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凝胶体系中有限的酶解豌豆蛋白与菊粉的相互作用

Limited enzymatically hydrolyzed pea protein-inulin interactions in gel systems.

作者信息

Sawant Sanjana, Alvarez Valente B, Heldman Dennis R

机构信息

Department of Food Science, University of Wisconsin-Madison, Madison, Wisconsin, USA.

Department of Food Science and Technology, The Ohio State University, Columbus, Ohio, USA.

出版信息

J Food Sci. 2024 Dec;89(12):9243-9256. doi: 10.1111/1750-3841.17581. Epub 2024 Dec 1.

DOI:10.1111/1750-3841.17581
PMID:39617827
Abstract

Gelation of protein-polysaccharide mixtures can help create a variety of distinctive gel systems as compared to single polysaccharide or protein gels. The properties of these functional gels are heavily reliant upon the nature of protein-polysaccharides interactions, their gelling compatibility, and mechanism. Pea protein isolate dispersions (7.5%) were subjected to limited enzymatic hydrolysis using the enzyme Alcalase at three hydrolysis times (0, 3, and 6 min). Inulin was added according to three ratios (0, 1:4, and 2:4) with pea protein. Viscoelastic properties of the gels formed were measured using amplitude sweep and frequency sweep. Storage modulus (G') measurements from the amplitude sweep indicated that samples hydrolyzed for 3 min with 1:4 ratio of inulin to pea protein had maximum gel strength, exhibiting G' values of ∼307 Pa. G' values for samples hydrolyzed for 0 and 6 min with different inulin ratios averaged ∼13 and ∼144 Pa, respectively. Confocal laser scanning microscopy showed that gels developed by samples hydrolyzed for 3 min showed a dense network as compared to an open network in gels formed by samples hydrolyzed for 6 min, whereas large random aggregates were observed in gels formed by samples hydrolyzed for 0 min. The study confirmed that inulin promotes noncovalent bond formation in samples hydrolyzed for 3 min with a 1:4 inulin ratio, shown by an ∼18% increased protein solubility in urea. Additionally, collaboration between noncovalent bonds and disulfide linkages stabilized the gel structure, as indicated by further increase in solubility in combination of urea and Dithiothreitol. PRACTICAL APPLICATION: Plant proteins are gaining attention as alternatives to animal proteins. However, they have inferior functionality, which affects their applicability in food products. This investigation aimed to evaluate enzymatic hydrolysis to enhance the structural and functional properties of pea proteins, thus increasing their applicability in the food industry. Inulin is an oligosaccharide and soluble fiber, which promotes gut health. Thus, gels combining hydrolyzed pea protein and inulin can serve as a model mixed food system of interest to both the industry and consumers.

摘要

与单一多糖或蛋白质凝胶相比,蛋白质 - 多糖混合物的凝胶化有助于创建各种独特的凝胶体系。这些功能性凝胶的性质在很大程度上依赖于蛋白质 - 多糖相互作用的性质、它们的凝胶相容性和机制。使用碱性蛋白酶在三个水解时间(0、3和6分钟)对豌豆分离蛋白分散液(7.5%)进行有限度的酶水解。菊粉与豌豆蛋白按三种比例(0、1:4和2:4)添加。使用振幅扫描和频率扫描测量形成的凝胶的粘弹性性质。振幅扫描的储能模量(G')测量表明,菊粉与豌豆蛋白比例为1:4且水解3分钟的样品具有最大凝胶强度,G'值约为307 Pa。不同菊粉比例下,水解0分钟和6分钟的样品的G'值平均分别约为13 Pa和144 Pa。共聚焦激光扫描显微镜显示,水解3分钟的样品形成的凝胶呈现致密网络,而水解6分钟的样品形成的凝胶为开放网络,水解0分钟的样品形成的凝胶中观察到大量随机聚集体。该研究证实,菊粉促进了菊粉与豌豆蛋白比例为1:4且水解3分钟的样品中的非共价键形成,尿素中蛋白质溶解度增加约18%表明了这一点。此外,非共价键和二硫键之间的协同作用稳定了凝胶结构,尿素和二硫苏糖醇联合使用时溶解度进一步增加表明了这一点。实际应用:植物蛋白作为动物蛋白的替代品正受到关注。然而,它们的功能较差,这影响了它们在食品中的适用性。本研究旨在评估酶水解对增强豌豆蛋白结构和功能性质的作用,从而提高其在食品工业中的适用性。菊粉是一种促进肠道健康的低聚糖和可溶性纤维。因此,结合水解豌豆蛋白和菊粉的凝胶可作为食品工业和消费者都感兴趣的混合食品模型体系。

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