PubMed · 16396163
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Lou Graham. 2005. Identifying, diagnosing, and treating dentin hypersensitivity.. https://pubmed.ncbi.nlm.nih.gov/16396163/
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The influence of gamma-irradiation (32 kGy) followed by the addition of polysaccharides (potato starch, soluble potato starch, and sodium alginate) and heating on the properties of the films based on calcium caseinate (CC)-whey proteins isolate (WPI) and the gels formed with CaCl(2) was evaluated. Radiation induced an improvement of the mechanical and barrier properties of all films. The polysaccharides' effect on the irradiated and non-irradiated CC-WPI gels could be predicted as the sum of their separate effects on CC and on WPI, apart from the alginate interaction with the irradiated CC-WPI. The better properties of the films achieved after admixing polysaccharides to the formerly irradiated protein solution correspond to the smaller strength of gels. Properties of the films and gels prepared using the irradiated proteins and alginate differed depending on whether alginate was admixed before or after irradiation. Results were related to the protein structure, interaction with polysaccharides, and the film's microstructure.
A metalloprotease secreted by the moderately halophilic bacterium Salinivibrio sp. strain AF-2004 when the culture reached the stationary growth phase. This enzyme was purified to homogeneity by acetone precipitation and subsequent Q-Sepharose anion exchange and Sephacryl S-200 gel filtration chromatography. The apparent molecular mass of the protease was 31 kDa by SDS-PAGE, whereas it was estimated as approximately 29 kDa by Sephacryl S-200 gel filtration. The purified protease had a specific activity of 116.8 mumol of tyrosine/min per mg protein on casein. The optimum temperature and salinity of the enzyme were at 55 degrees C and 0-0.5 M NaCl, although at salinities up to 4 M NaCl activity still remained. The protease was stable and had a broad pH profile (5.0-10.0) with an optimum of 8.5 for casein hydrolysis. The enzyme was strongly inhibited by phenylmethyl sulfonylfluoride (PMSF), Pefabloc SC, chymostatin and also EDTA, indicating that it belongs to the class of serine metalloproteases. The protease in solutions containing water-soluble organic solvents or alcohols was more stable than that in the absence of organic solvents. These characteristics make it an ideal choice for applications in industrial processes containing organic solvents and/or salts.
The objective of this research was to understand whether addition of soy protein to milk protein affects the properties of acid-induced casein gels. Different samples were prepared by suspending casein micelles pellets in milk serum containing soy proteins or whey proteins as well as mixtures of the two proteins. Glucono-delta-lactone was added, and the changes in apparent size (in diluted systems) as well as the viscoelastic properties of the mixtures were measured. Size exclusion chromatography was also carried out to characterize the soluble phase of the various mixtures before and after heating. Soy protein affected the gelation of the mixtures; however, not to the same extent as whey proteins, which dominated formation of the network in soy-whey-casein systems. It was concluded that, up to a critical ratio of soy/whey proteins, soy proteins can be incorporated in the mix without a significant change in structure of the casein gels.