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冷超滤或微滤牛奶截留物:组成差异对其胶凝功能影响的系统比较。

Cold ultrafiltered or microfiltered milk retentates: A systematic comparison of the effects of compositional differences on their gelation functionality.

机构信息

Department of Food Science, CiFood Multidisciplinary Center for Innovative Foods, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark.

Department of Food Science, CiFood Multidisciplinary Center for Innovative Foods, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark.

出版信息

J Dairy Sci. 2023 May;106(5):3123-3136. doi: 10.3168/jds.2022-22497. Epub 2023 Mar 29.

DOI:10.3168/jds.2022-22497
PMID:37002138
Abstract

The colloidal stability of casein micelles suspensions prepared using ultrafiltration (UF) and microfiltration (MF) was studied by testing acid- and rennet-induced destabilization. Skim milk and 4× (based on volume reduction) concentrates were obtained by processing under similar conditions, at temperatures below 10°C. Concentrates were subjected to different levels of diafiltration (DF), resulting in samples with comparable casein volume fractions but different amounts of proteins and ions in the serum phase. The novelty of the work is the systematic comparison of MF and UF concentrates of similar history. More specifically, concentrates similar in ionic composition but with or without serum proteins were compared, to evaluate whether whey proteins and β-casein depletion from the micelles will play a role in the processing properties, or whether these are affected solely by the ionic balance. Microfiltered micelles' apparent diameter decreased by about 50 nm during the specific hydrolysis of κ-casein by chymosin, whereas those in skim milk control showed a decrease of about half that size. All concentrates subjected to extensive DF showed smaller hydrodynamic diameters, with reductions of ∼18 and 13 nm for MF and UF, respectively. Highly diafiltered UF retentates showed a delayed onset of rennet-induced gelation, due to low colloidal calcium, compared with other samples. Low-diafiltered samples showed weak storage modulus (∼1 Pa) after 60 min of onset of gelation. In addition, onset pH increased with diafiltration to ∼5.8 for UF and ∼6 for MF in high-diafiltered samples. These results clearly demonstrated that the functional properties of casein micelles change during membrane concentration, and this cannot be solely attributed to changes in ionic equilibrium.

摘要

使用超滤(UF)和微滤(MF)制备的酪蛋白胶束悬浮液的胶体稳定性通过测试酸和凝乳酶诱导的失稳来研究。在低于 10°C 的温度下,在类似的条件下加工脱脂乳和 4 倍(基于体积减少)浓缩物。浓缩物经过不同程度的渗滤(DF),得到具有可比酪蛋白体积分数但血清相中蛋白质和离子量不同的样品。这项工作的新颖之处在于对具有相似历史的 MF 和 UF 浓缩物进行系统比较。更具体地说,比较了具有相似离子组成但含有或不含乳清蛋白的浓缩物,以评估乳清蛋白和β-酪蛋白从胶束中的耗尽是否会对加工性能产生影响,或者这些是否仅受离子平衡的影响。微滤胶束的表观直径在凝乳酶特异性水解κ-酪蛋白期间减小了约 50nm,而脱脂乳对照中的胶束直径减小了约一半。所有经过大量 DF 的浓缩物均表现出较小的水动力直径,MF 和 UF 分别减小了约 18nm 和 13nm。与其他样品相比,高度渗滤 UF 保留物由于胶体钙含量低,表现出凝乳酶诱导凝胶形成的起始延迟。低渗滤样品在凝胶形成起始后 60 分钟显示出较弱的储能模量(约 1Pa)。此外,在高渗滤样品中,渗滤使起始 pH 值增加到 UF 的约 5.8 和 MF 的约 6。这些结果清楚地表明,在膜浓缩过程中,酪蛋白胶束的功能性质发生变化,这不能仅仅归因于离子平衡的变化。

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