydrophobic interactions.

机构信息

School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, China.

School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, China; Engineering Research Center of Bio-process, Ministry of Education, Hefei University of Technology, Hefei 230601, China.

出版信息

Food Chem. 2021 Mar 30;341(Pt 2):128274. doi: 10.1016/j.foodchem.2020.128274. Epub 2020 Oct 3.

DOI:10.1016/j.foodchem.2020.128274
PMID:33038801
Abstract

In this study, the strategy of utilizing a model hydrophobic molecule, octenyl succinic anhydride (OSA), to inhibit over-aggregation of MP during heating, aiming to alleviate high temperature-induced textural deterioration of MP gels, was proposed, and a series of experiments were conducted to verify the effectiveness. The results showed that the effect was positively dependent on the concentrations of OSA. The addition of OSA at a concentration of 4 g/kg to 24 g/kg delayed the gelation temperature of MP, as confirmed by the DSC results, and inhibited the aggregation of MP through hydrophobic interactions between OSA and MP, as revealed by fluorescence and FTIR spectroscopy. Furthermore, when the concentration of OSA increased from 4 g/kg to 12 g/kg, the controlled aggregation of MP improved the gel properties of MP formed at high temperature, but when the concentration reached 24 g/kg, the protein aggregation was too inhibited to form developed gel networks.

摘要

在这项研究中,提出了一种利用模型疏水分子辛烯基琥珀酸酐(OSA)来抑制 MP 在加热过程中过度聚集的策略,旨在减轻 MP 凝胶因高温引起的质地劣化。进行了一系列实验来验证其有效性。结果表明,该效果与 OSA 的浓度呈正相关。通过 DSC 结果证实,添加浓度为 4 g/kg 至 24 g/kg 的 OSA 可延迟 MP 的胶凝温度,并通过 OSA 与 MP 之间的疏水相互作用抑制 MP 的聚集,这一点通过荧光和傅里叶变换红外光谱得到了揭示。此外,当 OSA 的浓度从 4 g/kg 增加到 12 g/kg 时,MP 的受控聚集改善了高温下形成的 MP 的凝胶特性,但当浓度达到 24 g/kg 时,蛋白质的聚集被过度抑制,无法形成发达的凝胶网络。

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