scholarly journals Antiviral properties of whey proteins and their activity against SARS-CoV-2 infection

2022 ◽  
pp. 104932
Author(s):  
Valentina Gallo ◽  
Francesco Giansanti ◽  
Alyexandra Arienzo ◽  
Giovanni Antonini
Keyword(s):  
Whey Proteins

Application of whey proteins microparticulate in the technology of kefir production

2018 ◽  
pp. 49-51
Author(s):  
E.B. Stanislavskaya ◽  
◽  
E.I. Melnikova ◽  
Keyword(s):  
Whey Proteins

Prospects of using dynamic membrane filtration module UF-RDM for concentrating cheese whey proteins

2019 ◽  
Vol 56 (6) ◽  
pp. 54-56
Author(s):  
E.Yu. Agarkova ◽  
◽  
A.G. Kruchinin ◽  
A.A. Agarkov ◽  
V.D. Haritonov
Keyword(s):  
Membrane Filtration ◽  
Cheese Whey ◽  
Whey Proteins ◽  
Dynamic Membrane

Proteolysis of caseins and the proteose-peptone fraction of bovine milk

1983 ◽  
Vol 50 (3) ◽  
pp. 275-290 ◽  
Author(s):  
Anthony T. Andrews ◽  
Efstathios Alichanidis
Keyword(s):  
Gel Electrophoresis ◽  
Whey Proteins ◽  
Bovine Milk ◽  
Major Product ◽  
Natural Course ◽  
Pasteurized Milk ◽  
Proteose Peptone ◽  
History Of

SummaryThe proteolysis of highly purified samples of αs1-, αs2-, β-and κ-caseins by porcine plasmin and by bovine plasminogen with urokinase has been examined principally by gel electrophoresis. The resulting peptide band patterns were compared with those of total proteose-peptone (TPP) samples prepared from fresh and stored raw and pasteurized milk, and also with those obtained during the natural course of proteolysis by indigenous enzymes in milk during storage. TPP was found to contain at least 38 components detectable by a single electrophoresis run. Apart from residual traces of whey proteins and intact caseins nearly all of these components were fragments of caseins produced by indigenous plasmin, with products from the breakdown of αs1- and β-casein predominating. Over 90 % of TPP has been accounted for in this way. A fragment consisting of residues 29–105 of β-casein was isolated and characterized from both stored milk and from plasmin digests of β-casein. This fragment was a relatively major product of the natural proteolysis occurring during storage of milk, but contrary to a report in the literature it was not the same as proteose-peptone component 8-slow. Since many of the components of TPP resulted from proteolysis, the composition of TPP was found to vary according to the time and temperature of storage of the milk from which it was prepared. Thus, while the proteose-peptone fraction of milk can easily be defined operationally it cannot be rigorously defined in terms of its composition unless the history of the milk is also defined.

scholarly journals Post translational modifications of milk proteins in geographically diverse goat breeds

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
P. K. Rout ◽  
M. Verma
Keyword(s):  
Protein Function ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Goat Milk ◽  
Peptide Sequence ◽  
Cow Milk ◽  
Post Translational Modification ◽  
Post Translational Modifications ◽  
Functional Roles ◽  
Dpp Iv

AbstractGoat milk is a source of nutrition in difficult areas and has lesser allerginicity than cow milk. It is leading in the area for nutraceutical formulation and drug development using goat mammary gland as a bioreactor. Post translational modifications of a protein regulate protein function, biological activity, stabilization and interactions. The protein variants of goat milk from 10 breeds were studied for the post translational modifications by combining highly sensitive 2DE and Q-Exactive LC-MS/MS. Here we observed high levels of post translational modifications in 201 peptides of 120 goat milk proteins. The phosphosites observed for CSN2, CSN1S1, CSN1S2, CSN3 were 11P, 13P, 17P and 6P, respectively in 105 casein phosphopeptides. Whey proteins BLG and LALBA showed 19 and 4 phosphosites respectively. Post translational modification was observed in 45 low abundant non-casein milk proteins mainly associated with signal transduction, immune system, developmental biology and metabolism pathways. Pasp is reported for the first time in 47 sites. The rare conserved peptide sequence of (SSSEE) was observed in αS1 and αS2 casein. The functional roles of identified phosphopeptides included anti-microbial, DPP-IV inhibitory, anti-inflammatory and ACE inhibitory. This is first report from tropics, investigating post translational modifications in casein and non-casein goat milk proteins and studies their interactions.

