Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking

乳状液 咀嚼度 组织谷氨酰胺转胺酶 化学 乳清蛋白 肿胀 的 共价键 二硫键 化学工程 流变学 生物物理学 色谱法 高分子化学 食品科学 酶 材料科学 生物化学 有机化学 复合材料 工程类 生物
作者
Yanli Zhao,Shiqi Xue,Xinyue Zhang,Tiehua Zhang,Xue Shen
出处
期刊:Gels [Multidisciplinary Digital Publishing Institute]
卷期号:7 (3): 135-135 被引量:23
标识
DOI:10.3390/gels7030135
摘要

This study investigated the effects of high-intensity ultrasound (HUS) and transglutaminase pretreatment on the gelation behavior of whey protein soluble aggregate (WPISA) emulsions. HUS pretreatment and TGase-mediated cross-linking delayed the onset of gelation but significantly increased (p < 0.05) the gel firmness (G′) both after gel formation at 25 °C and during storage at 4 °C. The frequency sweep test indicated that all gels had a similar frequency dependence at 4 and 25 °C, and the elasticity and viscosity of the WPISA-stabilized emulsion gel were significantly enhanced by HUS pretreatment and TGase-mediated cross-linking (p < 0.05). HUS and TGase-mediated cross-linking greatly improved the textural properties of WPISA-stabilized emulsion gels, as revealed by their increases in gel hardness, cohesiveness, resilience, and chewiness. HUS pretreatment and TGase-mediated cross-linking significantly increased the water-holding capacity but decreased the swelling ratios of the gels (p < 0.05). Interactive force analysis confirmed that noncovalent interactions, disulfide bonds, and TGase-induced covalent cross-links were all involved in the formation of gel networks. In conclusion, the combination of HUS and TGase-mediated cross-linking were beneficial for improving the gelation properties of WPISA-stabilized emulsion as a controlled release vehicle for potential food industrial applications.
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