Peculiarities of extraction of β-lactoglobuline in protein mineral concentrates at electroactivation of whey

2020 ◽  
Vol 2 (1) ◽  
pp. 52-68
Author(s):  
Mircea BOLOGA ◽  
Elvira VRABIE ◽  
Irina PALADII ◽  
Olga ILIASENCO ◽  
Tatiana STEPURINA ◽  
...  
Keyword(s):  
Protein Content ◽  
Whey Proteins ◽  
Sodium Dodecyl ◽  
Total Protein Content ◽  
Treatment Regimens ◽  
Sds Page ◽  
Different Types ◽  
Lower Protein ◽  
Β Lactoglobulin ◽  
Excellent Source

Introduction. Whey is a by-product and an excellent source of proteins that is rather aggressive due to a large amount of organic substances it contains. The electro-activation of whey applied in the experiments is a wasteless method that allows the va-lorification of all whey components. β-lactoglobulin (β-Lg) makes up 50% of the whey proteins and 12% of the total protein content in milk. Material and methods. The recovery of β-Lg in protein-mineral concentrates (PMC) by electro-activation processing of different types of whey with different initial protein content was investigated in seven configurations. The recovery of protein fractions in the PMCs were analyzed via electrophoresis with sodium dodecyl sulfate (SDS-PAGE) and 15% non-denaturing polyacrylamide gel (PAAG).      Results. Whey electro-fractionation and the obtaining of PMCs with predetermined protein content, namely of β-Lg, were studied on three whey types, processed at different treatment regimens and in seven configurations. The proper management of electroactivation by varying the treatment regimens will allow the electro-fractionation of different types of dairy by-products. Conclusions. The maximum amount of β-Lg recovered in PMCs on electroactivation is  66-71% depending on the processed whey and on the treatment regimens. Obviously, the extraction of β-Lg from initially lower protein content shows a higher recovery degree of β-Lg. The registered temperatures allows formation of PMCs without thermal denaturation.

The dynamics of individual whey protein concentrations in cows’ mammary secretions during the colostral and early lactation periods

2018 ◽  
Vol 86 (1) ◽  
pp. 88-93 ◽  
Author(s):  
Raquel F.S. Raimondo ◽  
Juliana S.P. Ferrão ◽  
Samantha I. Miyashiro ◽  
Priscila T. Ferreira ◽  
João Paulo E. Saut ◽  
...  
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Whey Proteins ◽  
Total Proteins ◽  
Mature Milk ◽  
Rennet Coagulation ◽  
Sds Page ◽  
Different Types ◽  
Biuret Method ◽  
Jersey Cows ◽  
Β Lactoglobulin

AbstractThe bovine whey consists of more than 200 different types of proteins, of which β-lactoglobulin, α-lactalbumin, serum albumin, immunoglobulins and lactoferrin predominate. However, their concentrations are not stable due to the existence of protein dynamics during a transition from colostrum secretion to mature milk. To evaluate the dynamics of whey proteins of Jersey cows during a colostral phase and first month of lactation and an influence of the number of lactations, 268 milk samples from 135 Jersey cows were selected through a clinical evaluation. Whey was obtained by rennet coagulation of the mammary secretion. The concentration of total proteins was determined by the biuret method and their fractions were identified by 12% dodecyl sulfate-polyacrylamide gel electrophoresis (12% SDS-PAGE). Maximum concentrations of all protein fractions were observed in the first 12 h of lactation, reducing over the course of the study. Modification of the protein predominance was also observed. The transition from colostrum secretion to milk occurred between 24 and 72 h postpartum. There was an influence of the number of lactations on the dynamics of whey proteins, indicating that multiparous cows had better immunological and nutritional quality when compared to primiparous cows.

