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转谷氨酰胺酶诱导的大豆蛋白-麦芽糖乳液凝胶的冻融稳定性:关注形态、质构特性和流变特性。

Freeze-thaw stability of transglutaminase-induced soy protein-maltose emulsion gel: Focusing on morphology, texture properties, and rheological characteristics.

机构信息

Key Laboratory of Soybean Biology of Chinese Education Ministry, Northeast Agricultural University, Harbin 150030, China; College of Food Science, Northeast Agricultural University, Harbin 150030, China.

College of Food Science, Northeast Agricultural University, Harbin 150030, China.

出版信息

Int J Biol Macromol. 2024 Mar;261(Pt 1):129716. doi: 10.1016/j.ijbiomac.2024.129716. Epub 2024 Jan 28.

DOI:10.1016/j.ijbiomac.2024.129716
PMID:38290624
Abstract

In this study, soy protein isolate (SPI) and maltose (M) were employed as materials for the synthesis of a covalent compound denoted as SPI-M. The emulsion gel was prepared by transglutaminase (TGase) as catalyst, and its freeze-thaw stability was investigated. The occurrence of Maillard reaction was substantiated through SDS-PAGE. The analysis of spectroscopy showed that the structure of the modified protein was more stretched, changed in the direction of freeze-thaw stability. After three freeze-thaw cycles (FTC), it was observed that the water holding capacity of SPI-M, SPI/M mixture (SPI+M) and SPI emulsion gels exhibited reductions of 8.49 %, 16.85 %, and 20.26 %, respectively. Moreover, the soluble protein content also diminished by 13.92 %, 23.43 %, and 35.31 %, respectively. In comparison to unmodified SPI, SPI-M exhibited increase in gel hardness by 160 %, while elasticity, viscosity, chewability, and cohesion demonstrated reductions of 17.7 %, 23.3 %, 33.3 %, and 6.76 %, respectively. Concurrently, the SPI-M emulsion gel exhibited the most rapid gel formation kinetics. After FTCs, the gel elastic modulus (G') and viscosity modulus (G″) of SPI-M emulsion were the largest. DSC analysis underscored the more compact structure and heightened thermal stability of the SPI-M emulsion gel. SEM demonstrated that the SPI-M emulsion gel suffered the least damage following FTCs.

摘要

在这项研究中,大豆分离蛋白(SPI)和麦芽糖(M)被用作合成共价化合物的材料,该化合物被表示为 SPI-M。通过转谷氨酰胺酶(TGase)作为催化剂制备乳状凝胶,并研究其冻融稳定性。SDS-PAGE 证实了美拉德反应的发生。光谱分析表明,修饰蛋白的结构更加伸展,朝着冻融稳定性的方向发生了变化。经过三个冻融循环(FTC)后,观察到 SPI-M、SPI/M 混合物(SPI+M)和 SPI 乳状凝胶的持水能力分别降低了 8.49%、16.85%和 20.26%。此外,可溶性蛋白含量也分别减少了 13.92%、23.43%和 35.31%。与未修饰的 SPI 相比,SPI-M 的凝胶硬度增加了 160%,而弹性、粘度、咀嚼性和内聚性分别降低了 17.7%、23.3%、33.3%和 6.76%。同时,SPI-M 乳状凝胶表现出最快的凝胶形成动力学。经过 FTC 后,SPI-M 乳状凝胶的凝胶弹性模量(G')和粘性模量(G″)最大。DSC 分析强调了 SPI-M 乳状凝胶更紧凑的结构和更高的热稳定性。SEM 表明,SPI-M 乳状凝胶在经过 FTC 后受到的损伤最小。

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