Unaided efficient transglutaminase cross-linking of whey proteins strongly impacts the formation and structure of protein alginate particles

IF 4.1 Q2 FOOD SCIENCE & TECHNOLOGY
Mikkel Madsen , Sanaullah Khan , Sonja Kunstmann , Finn L. Aachmann , Richard Ipsen , Peter Westh , Cecilia Emanuelsson , Birte Svensson
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引用次数: 3

Abstract

There is a dogma within whey protein modification, which dictates the necessity of pretreatment to enzymatic cross-linking of β-lactoglobulin (β-Lg). Here microbial transglutaminase (MTG) cross-linked whey proteins and β-Lg effectively in 50 mM NaHCO3, pH 8.5, without pretreatment. Cross-linked β-Lg spanned 18 to >240 kDa, where 6 of 9 glutamines reacted with 8 of 15 lysines. The initial isopeptide bond formation caused loss of β-Lg native structure with t1/2 = 3 h, while the polymerization occurred with t1/2 = 10 h. Further, cross-linking effects on protein carbohydrate interaction have been overlooked, leaving a gap in understanding of these complex food matrices. Complexation with alginate showed that β-Lg cross-linking decreased onset of particle formation, hydrodynamic diameter, stoichiometry (β-Lg/alginate) and dissociation constant. The complexation was favored at higher temperatures (40 °C), suggesting that hydrophobic interactions were important. Thus, β-Lg was cross-linked without pretreatment and the resulting polymers gave rise to altered complexation with alginate.

Abstract Image

乳清蛋白的无辅助高效转谷氨酰胺酶交联强烈影响海藻酸蛋白颗粒的形成和结构
在乳清蛋白修饰中有一个教条,它规定了酶交联β-乳球蛋白(β-Lg)的预处理的必要性。在这里,微生物转谷氨酰胺酶(MTG)在50 mM NaHCO3, pH 8.5中有效地交联乳清蛋白和β-Lg,无需预处理。交联的β-Lg跨越18至240 kDa,其中9种谷氨酰胺中的6种与15种赖氨酸中的8种发生反应。最初的异肽键形成导致β-Lg天然结构在t1/2 = 3 h时丢失,而在t1/2 = 10 h时发生聚合。此外,交联对蛋白质-碳水化合物相互作用的影响被忽视,这使得对这些复杂食物基质的理解存在空白。与海藻酸盐络合表明,β-Lg交联降低了颗粒形成的起始时间、水动力直径、化学计量(β-Lg/海藻酸盐)和解离常数。在较高的温度下(40°C)络合更有利,这表明疏水相互作用是重要的。因此,β-Lg无需预处理就交联,所得聚合物与海藻酸盐的络合作用发生了改变。
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来源期刊
Food Chemistry Molecular Sciences
Food Chemistry Molecular Sciences Agricultural and Biological Sciences-Food Science
CiteScore
6.00
自引率
0.00%
发文量
83
审稿时长
82 days
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