五味子乳杆菌发酵对花生蛋白分子结构和凝胶质量的影响

IF 5.2 Q1 FOOD SCIENCE & TECHNOLOGY Journal of Future Foods Pub Date : 2024-09-24 DOI:10.1016/j.jfutfo.2024.07.005
Wenjun Li , Yexia Guan , Shumin Chen , Xiaoxuan Du , Beibei Yan , Zixu Wang , Runze Ma , Yunxin Zhang , Huang Huang , Deyuan Li , Wei Li
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引用次数: 0

摘要

以五味子乳杆菌发酵花生蛋白,研究发酵过程中不同蛋白组成的花生蛋白分离物、花生素和伴生花生素对其分子结构和热学性质的影响,将花生蛋白与肌纤蛋白复配制备复合凝胶,研究复合乳液的流变学性质和复合凝胶的质构性质,揭示五味子乳杆菌对花生蛋白凝胶性质影响的分子机理。结果表明,五味子发酵增加了花生蛋白的游离巯基含量、表面疏水性和变性温度,降低了β片含量和变性焓。发酵能降低花生蛋白分离物和伴生花生蛋白的游离巯基含量、表面疏水性和变性焓,显著提高花生蛋白分离物和伴生花生蛋白的变性温度和α-螺旋含量。发酵后,花生蛋白分离物和花生素的α-螺旋含量明显增加,花生素的结构发展到最大程度,花生素的热稳定性更高,这证明五味子球菌能促进花生蛋白的凝胶改性。与花生蛋白和分离蛋白改性制备的复合凝胶相比,花生蛋白发酵形成的复合凝胶更容易形成多孔结构,宏观弹性更好。
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Effect of Lactobacillus pentosus fermentation on molecular structure and gel quality of peanut protein
Peanut protein was fermented by Lactobacillus pentosus, to study the effects of different protein composition of peanut protein isolate, arachin and concomitant arachin on their molecular structure and thermal properties during fermentation, the composite gel was prepared by compounding peanut protein with myofibril protein, the rheological properties of the composite emulsion and the texture properties of the composite gel were studied to reveal the molecular mechanism of the effect of L. pentosus on the gel properties of peanut protein. The results showed that the free sulfhydryl content, surface hydrophobicity and denaturation temperature of arachin were increased, β-sheet content and denaturation enthalpy were decreased by L. pentosus fermentation. It can reduce the content of free sulfhydryl group, surface hydrophobicity and denaturation enthalpy of peanut protein isolate and concomitant arachin, the denaturation temperature and α-helix content of peanut protein isolate and arachin were significantly increased. After fermentation, the structure of arachin developed to the maximum and the thermal stability of arachin was higher, which proved that L. pentosus could promote the gel modification of peanut protein. The complex gel formed by fermentation with arachin is easier to form porous structure and has better macro-elasticity than the complex gel prepared by modification of arachin and isolate protein.
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