Casein and casein micelle structures, functions and diversity in 20 species

Primary structures of caseins from 20 species, including two monotremes and two marsupials, have been compared. Sequences of the mature proteins are very divergent, whereas variation in amino acid composition is mostly restricted to a range of disorder-promoting residues. The number and size of clusters of phosphorylation sites in the caseins is variable, blurring the boundaries between them. Casein polar tract sequences were found in all caseins, though of variable lengths, and are chiefly responsible for weak and dynamic interactions among the tangled web of peptide chains in the matrix of casein micelles. The interactions take the predominant form of backbone-to-backbone contacts rather than the sequence-specific side chain interactions of the hydrophobic effect. It is suggested that the dynamic casein micelle matrix be represented by an ensemble of interchanging structures with different types and degrees of inhomogeneity, influenced by solvent quality and other environmental factors

A review of the biology of calcium phosphate sequestration with special reference to milk

In milk, a stable fluid is formed in which sequestered nanoclusters of calcium phosphate are substructures in casein micelles. As a result, calcium and phosphate concentrations in milk can be far in excess of their solubility. Variations of calcium, phosphate and casein concentrations in milks, both within and among species, are mainly due to the formation of the nanocluster complexes. Caseins evolved from tooth and bone proteins well before the evolution of lactation. It has therefore been suggested that the role of caseins in milk is an adaptation of an antecedent function in the control of some aspect of biomineralisation. There is new evidence that nanocluster-type complexes are also present in blood serum and, by implication, in many other closely related biofluids. Because such fluids are stable but nevertheless supersaturated with respect to the bone and tooth mineral hydroxyapatite, they allow soft and mineralised tissues to co-exist in the same organism with relative ease. An appreciable concentration of nanocluster complexes exists in fresh saliva. Such saliva may stabilise tooth mineral and help to repair demineralised lesions. In the extracellular matrix of bone, nanocluster complexes may be involved in directing the amorphous calcium phosphate to intrafibrillar spaces in collagen where they can mature into oriented apatite crystals. Thus, evidence is accumulating that calcium phosphate sequestration by phosphopeptides to form equilibrium complexes, first observed in milk, is more generally important in the control of physiological calcification

Letter to the Editor: a response to Horne and Lucey (2017)

No abstract available

Structural studies of hydrated samples of amorphous calcium phosphate and phosphoprotein nanoclusters

There are abundant examples of nanoclusters and inorganic microcrystals in biology. Their study under physiologically relevant conditions remains challenging due to their heterogeneity, instability, and the requirements of sample preparation. Advantages of using neutron diffraction and contrast matching to characterize biomaterials are highlighted in this article. We have applied these and complementary techniques to search for nanocrystals within clusters of calcium phosphate sequestered by bovine phosphopeptides, derived from osteopontin or casein. The neutron diffraction patterns show broad features that could be consistent with hexagonal hydroxyapatite crystallites smaller than 18.9 Å. Such nanocrystallites are, however, undetected by the complementary X-ray and FTIR data, collected on the same samples. The absence of a distinct diffraction pattern from the nanoclusters supports the generally accepted amorphous calcium phosphate structure of the mineral core

Effects of antimicrobial addition on lipid oxidation of rendered chicken fat

This study evaluated the effects of antimicrobial acidulant addition on lipid oxidation of rendered chicken fat. Chicken fat was untreated (control) or treated with either sodium bisulfate (SBS) or lactic acid (LA) at 0.5% w/w and incubated for 6 wk at 40 °C. Peroxide value (PV), p-anisidine value (AV), and free fatty acid (FFA) levels were measured at days 0 (D0), 1(D1), 3 (D3), 5 (D5), and 7 (D7), and weeks 2 (W2), 3 (W3), 4 (W4), 5 (W5), and 6 (W6). The FFA level of untreated-control fat was ~7% and remained consistent throughout the incubation until W6 (~8.5%; P \u3c 0.05). The FFA values in SBS-treated fat were constant (range 7.25%–8.30%) throughout the incubation, whereas the FFA in LA-treated fat peaked at W5 (9.3%; P \u3c 0.05). For the control fat, PVs were between 0.56 and 0.67 meq/100 g until W1 then declined. For the SBS-treated fat, the PVs remained low and similar to the control with the exception of a slight increase on W4 to 0.38 meqv/100 g (P \u3c 0.05). In the LA-treated fat, the PV was greater than (P \u3c 0.05) the control from W1 and increased to a peak on W5 (2.52 meq/100 g). The AV of control fat averaged 2.12 at D0 and increased through W2. In control and LA-treated fat, the AV values declined slightly thereafter, whereas SBS-treated fat increased (P \u3c 0.05) to 10.28 on W5. This study indicates that when included at antimicrobial effective levels, LA may reduce the shelf-life of chicken fat, but SBS had a minimal effect over 6 wk of storage