scholarly journals Study on milk composition and milk protein distribution in Romanian Holstein cattle

2020 ◽  
Vol 23 (1) ◽  
pp. 13-21
Author(s):  
Rodica Ştefania Pelmuş ◽  
Cristina Lazăr ◽  
M. L. Palade ◽  
Mariana Stancu ◽  
C. M. Rotar ◽  
...  

AbstractThe aim of this study was to determine milk quality indices as well as the milk protein composition in Romanian Holstein cattle raised under the conditions of experimental farm of INCDBNA-IBNA. The study was carried out on 22 milk samples. The types of different milk proteins were identified by SDS-PAGE technique. Sampling day and milk chemical composition were performed during the milking period of studied cattle. The quality indices were breed-specific for protein (3.38%) and higher for fat (4.39%).Milk proteins analysis of Romanian Holstein cattle separated by SDS-PAGE electrophoresis showed the presence of four major caseins (αs1-, αs2-, β- and k-casein) and two whey proteins (β-lactoglobulin, α-lactalbumin). The caseins accounted 77.28% of the total milk proteins, while the major proteins (β-lactoglobulin, α-lactalbumin) from the whey represented 22.72% of the total proteins. αs1-casein + αs2-casein had a higher expression (36.01%) followed by β-casein (31.45%), β-lactoglobulin (18.16%), k-casein (9.82%) and α-lactalbumin (4.56%). The most of milk samples was characterized by a medium expression level of both caseins and whey proteins

2009 ◽  
Vol 77 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Elin Hallén ◽  
Anne Lundén ◽  
Toomas Allmere ◽  
Anders Andrén

Impact of milk protein composition on casein (CN) retention in curd during the milk coagulation process was studied using a model cheese making system. Individual milk samples from 110 cows in mid lactation of the Swedish Red and Swedish Holstein breeds with known genotypes of β-casein, κ-casein and β-lactoglobulin were defatted, coagulated with chymosin, subjected to syneresis and subsequent pressing simulated by centrifugation. The results indicated that κ-casein concentration of milk plays an important role in the curd formation process and initial syneresis (whey after cutting), whereas an increased CN ratio was associated with less casein in whey after simulated pressing. Increased κ-casein concentration of milk also characterized the milk samples with no measurable loss of casein in whey, compared with milk samples with casein lost in whey, both after cutting and after simulated pressing. Concentrations of αs1-casein, β-casein, and total casein in milk were positively associated with fresh curd yield, which showed a strong correlation with amount of casein retained in curd. No effect of protein genotype on fresh curd yield or casein in whey was found. The β-lactoglobulin BB genotype was associated with increased casein retention in curd, most likely due to the association of this genotype with CN ratio.


Author(s):  
ALESSA SIQUEIRA DE O. DOS SANTOS ◽  
VANEIDA MARIA MEURER ◽  
FABIANO FREIRE COSTA ◽  
IGOR MOURA DE PAIVA ◽  
GISELE NOGUEIRA FOGAÇA ◽  
...  

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


2000 ◽  
Vol 25 ◽  
pp. 169-173
Author(s):  
M.J. Auldist ◽  
C.M. Menzies ◽  
R.J. Hooper ◽  
C.G. Prosser

AbstractThe objective of this study was to measure the effects of varying doses of atropine on the concentration and composition of milk protein and on blood α-amino N levels. Four treatments were administered to each of 12 cows over 12 days in a replicated Latin square experiment. There were at least 2 days between each of 4 treatment days. Treatments were: control (C; saline); low dose (L; 30mg atropine/kg LWT); medium dose (M; 40mg atropine/kg LWT); and 2 x low dose (2L). All treatments were administered via subcutaneous injection immediately after the morning milking; the second dose of the 2L treatment was given two hours later. Milk was sampled from each cow at the morning milking (time 0 h). Cows were then milked again 2, 6 and 10 h after treatment, and milk samples again collected. Blood samples were drawn from the coccygeal vein of each cow after each milking. Atropine decreased milk secretion at 6 h for the 2L treatment and 10 h for all treatments. Atropine reduced concentrations of milk protein and casein at 2 h and 6 h, but not at 10 h. Concentrations of whey proteins and of α-casein were depressed by atropine only at 6 h post-treatment, while a reduction in α-lactalbumin due to atropine was observed at 6 and 10 h post-treatment. In contrast, atropine increased concentrations of IgG and BSA at 6 h and 10 h post-treatment. Atropine also increased the ratio of casein:total protein at 6 h after injection. There was no difference between the effects of the low and medium doses of atropine, but the double low dose induced effects which were greater than for the single doses. Effects of a single dose of atropine were greatest for most milk proteins at 6 h post treatment; thus this would be the most useful milk sampling time for future experiments. Atropine did not significantly affect α-amino N concentrations in whole blood, although there was a trend for a reduction for all treatments at 2 h after treatment. Atropine may be useful for reducing milk protein concentrations and circulating levels of certain blood amino acids to base levels, during studies designed to elucidate the effects of perturbations in the blood amino acid profile on milk protein composition.


