Entity

Time filter

Source Type

Palmerston North, New Zealand

Anema S.G.,Fonterra Research Center | De Kruif C.G.,University Utrecht
Journal of Agricultural and Food Chemistry | Year: 2013

Casein micelles with bound lactoferrin or lysozyme were fractionated into sizes ranging in radius from ∼50 to 100 nm. The κ-casein content decreased markedly and the αS-casein/β-casein content increased slightly as micelle size increased. For lactoferrin, higher levels were bound to smaller micelles. The lactoferrin/κ-casein ratio was constant for all micelle sizes, whereas the lactoferrin/αS- casein and lactoferrin/β-casein ratio decreased with increasing micelle size. This indicates that the lactoferrin was binding to the surface of the casein micelles. For lysozyme, higher levels bound to larger casein micelles. The lysozyme/αS-casein and lysozyme/β-casein ratios were nearly constant, whereas the lysozyme/κ-casein ratio increased with increasing micelle size, indicating that lysozyme bound to αS- casein and β-casein in the micelle core. Lactoferrin is a large protein that cannot enter the casein protein mesh; therefore, it binds to the micelle surface. The smaller lysozyme can enter the protein mesh and therefore binds to the more charged αS-casein and β-casein. © 2013 American Chemical Society. Source


Anema S.G.,Fonterra Research Center | De Kruif C.G.,University Utrecht
Biomacromolecules | Year: 2011

On addition of lactoferrin (LF) to skim milk, the turbidity decreases. The basic protein binds to the caseins in the casein micelles, which is then followed by a (partial) disintegration of the casein micelles. The amount of LF initially binding to casein micelles follows a Langmuir adsorption isotherm. The kinetics of the binding of LF could be described by first-order kinetics and similarly the disintegration kinetics. The disintegration was, however, about 10 times slower than the initial adsorption, which allowed investigating both phenomena. Kinetic data were also obtained from turbidity measurements, and all data could be described with one equation. The disintegration of the casein micelles was further characterized by an activation energy of 52 kJ/mol. The initial increase in hydrodynamic size of the casein micelles could be accounted for by assuming that it would go as the cube root of the mass using the adsorption and disintegration kinetics as determined from gel electrophoresis. The results show that LF binds to casein micelles and that subsequently the casein micelles partly disintegrate. All micelles behave in a similar manner as average particle size decreases. Lysozyme also bound to the casein micelles, and this binding followed a Langmuir adsorption isotherm. However, lysozyme did not cause the disintegration of the casein micelles. © 2011 American Chemical Society. Source


Anema S.G.,Fonterra Research Center
Journal of Agricultural and Food Chemistry | Year: 2012

The effect of milk concentration (10-40% TS) on the kinetics of the pressure-induced denaturation of β-lactoglobulin (β-LG) was studied. The denaturation was found to be a second-order process at all milk concentrations and pressures. There was a change in pressure dependence of the rate constants for denaturation at about 300 MPa, and this effect became more pronounced as the milk concentration increased. At pressures ≥300 MPa, a small effect of milk concentration was observed, with small decreases in the rate of denaturation as the milk concentration was increased above 20% TS. This was attributed to the lower pH as the milk concentration was increased. In contrast, at 200 MPa, β-LG denaturation was markedly retarded as the milk solids concentration was increased. This was attributed to the increased lactose concentration at higher milk concentrations. This would promote β-LG dimerization at this pressure and this would stabilize the β-LG to denaturation. © 2012 American Chemical Society. Source


Dalbeth N.,University of Auckland | Palmano K.,Fonterra Research Center
Current Rheumatology Reports | Year: 2011

Dietary modification is frequently recommended for patients with gout. Longitudinal observational studies have shown a clear inverse relationship between low-fat dairy intake and gout risk. Several checkpoints in gout pathogenesis may be targeted by dairy intake. Cross-sectional and short-term intervention studies of healthy volunteers have demonstrated that low-fat dairy intake has a moderate urate-lowering effect. In addition, certain dairy fractions, particularly glycomacropeptide and G600 milk fat extract, have anti-inflammatory properties in experimental models of acute gout. Such anti-inflammatory properties may contribute to the reduction in gout risk through inhibition of the inflammatory response to monosodium urate crystals within the joint. Well-controlled intervention studies in patients with gout are now needed to determine the clinical relevance of these observations in order to guide dietary recommendations for this disease. © 2010 Springer Science+Business Media, LLC. Source


Kelly W.J.,Agresearch Ltd. | Ward L.J.H.,Fonterra Research Center | Leahy S.C.,Agresearch Ltd.
Genome Biology and Evolution | Year: 2010

A large collection of Lactococcus lactis strains, including wild-type isolates and dairy starter cultures, were screened on the basis of their phenotype and the macrorestriction patterns produced from pulsed-field gel electrophoresis (PFGE) analysis of SmaI digests of genomic DNA. Three groups of dairy starter cultures, used for different purposes in the dairy industry, and a fourth group made up of strains isolated from the environment were selected for analysis of their chromosomal diversity using the endonuclease I-CeuI. Chromosome architecture was largely conserved with each strain having six copies of the rRNA genes, and the chromosome size of individual strains ranged between 2,240 and 2,688 kb. The origin of L. lactis strains showed the greatest correlation with chromosome size, and dairy strains, particularly those with the cremoris phenotype, had smaller chromosomes than wild-type strains. Overall, this study, coupled with analysis of the sequenced L. lactis genomes, provides evidence that defined strain dairy starter cultures have arisen from plant L. lactis strains. Adaptation of these strains to the dairy environment has involved loss of functions resulting in smaller chromosomes and acquisition of genes (usually plasmid associated) that facilitate growth in milk. We conclude that dairy starter cultures generally and the industrially used cremoris and diacetylactis phenotype strains in particular comprise a specialized group of L. lactis strains that have been selected to become an essential component of industrial processes and have evolved accordingly, so that they are no longer fit to survive outside the dairy environment. © The Author(s) 2010. Source

Discover hidden collaborations