Results 351 to 360 of about 347,890 (386)
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Soft Matter, 2014
The poor water solubility and bioactivity of lipophilic phytochemicals can be potentially improved by delivery systems. In this study, a low-cost, low-energy, and organic solvent-free encapsulation technology was studied by utilizing the pH-dependent ...
K. Pan+4 more
semanticscholar +1 more source
The poor water solubility and bioactivity of lipophilic phytochemicals can be potentially improved by delivery systems. In this study, a low-cost, low-energy, and organic solvent-free encapsulation technology was studied by utilizing the pH-dependent ...
K. Pan+4 more
semanticscholar +1 more source
Inhibition of Dental Erosion by Casein and Casein-Derived Proteins
Caries Research, 2010The application of milk-derived proteins such as casein as anti-erosion agents in oral healthcare products is of current interest. The aim of this study was to investigate the potential of 3 commercially available, milk-derived proteins as agents to inhibit enamel erosion.
White, AJ, Gracia, LH, Barbour, ME
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Calpain Zymography with Casein or Fluorescein Isothiocyanate Casein
2003Methods for analyzing enzyme activity after electrophoresis in acrylamide gels have been described for a variety of proteins, including several proteases and kinases. The application of this approach to detect calpain activity by casein zymography was first described by Raser et al.
Arthur, J. Simon C., Mykles, Donald L.
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Journal of Dairy Research, 1979
SUMMARYHuman β-casein occurs in multiphosphorylated forms having the same amino acid composition but with 0–5 phosphate groups/molecule. Sequence analysis was used to determine whether each of the phosphorylated forms is a mixture of species having a certain number of phosphate groups randomly distributed or whether each form contains phosphate groups ...
M L Groves, R Greenberg
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SUMMARYHuman β-casein occurs in multiphosphorylated forms having the same amino acid composition but with 0–5 phosphate groups/molecule. Sequence analysis was used to determine whether each of the phosphorylated forms is a mixture of species having a certain number of phosphate groups randomly distributed or whether each form contains phosphate groups ...
M L Groves, R Greenberg
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Enhanced dispersibility and bioactivity of curcumin by encapsulation in casein nanocapsules.
Journal of Agricultural and Food Chemistry, 2013In this work, a novel encapsulation method was studied by spray-drying a warm aqueous ethanol solution with codissolved sodium caseinate (NaCas) and lipophilic food components, using curcumin as a model compound.
K. Pan, Q. Zhong, S. Baek
semanticscholar +1 more source
The structure of the casein micelle of milk and its changes during processing.
Annual Review of Food Science and Technology, 2012The majority of the protein in cow's milk is contained in the particles known as casein micelles. This review describes the main structural features of these particles and the different models that have been used to define the interior structures.
D. Dalgleish, M. Corredig
semanticscholar +1 more source
Casein micelle structure: location of κ-casein
Journal of Dairy Research, 1972SummaryThe effect of heat treatment on the rennet coagulation times (RCTs) of various casein–whey protein systems, the effect of pre-renneting centrifugal serum on the RCT of casein subsequently mixed with such serum, the influence of repeated centrifugation and resuspension at constant protein level on the RCT of such suspensions, and the rate and ...
Patrick A. Morrissey, Patrick F. Fox
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Casein kinase: the triple meaning of a misnomer.
Biochemical Journal, 2014The term 'casein kinase' has been widely used for decades to denote protein kinases sharing the ability to readily phosphorylate casein in vitro. These fall into three main classes: two of them, later renamed as protein kinases CK1 (casein kinase 1, also
A. Venerando, M. Ruzzene, L. Pinna
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Structure of casein micelles II. ? s1-casein
Colloid & Polymer Science, 1987Following the earlier study of theβ- andϰ-casein micelle structure, we will now report results from theαs1-casein. Static and dynamic light scattering measurements were performed in a concentration range from 0.5 to 6.0 mg/ml atT=35 °C. A constant apparent molecular weight of 3.4×106 daltons was found over the whole range.
R. Niki+2 more
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Food Science and Technology International, 2006
Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in β-CN (β-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH =2, 37°C 2h) and intestinal stage (pancreatic-bile extract, pH =5.2, 37°C 2h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation ...
Reyes Barberá+5 more
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Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in β-CN (β-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH =2, 37°C 2h) and intestinal stage (pancreatic-bile extract, pH =5.2, 37°C 2h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation ...
Reyes Barberá+5 more
openaire +2 more sources