2011 ◽  
Vol 79 (1) ◽  
pp. 110-118 ◽  
Author(s):  
Maria Glantz ◽  
Helena Lindmark Månsson ◽  
Hans Stålhammar ◽  
Marie Paulsson

The relations between cow genetics and milk composition have gained a lot of attention during the past years, however, generally only a few compositional traits have been examined. The aim of this study was to determine if polymorphisms in the leptin (LEP), leptin receptor (LEPR) and acyl-CoA:diacylglycerol acyltransferase 1 (DGAT1) genes as well as genetic polymorphism of β-casein (β-CN), κ-CN and β-lactoglobulin (β-LG) impact several bovine milk composition traits. Individual milk samples from the Swedish Red and Swedish Holstein breeds were analyzed for components in the protein, lipid, carbohydrate and mineral profiles. Cow alleles were determined on the following SNP: A1457G, A252T, A59V and C963T on the LEP gene, T945M on the LEPR gene and Nt984+8(A-G) on the DGAT1 gene. Additionally, genetic variants of β-CN, κ-CN and β-LG were determined. For both the breeds, the same tendency of minor allele frequency was found for all SNPs and protein genes, except on LEPA1457G and LEPC963T. This study indicated significant (P<0·05) associations between the studied SNPs and several compositional parameters. Protein content was influenced by LEPA1457G (G>A) and LEPC963T (T>C), whereas total Ca, ionic Ca concentration and milk pH were affected by LEPA1457G, LEPA59V, LEPC963T and LEPRT945M. However, yields of milk, protein, CN, lactose, total Ca and P were mainly affected by β-CN (A2>A1) and κ-CN (A>B>E). β-LG was mainly associated with whey protein yield and ionic Ca concentration (A>B). Thus, this study shows possibilities of using these polymorphisms as markers within genetic selection programs to improve and adjust several compositional parameters.


2017 ◽  
pp. 150-155
Author(s):  
Thi Huyen Nguyen ◽  
Thi Minh Phuong Phan ◽  
Galleri Grazia

Background: Cow’s milk protein allergy (CMPA) is the most common food allergy, especially, in infants and young children. In this case, milk from other mammalian species has been suggested as a possible nutritional alternative to cow’s milk. Goat’s milk is used quite popular to replace for cow’s milk. In the goat species, αS1casein (αS1-CN), coded by the CSN1S1 gene, is characterized by qualitative and quantitative polymorphisms extensively. This aim of this study is to evaluate allergenicity of goat’s milk containing differentk kinds of αS1CN. Methods: Individual milk samples from 26 selected goats with different CSN1S1 genotypes were analyzed by SDS-PAGE and immunoblotting by using sera from children allergic to cow’s milk with IgE specific to CN and/or serum protein. Results: The absence of reactivity for the αs1-CN highlighted with immunoblotting for all goat milk samples. Conclusions: The goat’s milk with particular genotype for CSN1S1 could be used as a source protein alternative in the case of αs1-CN awareness. Furthermore, these tests could be useful for evaluating from time to time the reactivity of patients with CMPA against milk proteins of these goats selected to establish the safety of its use in the specific subject. Key words: Allergenicity, milk protein, goat, alphaS1-Casein, CSN1S1gene


Nutrients ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 1476
Author(s):  
Jian Zhang ◽  
Ai Zhao ◽  
Shiyun Lai ◽  
Qingbin Yuan ◽  
Xiaojiang Jia ◽  
...  

Our knowledge related to human milk proteins is still limited. The present study determined the changes in multiple human milk proteins during the first six months of lactation, investigated the influencing factors of milk proteins, and explored the impact of milk proteins on infant growth. A total of 105 lactating women and their full-term infants from China were prospectively surveyed in this research. Milk samples were collected at 1–5 days, 8–14 days, 1 month, and 6 months postpartum. Concentrations of total protein and α-lactalbumin were measured in all milk samples, and concentrations of lactoferrin, osteopontin, total casein, β-casein, αs−1 casein, and κ-casein were measured in milk from 51 individuals using ultra performance liquid chromatography coupled with mass spectrometry. The concentration of measured proteins in the milk decreased during the first six months of postpartum (p-trend < 0.001). Maternal age, mode of delivery, maternal education, and income impacted the longitudinal changes in milk proteins (p-interaction < 0.05). Concentrations of αs−1 casein in milk were inversely associated with the weight-for-age Z-scores of the infants (1 m: r −0.29, p 0.038; 6 m: r −0.33, p 0.020). In conclusion, the concentration of proteins in milk decreased over the first six months postpartum, potentially influenced by maternal demographic and delivery factors. Milk protein composition may influence infant weights.


