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胶束酪蛋白粉末的增强复水行为:高静压处理对胶束结构的影响。

Enhanced rehydration behaviors of micellar casein powder: The effects of high hydrostatic pressure treatments on micelle structures.

机构信息

College of Food Science and Nutritional Engineering, National Engineering Research Center for Fruit and Vegetable Processing, China Agricultural University, Key Lab of Fruit and Vegetable Processing, Ministry of Agriculture and Rural Affairs, Beijing 100083, China.

Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland.

出版信息

Food Res Int. 2021 Dec;150(Pt A):110797. doi: 10.1016/j.foodres.2021.110797. Epub 2021 Nov 2.

DOI:10.1016/j.foodres.2021.110797
PMID:34865812
Abstract

Natural micellar casein is generally dried into powdered forms for commercial transportation and storage. However, the poor rehydration ability of micellar casein powder critically limited the potential applications due to its dense cross-linked structures caused by colloidal calcium phosphate (CCP). In this study, micellar casein solutions were exposed to a high hydrostatic pressure (HHP) ranging from 100 to 500 MPa and were then freeze dried to produce powders. The effects on the casein micelle structures and the rehydration characteristics including wetting, dispersion and dissolving were comprehensively investigated. The results showed that HHP could induce smaller micelle sizes and significantly increase the free calcium in the reconstituted solution. It demonstrated that the majority of CCP bridges in casein micelles were dissociated, which produced porous powders with loose structures and thus significantly improved rehydration behaviors. 300 MPa was the pressure level that caused the quickest dispersion process and best solubility. Consequently, HHP has potential to be a novel physical technique to potentially modify the protein higher-order structures as well as improve the corresponding functionalities.

摘要

天然胶束酪蛋白通常被干燥成粉末形式,以进行商业运输和储存。然而,由于胶束酪蛋白粉末的致密交联结构(由磷酸钙胶体引起),其再水合能力很差,严重限制了其潜在应用。在这项研究中,胶束酪蛋白溶液在 100 至 500 MPa 的高压(HHP)下进行处理,然后进行冷冻干燥以产生粉末。全面研究了对酪蛋白胶束结构的影响以及再水合特性,包括润湿、分散和溶解。结果表明,HHP 可以诱导较小的胶束尺寸,并显著增加复溶溶液中的游离钙。这表明胶束中大多数 CCP 桥接都已解离,从而产生具有疏松结构的多孔粉末,因此显著改善了再水合行为。300 MPa 是导致最快分散过程和最佳溶解度的压力水平。因此,HHP 有可能成为一种新型物理技术,可潜在地改变蛋白质的高级结构,并改善其相应的功能。

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