STUDYING THE INFLUENCE OF SEASONAL FACTORS ON CASEIN AND WHEY PROTEIN CONTENT IN RAW MILK AND CHEESE YIELD

2020 ◽  
pp. 142-151
Author(s):  
L. Bahdanava ◽  
A. Podryabinkina ◽  
I. Bahdanau ◽  
T. Savelyeva
Keyword(s):  
Protein Content ◽  
Whey Protein ◽  
Total Protein ◽  
Seasonal Changes ◽  
Whey Proteins ◽  
Raw Milk ◽  
National Average ◽  
Total Protein Content ◽  
Seasonal Factors

The article presents the results of research to study seasonal changes in the content of total protein, casein and whey proteins in raw milk and to analyze their impact on cheese yield. It was determined that the lowest casein content in raw milk (18% lower than the national average) was observed in October and March. The linear dependence of the cheese yield on both the total protein content and casein content was established.

scholarly journals Depicting the Non-Covalent Interaction of Whey Proteins with Galangin or Genistein Using the Multi-Spectroscopic Techniques and Molecular Docking

Foods ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 360 ◽  
Author(s):  
Chun-Min Ma ◽  
Xin-Huai Zhao
Keyword(s):  
Molecular Docking ◽  
Hydrophobic Interaction ◽  
Whey Proteins ◽  
Sodium Dodecyl ◽  
Binding Constants ◽  
Spectroscopic Techniques ◽  
Stereochemical Structure ◽  
Non Covalent Interactions ◽  
Β Lactoglobulin ◽  
Covalent Interactions

The non-covalent interactions between a commercial whey protein isolate (WPI) and two bioactive polyphenols galangin and genistein were studied at pH 6.8 via the multi-spectroscopic assays and molecular docking. When forming these WPI-polyphenol complexes, whey proteins had changed secondary structures while hydrophobic interaction was the major driving force. Detergent sodium dodecyl sulfate destroyed the hydrophobic interaction and thus decreased apparent binding constants of the WPI-polyphenol interactions. Urea led to hydrogen-bonds breakage and protein unfolding, and therefore increased apparent binding constants. Based on the measured apparent thermodynamic parameters like ΔH, ΔS, ΔG, and donor-acceptor distance, galangin with more planar stereochemical structure and random B-ring rotation showed higher affinity for WPI than genistein with location isomerism and twisted stereochemical structure. The molecular docking results disclosed that β-lactoglobulin of higher average hydrophobicity had better affinity for the two polyphenols than α-lactalbumin of lower average hydrophobicity while β-lactoglobulin possessed very similar binding sites to the two polyphenols. It is concluded that polyphenols might have different non-covalent interactions with food proteins, depending on the crucial polyphenol structures and protein hydrophobicity.

scholarly journals Determination of whey proteins in different types of milk

2014 ◽  
Vol 83 (1) ◽  
pp. 67-72 ◽  
Author(s):  
Lenka Ruprichová ◽  
Michaela Králová ◽  
Ivana Borkovcová ◽  
Lenka Vorlová ◽  
Iveta Bedáňová
Keyword(s):  
High Performance ◽  
Dairy Product ◽  
Whey Proteins ◽  
Reversed Phase ◽  
Cow’S Milk ◽  
Cow's Milk ◽  
Goat’S Milk ◽  
Different Types ◽  
Goat's Milk ◽  
Β Lactoglobulin

Protein analysis is very important both in terms of milk protein allergy, and of milk and dairy product adulteration (β-lactoglobulin may be an important marker in the detection of milk adulteration). The aim of this study was to detect major whey proteins α-lactalbumin and β-lactoglobulin and their genetic variants by reversed-phase high-performance liquid chromatography. Milk samples from cows (n = 40), goats (n = 40) and sheep (n = 40) were collected at two farms and milk bars in the Czech Republic from April to June 2010. The concentration of α-lactalbumin was higher in goat’s milk (1.27 ± 0.05 g·l-1, P < 0.001) and cow’s milk (1.16 ± 0.02 g·l-1, P = 0.0037) compared to sheep’s milk (0.95 ± 0.06 g·l-1); however, concentration of α-lactalbumin in goat’s milk and cow’s milk did not differ significantly (P < 0.05). Goat’s milk contained less β-lactoglobulin (3.07 ± 0.08 g·l-1) compared to cow’s milk (4.10 ± 0.04 g·l-1, P < 0.001) or sheep’s milk (5.97 ± 0.24 g·l-1, P < 0.001). A highly significant positive correlation (r = 0.8686; P < 0.001) was found between fraction A and B of β-lactoglobulin in sheep’s milk, whereas in cow’s milk there was a negative correlation (r = -0.3010; P = 0.0296). This study summarizes actual information of the whey protein content in different types of milk which may be relevant in assessing their allergenic potential.

