A possible structure of the casein micelle based on high-resolution field-emission scanning electron microscopy

New electron micrographs, produced using the technique of Field Emission Scanning Electron Microscopy, showing the details of the micellar surface, are presented. The images show the micellar surfaces without any coating, and suggest that the surface of the micelle may have a much more complex structure than has previously been demonstrated. Although there appear to be no spherical subunits (submicelles), there is evidence for the organization of the caseins into tubular structures within the micelle. The surface is not smooth, and contains gaps between the substructures. The observations are discussed in terms of published models of micellar structure, where is it suggested how the depiction of the micellar surface can be used to explain certain factors of its reactivity and behaviour.     

Casein glycomacropeptide pH-driven self-assembly and gelation upon heating

Casein glycomacropeptide (CMP) found in cheese whey is a C-terminal hydrophilic glycopeptide released from κ-casein by the action of chymosin during cheese making. In a previous work a self-assembly model for CMP at room temperature was proposed, involving a first step of hydrophobic assembly followed by a second step of electrostatic interactions which occurs below pH 4.5. The objective of the present work was to study, by dynamic light scattering (DLS), the effect of heating (35–85 °C) on the pH-driven CMP self-assembly and its impact on the dynamics of CMP gelation. The concentration of CMP was 3% w/w for DLS and 12% w/w for rheological measurements. The solutions at pH 4.5 and 6.5 did not show any change in the particle size distributions upon heating. In contrast the solutions at pH lower than 4.5 that showed electrostatic self-assembly at room temperature were affected by heating. The mean diameter of assembled CMP increased by decreasing pH. For all solutions with pH lower than 4.5, the particle size did not change on cooling, suggesting that the assembled CMP forms formed during heating were stable. The gel point determined as G′–G″ crossover, occurred in all systems at 70 °C, but at different times. The rate of self-assembly determined by DLS as well as the rate of gelation increased with increasing temperature and decreasing pH from 4 to 2. Increasing temperature and decreasing pH, the first step of CMP self-assembly by hydrophobic interactions is speed out. All the self-assembled structures and the gels formed at different temperatures were pH-reversible but did not revert to the initial size (monomer) but to associated forms that correspond mainly to CMP dimers.     

酪朊胶粘贴啤酒商标耐水性的研究

本文对酪朊胶粘贴的啤酒商标的耐水性进行了较系统的研究。试验证明其耐水性与酚朊胶组分、贴标时胶的用量、贴标质量、贴标后放置的时间以及商标本身的质量等各因素有关．在具有较好耐水性的酪朊胶的基础上保持一定的上胶量（78.5cm2珠啤普通标，250mg左右），胶上得均匀，标贴得平整，贴标后放置十天左右，再在约5℃冰水中冷冻，商标就能在72小时内不自行脱落．     

Development of highly soluble and functional buffalo milk protein concentrate 60 by modifying ionic environment and characterisation thereof

The ionic and protein environment of buffalo skim milk was modified by instant pH drop and its restoration for the development of highly soluble milk protein concentrate-60 (BuMRate–60^@), which resulted in depletion of 88.64% calcium, 89.18% magnesium, 91.69% potassium and 93.96% phosphorous. BuMRate–60^@ displayed excellent wetting, rehydration and solubility (97.76%). The Fourier transform infrared spectrometer spectra revealed significant stretching (C-H and O-H), N-H bending and a large extent of H-bonding. Scanning electron microscopy micrographs presented particles with porous nature and dimples, while transmission electron microscopy confirmed a greater release of minerals with altered casein micelles.     

