Size of native and heated casein micelles, content of protein and minerals in milk from Norwegian Red Cattle—effect of milk protein polymorphism and different feeding regimes

AbstractThe objective of this work was to evaluate the impact of changes during membrane filtration on the heat stability of milk protein concentrates. Dairy protein concentrates have been widely employed in high protein drinks formulations and their stability to heat treatment is critical to ensure quality of the final product. Pasteurized milk was concentrated three-fold by membrane filtration, and the ionic composition was modified by addition of water or permeate from filtration (diafiltration). Diafiltration with water did not affect the apparent diameter of the casein micelles, but had a positive effect on heat coagulation time (HCT), which was significantly longer (50 min), compared to the non diafiltered concentrates (about 30 min). UHT treatments increased the particle size of the casein micelles, as well as the turbidity of retentates. Differences between samples with and without diafiltration were confirmed throughout further analysis of the protein composition of the unsedimentable fraction, highlighting the importance of soluble protein composition on the processing functionality of milk concentrates.

Download Full-text

Structure of casein micelles in milk protein concentrate powders via small angle X-ray scattering

Soft Matter ◽

10.1039/c0sm01010c ◽

2011 ◽

Vol 7 (8) ◽

pp. 3837 ◽

Cited By ~ 35

Author(s):

Jitendra P. Mata ◽

Punsandani Udabage ◽

Elliot P. Gilbert

Keyword(s):

Small Angle ◽

Milk Protein ◽

Protein Concentrate ◽

Casein Micelles ◽

Milk Protein Concentrate ◽

X Ray ◽

X Ray Scattering ◽

Ray Scattering

Download Full-text

Effect of calcium sequestration by ion-exchange treatment on the dissociation of casein micelles in model milk protein concentrates

Food Hydrocolloids ◽

10.1016/j.foodhyd.2016.03.026 ◽

2016 ◽

Vol 60 ◽

pp. 59-66 ◽

Cited By ~ 19

Author(s):

Yuting Xu ◽

Dasong Liu ◽

Hongxu Yang ◽

Jie Zhang ◽

Xiaoming Liu ◽

...

Keyword(s):

Ion Exchange ◽

Milk Protein ◽

Casein Micelles ◽

Protein Concentrates ◽

Calcium Sequestration

Download Full-text

MILK PROTEIN POLYMORPHISM IN SUDANESE DAIRY CATTLE BREEDS

Assiut Veterinary Medical Journal ◽

10.21608/avmj.2010.173819 ◽

2010 ◽

Vol 56 (124) ◽

pp. 1-9

Keyword(s):

Dairy Cattle ◽

Milk Protein ◽

Protein Polymorphism ◽

Cattle Breeds

Download Full-text

Characteristics of Phase Behavior Transformation of Milk Protein-Polysaccharide Multicomponent Systems with κ-Carrageenan

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.781-784.1589 ◽

2013 ◽

Vol 781-784 ◽

pp. 1589-1594

Author(s):

Qing Qing Liu ◽

Ya Li Peng ◽

Fei Hu

Keyword(s):

Weight Loss ◽

Phase Separation ◽

Phase Behavior ◽

Milk Protein ◽

Rheological Characteristics ◽

Multicomponent Systems ◽

Spherical Micelle ◽

Casein Micelles ◽

Discrete Phase ◽

High Degree

To meet the needs of consumers desiring for weight-loss food, investigation on phase characteristics of milk protein-konjac glucomannan multicomponent systems with κ-carrageenan was carried out to simulate healthy ice cream product. Methods of rheology, light scattering and microscopy were used to examine the mechanism underlying the transformation of phase behavior. Addition of κ-carrageenan (0%) evidently showed extensive phase separation that casein micelles concentrated into an irregular discrete phase. A high degree of emulsification of spherical micelle droplets occurring in the continuous serum phase prevented bulk phase separation when the κ-carrageenan concentration increased (0.025%, 0.05%). The analysis of rheological characteristics revealed that multicomponent systems with higher κ-carrageenan concentration were more viscous and showed higher thixotropy behavior due to intense interactions between κ-carrageenan and casein micelles. Frequency independence of G and G was also greatly enhanced as concentration of κ-carrageenan increased. Moreover, differences of size distribution evidenced the structure formation of systems in presence of κ-carrageenan. The joint effects of κ-carrageenan helix aggregation and the interaction between casein micelles and κ-carrageenan were contributed to phase behavior transformation.

Download Full-text

Restrained molecular dynamics investigation of the differences in association of chymosin to κ-caseins A and C

Journal of Dairy Research ◽

10.1017/s0022029996002117 ◽

1997 ◽

Vol 64 (2) ◽

pp. 299-304 ◽

Cited By ~ 7

Author(s):

JEFFREY E. PLOWMAN ◽

LAWRENCE K. CREAMER ◽

MARK H. SMITH ◽

JEREMY P. HILL

Keyword(s):

Molecular Dynamics ◽

Whey Protein ◽

Milk Protein ◽

Protein Polymorphism ◽

Micelle Size ◽

Milk Casein ◽

The Relationship ◽

Restrained Molecular Dynamics

There is considerable interest in the relationship between milk protein polymorphism and cheesemaking properties of milk (e.g. Jakob & Puhan, 1992, 1995; Jakob, 1993). For example, the B variant of κ-casein is associated with firmer cheese curds, shorter renneting times, a smaller average micelle size, higher milk casein and κ-casein concentrations and lower whey protein concentrations (Jakob, 1994; Horne et al. 1995).

Download Full-text