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NaCl 和温度诱导的蛋白质聚集对家蚕蛹原粉胶凝的影响。

Effects of protein aggregation induced by NaCl and temperature on gelation of silkworm (Antheraea pernyi) pupa raw powder.

机构信息

College of Food Science and Engineering, Shenyang Agricultural University, Shenyang 110866, Liaoning, China.

College of Biological Science and Technology, Shenyang Agricultural University, Shenyang 110866, Liaoning, China.

出版信息

Int J Biol Macromol. 2023 Dec 31;253(Pt 1):126679. doi: 10.1016/j.ijbiomac.2023.126679. Epub 2023 Sep 2.

DOI:10.1016/j.ijbiomac.2023.126679
PMID:37666404
Abstract

Edible insects have great potential for producing protein-rich ingredients. This study aimed to investigate the effects of protein aggregation induced by NaCl (0-1 M) and temperature (65-95 °C) on gelation of Antheraea pernyi (A. pernyi) pupa raw powder. No thermal aggregates were observed at low temperature (65 °C), on the basis of there being no significant enhancement in turbidity and particle size (P > 0.05), regardless of NaCl concentrations. At elevated temperatures (75-95 °C), protein solutions exhibited significantly higher turbidity and particle size (P < 0.05), accompanied by an initial rise in surface hydrophobicity followed by a decline, alongside declining sulfhydryl. This marks the beginning of massive thermal aggregation driven by molecular forces. In addition, covalent (disulfide bonds) and non-covalent (hydrogen bonding, electrostatic interactions, and hydrophobicity) forces were influenced by NaCl, leading to variability in the protein aggregation and gelation. Correlation analysis indicates that the higher protein aggregation induced by ions was beneficial to the construction of more compact three-dimensional structures, as well as to the rheology, texture, and water-holding capacity of A. pernyi pupa gels. However, excessive salt ions destroyed the gel structure. Our findings will aid the use of A. pernyi pupae as textural ingredients in formula foods.

摘要

食用昆虫在生产富含蛋白质的成分方面具有巨大的潜力。本研究旨在探讨 NaCl(0-1 M)和温度(65-95°C)诱导的蛋白质聚集对柞蚕蛹原粉凝胶形成的影响。根据浊度和粒径(P>0.05)没有显著增加,低温(65°C)下没有观察到热聚集,无论 NaCl 浓度如何。在较高温度(75-95°C)下,蛋白质溶液表现出显著更高的浊度和粒径(P<0.05),伴随着表面疏水性的初始增加随后下降,同时巯基下降。这标志着由分子力驱动的大规模热聚集的开始。此外,NaCl 影响了共价(二硫键)和非共价(氢键、静电相互作用和疏水性)力,导致蛋白质聚集和凝胶形成的可变性。相关分析表明,离子诱导的更高蛋白质聚集有利于构建更紧凑的三维结构,以及柞蚕蛹凝胶的流变学、质地和持水性。然而,过多的盐离子会破坏凝胶结构。我们的研究结果将有助于柞蚕蛹作为配方食品中结构成分的使用。

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