Quantification of Whey Protein Content in Infant Formulas by Sodium Dodecyl Sulfate-Capillary Gel Electrophoresis (SDS-CGE): Single-Laboratory Validation, First Action 2016.15

2017 ◽  
Vol 100 (2) ◽  
pp. 510-521 ◽  
Author(s):  
Ping Feng ◽  
Christophe Fuerer ◽  
Adrienne McMahon
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Protein Content ◽  
Whey Protein ◽  
Gel Electrophoresis ◽  
Whey Proteins ◽  
Sodium Dodecyl ◽  
Infant Formulas ◽  
Method Performance ◽  
Capillary Gel Electrophoresis ◽  
Dodecyl Sulfate

Abstract Protein separation by sodium dodecyl sulfate-capillary gel electrophoresis, followed by UV absorption at 220 nm, allows for the quantification of major proteins in raw milk. In processed dairy samples such as skim milk powder (SMP) and infant formulas, signals from individual proteins are less resolved, but caseins still migrate as one family between two groups of whey proteins. In the first group, α-lactalbumin and β-lactoglobulin migrate as two distinct peaks. Lactosylated adducts show delayed migration times and interfere with peak separation, but both native and modified forms as well as other low-MW whey proteins still elute before the caseins. The second group contains high-MW whey proteins (including bovine serum albumin, lactoferrin, and immunoglobulins) and elutes after the caseins. Caseins and whey proteins can thus be considered two distinct nonoverlapping families whose ratio can be established based on integrated areas without the need for a calibration curve. Because mass-to-area response factors for whey proteins and caseins are different, an area correction factor was determined from experimental measurement using SMP. Method performance assessed on five infant formulas showed RSDs of 0.2–1.2% (within day) and 0.5–1.1% (multiple days), with average recoveries between 97.4 and 106.4% of added whey protein. Forty-three different infant formulas and milk powders were analyzed. Of the 41 samples with manufacturer claims, the measured whey protein content was in close agreement with declared values, falling within 5% of the declared value in 76% of samples and within 10% in 95% of samples.

Genetic improvement of two cultivars of Vicia faba L. using gamma irradiation and ethyl methanesulphonate mutagenesis

2016 ◽  
Author(s):  
Shahnawaz Khursheed ◽  
Samiullah Khan
Keyword(s):  
Gamma Irradiation ◽  
Protein Content ◽  
Vicia Faba ◽  
Mineral Content ◽  
Sodium Dodecyl ◽  
Ethyl Methanesulphonate ◽  
Mineral Contents ◽  
Sds Page ◽  
Vicia Faba L ◽  
Mutant Lines

The present experiment was conducted to induce genetic variation using gamma irradiation and ethyl methanesulphonate mutagenesis and isolate and analyze the desirable mutant lines of Vicia faba L. var. Vikrant and PRT-12 in the M3 generation. The seeds of the mutant lines isolated from 3rd generation plants were analyzed for different parameters including total protein content, protein profiles and mineral content using Lowry method, Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and atomic absorption spectrophotometer, respectively. SDS-PAGE profile of mutants from variety Vikrant showed more polymorphism and expression of proteins than mutants isolated from variety PRT-12. Mutant seeds showed significantly higher protein content (0.18 to 1.29%) and mineral content (0.21 to 2.98 mg.g-1) compared to the controls. The mutants selected from variety Vikrant showed more increase in protein and mineral contents than the mutants selected from PRT-12. The selected mutant lines may serve as a valuable genetic material to breed for the improvement of protein and mineral contents in faba bean and other valuable crop plants.