Comparison of pH-dependent sonodisruption of re-assembled casein micelles by 35 and 130 kHz ultrasounds

Sonodisruption behavior of re-assembled casein micelles was compared at two ultrasound frequencies (35 and 130 kHz) by turbidity measurement and laser-diffraction based particle size analysis. Sonochemical ultrasound (130 kHz) was more effective than power ultrasound (35 kHz) in micelle disruption. This was attributed to the higher strain rates generated upon implosion of cavities, as well as the liberation of more free radicals to the surrounding medium. The higher the pH of solution, the more effective was the ultrasonic disruption due to a looser expanded assembly of particles at higher pH values. Sonochemical ultrasound decreased the consistency coefficient of casein solutions and increased their flow index except at a pH value of 6.35, while power ultrasound did not affect the flow behavior of solutions across the whole pH range.     

Rehydration process of milk protein concentrate powder monitored by static light scattering

Static light scattering (SLS) was applied to monitor the rehydration process of milk protein concentrate (MPC) powder. The size distribution and volume concentration of the suspended powder particles were measured to quantify the dissolution kinetics of MPC powder. The results obtained showed that the low solubility index reported for MPC85 (85% protein) powder at room temperature was the consequence of slow dissolution kinetics rather than the presence of a large amount of insoluble material in the rehydrated powder. The rehydration process of MPC85 powder occurs in two overlapping steps: the disruption of agglomerated particles into primary powder particles and, simultaneously, the release of material from the powder particles into the surrounding aqueous phase. The latter process appeared to be the rate-limiting step of dissolution of MPC85 and was accelerated by an increase of the solvent temperature.     

酪蛋白磷酸肽的体外功能试验

对不同级别的酪蛋白磷酸肽（Casein Phosphopeptide,以下简称CPP）促进钙吸收的体外功能性质进行了研究,测定了CPP的结合钙量、CPP阻止磷酸钙沉淀形成的效果及持钙能力.结果表明CPP对钙的结合量随温度的升高而减少,随pH值的升高而增加;CPP对阻止磷酸钙沉淀的作用随温度升高和溶液钙磷比增加而下降;随氮磷摩尔比降低,CPP阻止磷酸钙沉淀形成的最低有效浓度下降;对于不同的钙磷比,CPP的氮磷摩尔比越小,保持在溶液中的钙量越多,但每摩尔磷保持钙的摩尔数随氮磷摩尔比的降低而降低.     

UHT milk contains multiple forms of αS1-casein that undergo degradative changes during storage

Milk proteins are susceptible to chemical changes during processing and storage. We used proteomic tools to analyse bovine α_S1-casein in UHT milk. 2-D gels of freshly processed milk α_S1-casein was presented as five or more spots due to genetic polymorphism and variable phosphorylation. MS analysis after phosphopeptide enrichment allowed discrimination between phosphorylation states and genetic variants. We identified a new alternatively-spliced isoform with a deletion of exon 17, producing a new C-terminal sequence, K¹⁶⁴SQVNSEGLHSYGL¹⁷⁷, with a novel phosphorylation site at S¹⁷⁴. Storage of UHT milk at elevated temperatures produced additional, more acidic α_S1-casein spots on the gels and decreased the resolution of minor forms. MS analysis indicated that non-enzymatic deamidation and loss of the N-terminal dipeptide were the major contributors to the changing spot pattern. These results highlight the important role of storage temperature in the stability of milk proteins and the utility of proteomic techniques for analysis of proteins in food.     

Polyethylene/Polycaprolactone Nanocomposite Films for Food Packaging Modified with Magnetite and Casein: Oxygen Barrier,Mechanical, and Thermal Properties

Polyethylene (PE) was modified and prepared as double-layer polyethylene/polycaprolactone (PE/PCL) film. Magnetite and casein were added to the PCL-coating film to improve barrier properties and prevent destruction of basic structure of primary polymer PE. Significant improvements were observed with regards to mechanical (tensile strength, elongation at break) and thermal properties, while barrier (O₂ permeability) properties were slightly improved. Overall migration values into acetic acid were lower (from 1 to 4.6 mg/dm²) than the upper limit set by the legislation. Specific migration of iron in PE/PCL-Fe samples is also below (µg/L) specific migration limit value set by the legislation (mg/kg).