Electrofractionation of protein mineral complexes obtained by electrophysial whey processing
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BOLOGA, M., STEPURINA, Tatiana, ILIASENCO, Olga, SAJIN, Tudor, POLIKARPOV, Albert, VRABIE, Valeria, GONCEARUC, Vladimir, PALADII, Irina, SPRINCEAN, Cătălina, VRABIE, Elvira. Electrofractionation of protein mineral complexes obtained by electrophysial whey processing. In: Materials Science and Condensed Matter Physics, Ed. 8-th Edition, 12-16 septembrie 2016, Chişinău. Chişinău: Institutul de Fizică Aplicată, 2016, Editia 8, p. 361. ISBN 978-9975-9787-1-2.
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Materials Science and Condensed Matter Physics
Editia 8, 2016
Conferința "International Conference on Materials Science and Condensed Matter Physics"
8-th Edition, Chişinău, Moldova, 12-16 septembrie 2016

Electrofractionation of protein mineral complexes obtained by electrophysial whey processing


Pag. 361-361

Bologa M.1, Stepurina Tatiana1, Iliasenco Olga1, Sajin Tudor2, Polikarpov Albert1, Vrabie Valeria1, Goncearuc Vladimir1, Paladii Irina1, Sprincean Cătălina1, Vrabie Elvira1
 
1 Institute of Applied Physics, Academy of Sciences of Moldova,
2 "Vasile Alecsandri" University of Bacau
 
Disponibil în IBN: 7 august 2019


Rezumat

Whey proteins are well structured proteins with secondary and tertiary stable structures. It is known that whey proteins make up about 20% of milk proteins. Four major whey protein components: βlactoglobulin (β-Lg), α-lactalbumin (α-La), bovine serum albumin (BSA), and immunoglobulin (Ig), make up 90% of the whey proteins: The remaining 10% are such proteins as lactoperoxidase, serum transferrin, lactoferrin, lactolin, and proteo-peptone fraction.     β-Lg makes up 50% of the whey proteins and 12% of the total protein content of milk. The β-Lg molecule consists of an α-helix, β-sheet and random coil structures represented in a ratio of 10 to 15%, 43% and 47%, respectively [1].   α-La makes up 20% of bovine milk whey proteins. It is а small globulаr whеy protеin found in аll milk studiеd to dаtе. It consists of 123 amino acid residues with a molecular mass of 14.2 kDa. It is a regulatory protein of the enzyme complex lactose synthetase, and lactose concentration in milk is directly related to the concentration of α-La     BSA is not synthesized in the mammary glands but gets into milk being passively transported from the bloodstream. It contains 17 intermolecular disulfide bonds and one thiol group in the rest of 34 amino acid residues (Fox, 1989). It is characterized by a low tryptophan and methionine content and a high content of cysteine and charged amino acids (glutamic and aspartic acids, lysine and arginine) (Peters, 1985). The secondary structure of BSA is represented predominantly by an alphahelix structure (67%). The rest of the polypeptide chain consists of curves (turns) and flexible extensive regions between domains without beta structures. The electrophysical processing of whey after the manufacture of the granulated cottage cheese „Grăuncior” and that after the manufacture of the “Cottage cheese”, 2% fat content, in electrolizer EDP-2, with a uniform flow in the cathode cell, at a current density of j=20 mA/cm2, and an electrophoretic analysis of the samples collected each 5 minutes with the gel SDS-PAGE 15%, as well as the isolation of soluble proteins with the phosphate-citrate buffer (Me Ilvane) 0.5 M NaCl, 0.5 mM EDTA (0.04% NaN3), pH 5.6, made it possible to identify many protein fractions that are various depending on the energy consumption, volume of the processed whey, duration of processing and variations of pH. In order to determine the quantity of the major fractions in the PMCs, the obtained results were scanned through the HP Scanget 3800 with the software Microsoft Photo Editor, and analyzed with the Phoretix 1D Advans[2] This research has been carried out in the framework of the STCU project 6011 whose support is acknowledged.