scholarly journals Whey pretreatments before ultrafiltration

1994 ◽  
Vol 3 (5) ◽  
pp. 473-479
Author(s):  
Tuomo Tupasela ◽  
Heikki Koskinen ◽  
Pirkko Antila
Keyword(s):  
Protein Content ◽  
Dry Matter ◽  
Whey Proteins ◽  
Ph Adjustment ◽  
Total Solids ◽  
Heat Treated ◽  
Protein Membrane ◽  
Membrane Isolation ◽  
Solids Content ◽  
Β Lactoglobulin

Whey is a by-product of cheesemaking. Whey dry matter contains mainly lactose, but also valuable whey proteins. The aim of this study was to develop improvements to whey protein membrane isolation processes. In our trials CaCl2 -added, pH-adjusted and heat-treated wheys were found to have MF (microfiltration) permeate fluxes about 30% higher than in untreated MF whey. The total solids and protein content of the MF permeates decreased compared to the original wheys. UF (ultrafiltration) trials were conducted using MF whey to compare it with centrifugally separated whey. The MF whey consistently maintained an UF flux about 1.5 to 2.5 times higher than that of the separated whey. Differently treated MF whey UF permeate fluxes also showed a difference. With CaCl2 addition, pH adjustment and heat treatment, the UF permeate fluxes were about 20 to 40% higher than when only MF was used. The total solids content decreased in each trial. The protein content of the UF concentrate also decreased compared to the MF permeate. The (β-lg (β-lactoglobulin) and α-la (α-lactalbumin) content was almost the same in UF concentrates as in MF permeates.

Effect of sodium azide on Bambara groundnut (Vigna subterranean (L.) verdc.) as revealed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (sds-page)

2021 ◽  
Vol 20 (1) ◽  
pp. 183-194
Author(s):  
Odunayo Joseph Olawuyi ◽  
Juliet Ese Naworu ◽  
Roseline Tolulope Feyisola
Keyword(s):  
Protein Content ◽  
Sodium Azide ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Lethal Effect ◽  
Bambara Groundnut ◽  
International Institute ◽  
Yield Traits ◽  
North East ◽  
Sds Page

This study investigated the mutagenic effects of Sodium Azide (NaN3) on the agromorphological and protein content of eight Bambara groundnut genotypes. The seeds of six genotypes; TVSu-86, TVSu-91, TVSu-186, TVSu-235, TVSu-242, TVSu-350 were collected fromthe International Institute of Tropical Agriculture (IITA) and two landraces from Abia State and Enugu State North East, Nigeria local markets. The seeds were treated with five concentrations: 0.00%(control), 0.01%, 0.03%, 0.05% and 0.07% of NaN3 after pre-soakingfor 6hrs in distilled water and sown in pots arranged in a Complete Randomized Design with three replicates. There was reduction in germination percentage and growth characters as concentrations of NaN3 increases. Early flowering was recorded at 37 days mutated with 0.07% of NaN3 compared to control which flowered late at 42 days. NaN3 (0.07%) caused lethal effect on Abia and Enugu landraces. There was no significant (P>0.05) difference in yield traits among mutants and control. Mutant seeds significantly (P<0.05) increased protein content (19.12%) at 0.05% of NaN3 compared to control (18.5%). The number of seeds (0.99), seed yield (0.89) and pod yield (0.96) strongly correlated with seeds per pod (0.85). The SDS-PAGE revealed the presence of polypeptide bands in mutants compared to control. TVSu-235 and TVSu-350 genotypes had higher tolerance and yield traits to 0.01% concentration of NaN3, thuscould be further improved in subsequent breeding. Keywords: Bambara groundnut, Sodium azide, SDS-PAGE, polypeptide bands.