scholarly journals Changes in Particle Size, Sedimentation, and Protein Microstructure of Ultra-High-Temperature Skim Milk Considering Plasmin Concentration and Storage Temperature

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2339
Author(s):  
So-Yul Yun ◽  
Jee-Young Imm
Keyword(s):  
Particle Size ◽  
High Temperature ◽  
Storage Temperature ◽  
Whey Proteins ◽  
Skim Milk ◽  
Storage Period ◽  
Sediment Analysis ◽  
Sediment Formation ◽  
And Storage ◽  
Ultra High Temperature

Age gelation is a major quality defect in ultra-high-temperature (UHT) pasteurized milk during extended storage. Changes in plasmin (PL)-induced sedimentation were investigated during storage (23 °C and 37 °C, four weeks) of UHT skim milk treated with PL (2.5, 10, and 15 U/L). The increase in particle size and broadening of the particle size distribution of samples during storage were dependent on the PL concentration, storage period, and storage temperature. Sediment analysis indicated that elevated storage temperature accelerated protein sedimentation. The initial PL concentration was positively correlated with the amount of protein sediment in samples stored at 23 °C for four weeks (r = 0.615; p < 0.01), whereas this correlation was negative in samples stored at 37 °C for the same time (r = −0.358; p < 0.01) due to extensive proteolysis. SDS-PAGE revealed that whey proteins remained soluble over storage at 23 °C for four weeks, but they mostly disappeared from the soluble phase of PL-added samples after two weeks’ storage at 37 °C. Transmission electron micrographs of PL-containing UHT skim milk during storage at different temperatures supported the trend of sediment analysis well. Based on the Fourier transform infrared spectra of UHT skim milk stored at 23 °C for three weeks, PL-induced particle size enlargement was due to protein aggregation and the formation of intermolecular β-sheet structures, which contributed to casein destabilization, leading to sediment formation.

Influence of dietary proteins on rennin and pepsin content of preruminant calf vell

1974 ◽  
Vol 41 (1) ◽  
pp. 19-23 ◽  
Author(s):  
Pascaline Garnot ◽  
E. Valles ◽  
J.-L. Thapon ◽  
R. Toullec ◽  
R. Tomassone ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Whey Proteins ◽  
Deae Cellulose ◽  
Milk Proteins ◽  
Total Activity ◽  
Separate Experiment ◽  
Dietary Proteins ◽  
Constant Weight ◽  
Cellulose Column ◽  
Qualitative Analyses

SummaryStudies were undertaken to determine the influence of dietary proteins on the rennin and pepsin contents of preruminant calf vell. Three groups of 12 Friesian calves were each fed either milk proteins, whey proteins or a 50:50 mixture of these 2 diets. They were slaughtered at a constant weight of 150kg and their vells collected and dried. Another group of vells was obtained from 8 animals that had been fed milk proteins in a separate experiment. The extraction of the abomasal enzymes was carried out at acid pH, and the extracts were quantitatively analysed for rennin and pepsin by DEAE-cellulose column chromatography. Qualitative analyses were also performed by agarose-acrylamide gel electrophoresis. The only enzymes observed using this last method were rennin and bovine pepsin II. Statistical analysis of the quantitative enzyme determinations indicated a trend for the vells from calves fed diets containing casein to be richer in total activity and in rennin, while the level of pepsin remained approximately constant. It seems that casein may induce the secretion of rennin. However, further experiments will be necessary to confirm this. Important differences were observed between the 2 groups of veils from calves given the same diet, but grown in slightly different conditions.

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