Author(s):  
Alina NASALEAN ◽  
Laurentiu OGNEAN ◽  
Sergiu MUNTEAN ◽  
Stefana BALICI ◽  
Horea MATEI

The milk’s proteins provide nutritional and biologically active values, essential in human and animal nutrition. In the case of goat milk, the proteins’ concentration and quality represent basic indices for the evaluation of the nutritional and biologically active values. The proposal is to comparatively analyse the protein profile of milk. The milk was collected from two different breeds: French Alpine and Romanian Carpathian. During March and April 2016 there were collected samples of raw milk in hygienic and sanitation conditions. There were two lots: first lot has 10 Carpathian goats and the second lot has 10 Alpine goats. The protein composition of goat milk was established with SDS-PAGE, after the evaluation of the total proteins’ concentration with the Bradford method. The quantitative and percentage data obtained with electrophoresis revealed few differences between those 8 identified protein fractions. Between those two lots, regarding the levels of β-CN, k-CN and β-lactoglobulines there were significant differences. The other protein fractions have values almost identical. Statistical analysis of obtained data shaped the differences in the protein profile at those two breeds. Based on those differences it is to note the superior potential of the Alpine breed regarding the content in biologically active milk proteins. Regarding the obtained data, this study brings new contributions for the evaluation and analysis of protein profile as a nutritive and biologically active component of goat milk, confirming its character as a functional aliment.


1990 ◽  
Vol 57 (1) ◽  
pp. 53-62 ◽  
Author(s):  
Anne-Marie Bech ◽  
K. Rotvig Kristiansen

SummaryIn milk samples from 549 cows of the breeds Danish Jersey, Red Danish Dairy Cattle (RDM), and Black and White Danish Dairy Cattle (SDM) the genetic polymorphisms of the αs1, β and K-cascin and β-lactoglobulin (β-Lg) loci were determined by isoelectric focusing in agarose gels. The results of the screening were comparcd with results obtained by Larsen & Thymann (1966). In addition, the genetic linkage of the three casein loci was studied, and the association between milk protein genotypes and yields in first and second lactations of milk, fat and protein were investigated.The distribution of genotypes of all four milk protein Systems was different from breed to breed.For Jersey cows, significant differences in the gene frequencies from the results of the 1966 investigation were found for αs1 and K-casein and β-Lg. For SDM cows a change in the K-casein frequency had occurred whereas for RDM cows no changes were found.Linkage between some of the casein loci was found within ail three breeds. For the RDM breed the possible linkage between αs1-casein and the other caseins could not be tested bccause nearly ail thc cows were homozygous for the αs1-cascin-B genotypes.β-Casein genotypes were associated with yield parameters in ail breeds. The A2A2 genotype of this protein gave higher yields of milk, fat, and protein in the second lactation than thc A1A1 genotype.


PEDIATRICS ◽  
1991 ◽  
Vol 87 (4) ◽  
pp. 439-444
Author(s):  
Patrick S. Clyne ◽  
Anthony Kulczycki

Previous studies have suggested that an unidentified cow's milk protein, other than β-lactoglobulin and casein, might play a pathogenetic role in infant colic. Therefore, a radioimmunoassay was used to analyze human breast milk and infant formula samples for the presence of bovine IgG. Milk samples from 88 of the 97 mothers tested contained greater than 0.1 µg/mL of bovine IgG. In a study group of 59 mothers with infants in the colic-prone 2- to 17-week age group, the 29 mothers of colicky infants had higher levels of bovine IgG in their breast milk (median 0.42 µg/mL) than the 30 mothers of noncolicky infants (median 0.32 µg/mL) (P &lt; .02). The highest concentrations of bovine IgG observed in human milk were 8.5 and 8.2 µg/mL. Most cow's milk-based infant formulas contained 0.6 to 6.4 µg/mL of bovine IgG, a concentration comparable with levels found in many human milk samples. The results suggest that appreciable quantities of bovine IgG are commonly present in human milk, that significantly higher levels are present in milk from mothers of colicky infants, and that bovine IgG may possibly be involved in the pathogenesis of infant colic.


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 ◽  
...  

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.


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