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转谷氨酰胺酶在 NaSO 存在下催化磷酸化麦醇溶蛋白-小麦谷蛋白复合物的形成、交联行为及乳化性质。

Phosvitin-wheat gluten complex catalyzed by transglutaminase in the presence of NaSO: Formation, cross-link behavior and emulsifying properties.

机构信息

College of Food Science and Engineering, Northwest A&F University, Yangling 712100, PR China.

Department of Food Science and Technology, Shanghai Jiao Tong University, Shanghai 200240, PR China.

出版信息

Food Chem. 2021 Jun 1;346:128903. doi: 10.1016/j.foodchem.2020.128903. Epub 2020 Dec 24.

DOI:10.1016/j.foodchem.2020.128903
PMID:33429299
Abstract

Phosvitin (PSV) is considered as a good emulsifier, although it has a low proportion of hydrophobic regions and steric hindrance. Wheat gluten (WG) possesses excellent hydrophobicity and macromolecular network structure. In this work, WG was subjected to a series of NaSO solution, followed by cross-linking with PSV under transglutaminase (TGase) catalyzation. The results showed that NaSO could break disulfide bonds of WG and increase its solubility from 7.33% to 42.82% with 1200 mg/L of NaSO. Correspondingly, the cross-linking degree was significantly enhanced. Compared to PSV, the cross-linked PSV-WG exhibited a higher surface hydrophobicity and thermal stability, with a lower zeta potential and apparent viscosity. The emulsifying activity of PSV-WG reached 17.42, 20.63 and 20.28 m/g with NaSO concentration of 300, 600 and 900 mg/L, which were all higher than that of PSV (15.19 m/g). This work provided a novel strategy to elevate emulsifying properties of PSV by cross-link reaction.

摘要

磷酸化蛋白(PSV)被认为是一种良好的乳化剂,尽管它的疏水区比例和空间位阻较低。小麦面筋(WG)具有极好的疏水性和高分子网络结构。在这项工作中,WG 经过一系列的亚硫酸钠溶液处理,然后在转谷氨酰胺酶(TGase)催化下与 PSV 进行交联。结果表明,亚硫酸钠可以打断 WG 的二硫键,将其溶解度从 7.33%提高到 42.82%,亚硫酸钠的浓度为 1200mg/L。相应地,交联程度显著增强。与 PSV 相比,交联的 PSV-WG 具有更高的表面疏水性和热稳定性,较低的 Zeta 电位和表观黏度。在亚硫酸钠浓度为 300、600 和 900mg/L 时,PSV-WG 的乳化活性分别达到 17.42、20.63 和 20.28m/g,均高于 PSV(15.19m/g)。这项工作提供了一种通过交联反应提高 PSV 乳化性能的新策略。

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