Impact of shear and pH on properties of casein micelles in milk protein concentrate

被引：19

作者：

Ranadheera, C. S. ^{[1
,2
,3
]}

Liyanaarachchi, W. S. ^{[1
,2
]}

Dissanayake, M. ^{[1
,2
]}

Chandrapala, J. ^{[1
,2
,4
]}

Huppertz, T. ^{[1
,2
,5
]}

Vasiljevic, T. ^{[1
,2
]}

机构：

[1] Victoria Univ, Inst Sustainable Ind & Liveable Cities, Adv Food Syst Res Unit, Werribee, Vic 3030, Australia

[2] Victoria Univ, Coll Hlth & Biomed, Werribee, Vic 3030, Australia

[3] Univ Melbourne, Fac Vet & Agr Sci, Sch Agr & Food, Melbourne, Vic 3010, Australia

[4] RMIT Univ, Sch Sci, Bundoora, Vic 3083, Australia

[5] FrieslandCampina, Amersfoort, Netherlands

来源：

LWT-FOOD SCIENCE AND TECHNOLOGY | 2019年 / 108卷

关键词：

Casein micelle; Shear; Low pH; Aggregation; Dissociation; WHEY PROTEINS; FUNCTIONAL-PROPERTIES; AGGREGATION; TEMPERATURE; BEHAVIOR; MODEL;

D O I：

10.1016/j.lwt.2019.03.090

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Properties of casein micelles can be manipulated by changing environmental conditions, which leads to formation of particles of varying sizes with different physical properties. This study evaluated the impact of shear (100 and 1000 s(-1)) on the properties of casein micelles in milk protein concentrate in the pH range 2.0-7.5. Casein micelle size was not affected by shear at pH 6.7 or 7.5, whereas casein aggregates, which were formed at pH 4.6 and 2.0, had their size considerably reduced upon high shearing. The composition of the soluble phase was dependent on pH as increased concentrations of beta-casein and alpha(s)-caseins were found at pH 4.6 and pH 2, respectively. Greatest dissociation of individual caseins from the micelle occurred at pH 2.0. These serum caseins appeared in a form of fairly small soluble aggregates mainly consisting of alpha(s)- and beta-caseins. The composition of aggregates varied with applied shear, indicating orthokinetic aggregation and fragmentation.

引用

页码：370 / 376

页数：7

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