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乳清蛋白与扁豆蛋白在独特蛋白质结构形成过程中的结构相互作用机制。

Mechanism of the structural interaction between whey and lentil proteins in the unique creation of a protein structure.

作者信息

Alrosan Mohammad, Tan Thuan-Chew, Easa Azhar Mat, Gammoh Sana, Alu'datt Muhammad H

机构信息

Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, Penang, Malaysia.

Department of Nutrition and Food Technology, Faculty of Agriculture, Jordan University of Science and Technology, Irbid, Jordan.

出版信息

J Food Sci. 2021 Dec;86(12):5282-5294. doi: 10.1111/1750-3841.15974. Epub 2021 Nov 18.

Abstract

Poor solubility is a substantial factor that restricts the production of high value-added lentil proteins (LPs). In this study, whey protein isolates (WPIs), which have high solubility and are used in various food industries, were mixed with LPs at pH 12 to create LP-WPI protein complexes with improved water solubility properties using pH-recycling approach (maintained at pH 12.0 for 60 min and then readjusting to pH 7.0). LP-WPI protein complexes produced in this study have gained high surface charge, increased in the solubilization of protein complexes to ≈92%, as well as improved resistance against protein aggregation. The ratio of LPs to WPIs has a significant effect on the generation of unique tertiary and secondary protein structures based on the protein-protein interaction (PPI) technique via pH-recycling. The protein interaction between LPs and WPIs resulted in alteration on the surface morphology of the produced protein complexes. This study showed that electrostatic interaction, hydrophobic force, and hydrogen bond appear as major molecular forces in this PPI. The efficacy of the pH-recycling method used in this research indicates that this approach could be a robust approach to enhance the functional properties of food proteins. PRACTICAL APPLICATION: The pH-recycling technique is a proven technique for protein complexation in creating novel protein complexes with improved functional properties. Even though lentils are a rich source of plant-based protein, its utilization by food industries is restricted due to the poor water solubility of lentil proteins (LPs). However, by using complexing lentil proteins with whey protein isolates (WPIs), that is, LP-WPI protein complex, was developed. The water solubility of LP-WPI protein complex was significantly higher than LPs, up to approximately 92%. In addition, this could improve the utilization of lentil seeds in food application as an alternative for animal-based proteins.

摘要

溶解性差是限制高附加值扁豆蛋白(LPs)生产的一个重要因素。在本研究中,将具有高溶解性且应用于各种食品工业的乳清分离蛋白(WPIs)与LPs在pH 12下混合,采用pH循环法(在pH 12.0下保持60分钟,然后重新调节至pH 7.0)制备具有改善的水溶性特性的LP-WPI蛋白复合物。本研究中制备的LP-WPI蛋白复合物具有高表面电荷,蛋白质复合物的溶解度提高至约92%,并且对蛋白质聚集的抗性增强。基于pH循环的蛋白质-蛋白质相互作用(PPI)技术,LPs与WPIs的比例对独特的三级和二级蛋白质结构的产生有显著影响。LPs与WPIs之间的蛋白质相互作用导致所产生的蛋白质复合物的表面形态发生改变。本研究表明,静电相互作用、疏水力和氢键是该PPI中的主要分子力。本研究中使用的pH循环方法的有效性表明,该方法可能是增强食品蛋白质功能特性的一种可靠方法。实际应用:pH循环技术是一种经证实的用于蛋白质复合的技术,可用于创建具有改善功能特性的新型蛋白质复合物。尽管扁豆是植物性蛋白质的丰富来源,但由于扁豆蛋白(LPs)的水溶性差,食品工业对其利用受到限制。然而,通过将扁豆蛋白与乳清分离蛋白(WPIs)复合,即开发了LP-WPI蛋白复合物。LP-WPI蛋白复合物的水溶性显著高于LPs,高达约92%。此外,这可以提高扁豆种子在食品应用中作为动物蛋白替代品的利用率。

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