منابع مشابه
Detecting β-Casein Variation in Bovine Milk.
In bovine species, β-casein (β-CN) is characterized by genetic polymorphism. The two most common protein variants are β-CN A² (the original one) and A¹, differing from A² for one amino acid substitution (Pro67 to His67). Several bioactive peptides affecting milk nutritional properties can originate from β-CN. Among them, β-casomorphin-7 (BCM7) ranging from amino acid 60 to 66 can be released mo...
متن کاملβ-casein gene polymorphism permits identification of bovine milk mixed with bubaline milk in mozzarella cheese
Mozzarella cheese is traditionally prepared from bubaline (Bubalus bubalis) milk, but product adulteration occurs mainly by addition of or full substitution by bovine milk. The aim of this study was to show the usefulnes of molecular markers to identify the admixture of bovine milk to bubaline milk during the manufacturing process of mozzarella cheese. Samples of mozzarella cheese were produced...
متن کاملAdsorption of Milk Proteins (β-Casein and β-Lactoglobulin) and BSA onto Hydrophobic Surfaces
Here, we study films of proteins over planar surfaces and protein-coated microspheres obtained from the adsorption of three different proteins ( β -casein, β -lactoglobulin and bovine serum albumin (BSA)). The investigation of protein films in planar surfaces is performed by combining quartz crystal microbalance (QCM) and atomic force microscopy (AFM) measurements with all-atomic molecular dyna...
متن کاملNew functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors.
We found new inhibitory function of lactoferrin and beta-casein in milk against cysteine proteases using reverse zymography. The inhibition of cathepsin L by lactoferrin was strongest and the inhibition kinetics were of a non-competitive type. Heat denatured lactoferrin lost the inhibitory activity completely, therefore the tertiary structure is essential to show the inhibition. Native lactofer...
متن کاملFlocculation of diatomite by methylated milk casein in seawater.
A new biodegradable flocculant was prepared from a common and inexpensive protein. Milk casein was methylated in a 0.05 M HCl methyl alcohol solution at room temperature. The methylated milk casein (MeCS), having a methylation degree of 81%, was applied to the separation or flocculation of diatomite in seawater (pH 8.1+/-0.1) at room temperature (18-23 degrees C). The flocculating ability of Me...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1972
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.36.255