Association of the CSN1S1 gene polymorphism with milk composition traits in Jamunapari goat

2018 ◽  
Author(s):  
Pallavi Singh ◽  
M. K. Singh ◽  
P. K. Rout ◽  
M. S. Dige
Keyword(s):  
Protein Content ◽  
Goat Milk ◽  
Milk Composition ◽  
Allelic Frequency ◽  
Total Protein Content ◽  
Genotypic Frequency ◽  
Genetic Stock ◽  
Sds Page ◽  
Genotype Information ◽  
Pcr Rflp

The genetic polymorphism of the CSN1S1 (casein alpha-s1) locus was investigated in Jamunapari goat breed by Sodium Dodicyle Sulphate – Poly Acrylamide Gel Electrophoresis (SDS-PAGE) and Polymerase Chain Reaction – Restriction Fragment Length Polymorphism (PCR-RFLP). A total of 122 milk and blood samples were collected. The SDS-PAGE pattern revealed the presence of four variants of CSN1S1 locus namely, A, B, E and F. The A allele of a-s1 – casein was observed in the majority of goats. The genotypic frequency of the AA, BB, BE, AF and FF genotypes of CSN1S1 locus were 0.437, 0.175, 0.250, 0.125 and 0.012, respectively. The PCR-RFLP was performed, six different variant groups of F allele (224)bp, the B/E allelic pair (161+63) bp, A/0 allelic pair (150+63) bp, AD allelic pair (212+150+63) bp, AF allelic pair (224+150+63) bp and BF allelic pair (224+160+63) were obtained after restriction digestion with XmnI. The genotypic frequency of AA, AD, AF, BB, BE, BF and BC genotypes were 0.274, 0.114, 0.147, 0.098, 0.163, 0.081 and 0.163, respectively. The allelic frequency of A, B, C, D, E and F were 0.360, 0.303, 0.081, 0.057, 0.081 and 0.114, respectively. The present study showed that AA genotype had significant effect on total protein content on the milk and AD genotype had significant effect on 90 day milk yield in Jamunapari goat. Thus the CSN1S1 genotype information in Jamunapari could be utilised in selection strategies, in order to select genetic stock for the production of goat milk with higher protein content in marker assisted selection to increase the rate of genetic gain.

scholarly journals MAJOR GOAT MILK PROTEIN: SEPARATION AND CHARACTERIZATION BY “LAB-ON-A-CHIP” MICROFLUIDIC ELECTROPHORES

2018 ◽  
Vol 35 (2) ◽  
Author(s):  
ALESSA SIQUEIRA DE O. DOS SANTOS ◽  
VANEIDA MARIA MEURER ◽  
FABIANO FREIRE COSTA ◽  
IGOR MOURA DE PAIVA ◽  
GISELE NOGUEIRA FOGAÇA ◽  
...  
Keyword(s):  
Protein Separation ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Goat Milk ◽  
Lab On A Chip ◽  
Cow Milk ◽  
Total Percentage ◽  
Chip Technology ◽  
Sds Page ◽  
Β Lactoglobulin

This work presents the electrophoretic profile of goat and cow milk samples and their mixtures using microfluidic and conventional electrophoresis. The microfluidic method allowed the separation of the major caseins from milk, excepting the goat κ-casein.  Besides, the major whey proteins were separated with perfect distinction of A and B β-lactoglobulin variants. Comparing to SDS-PAGE, a variation in the molecular weight was observed in all milk proteins. However, A and B β-lactoglobulin variants could not be isolated using SDS-PAGE. Although urea-PAGE did not show high resolution among whey proteins, γ-, κ-, β-, and α-caseins were clearly identified. This method also showed a lower limit detection of cow milk in mixture samples than the "lab-on-a-chip" electrophoresis. In both methods, the highest linearity obtained from plotting total percentage against cow milk concentration was observed by using cow αs1-casein (R2 = 0.986 and R² = 0.973). This result indicates that microfluidic electrophoresis is an effective tool to detect the presence of some proteins in goat and cow milk, and in mixtures. Microfluidic chip technology might will complement the current methods for analyzing milk proteins, highlighting its speed amount of reagents and whey protein separation, which showed a better result than urea or SDS-PAGE

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