“…1): lactoferrin (84.0 ± 4.0 kDa); albumin (66.0 ± 2.0 kDa); heavy chain immunoglobulin (52.0 ± 2.0 kDa); light-chain immunoglobulin (26.0 ± 1.5 kDa); Β-lactoglobulin (β-LG) (16.0 ± 1.0 kDa) and α-lactalbumin (α-LA) (12.0 ± 0.65 kDa). The identification of whey proteins through 12% SDS-PAGE using purified proteins has already been described as efficient in previous studies (Raimondo et al 2013a; 2013 b ). Fig.…”
The 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.
“…1): lactoferrin (84.0 ± 4.0 kDa); albumin (66.0 ± 2.0 kDa); heavy chain immunoglobulin (52.0 ± 2.0 kDa); light-chain immunoglobulin (26.0 ± 1.5 kDa); Β-lactoglobulin (β-LG) (16.0 ± 1.0 kDa) and α-lactalbumin (α-LA) (12.0 ± 0.65 kDa). The identification of whey proteins through 12% SDS-PAGE using purified proteins has already been described as efficient in previous studies (Raimondo et al 2013a; 2013 b ). Fig.…”
The 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.
“…In the fractionation of the proteins by 12% SDS-PAGE during the colostral phase and the first month of lactation of Saanen goats, the following protein fractions were identified and quantified: lactoferrin (84.0 ± 4.0 kDa); albumin (66.0 ± 2.0 kDa); heavy chain immunoglobulin (52.0 ± 2.0 kDa); light chain immunoglobulin (26.0 ± 1.5 kDa); β -lactoglobulin (β-LG) (16.0 ± 1.0 kDa) and α-lactalbumin (α-LA) (12.0 ± 0.65 kDa). Identifying whey proteins through 12% SDS-PAGE using purified proteins has already been described as efficient in previous studies (Raimondo et al, 2013a(Raimondo et al, , 2013b(Raimondo et al, , 2018.…”
Section: Resultsmentioning
confidence: 99%
“…Specifically, various studies have focused on the whey proteome of goat milk (Sun et al ., 2020). Investigations into the whey proteomes at different stages of lactation have been carried out in both bovine (Yang et al ., 2017; Raimondo et al ., 2018) and goat species (Raimondo et al ., 2013a; Sun et al ., 2020). Previous studies have also examined goat milk whey proteomes at different lactation stages (Raimondo et al ., 2013b; Hernández-Castellano et al ., 2014).…”
The protein composition in goat milk undergoes changes throughout the different lactation periods, displaying distinct characteristics that are influenced by the dynamic nature of protein composition and concentration during the transition from colostrum secretion to mature milk. To evaluate the dynamics of whey proteins of Saanen goats during the colostral phase and the first month of lactation, 110 milk samples from 11 healthy mammary halves of seven Saanen goats were selected through a clinical evaluation. Whey was obtained by rennet coagulation of the mammary secretion. The biuret method determined total protein concentration, and their fractions were identified by 12% dodecyl sulfate-polyacrylamide gel electrophoresis. Maximum concentrations of all protein fractions were observed in the first 12 h of lactation, reducing throughout the study. Modification of the protein predominance was also observed. The transition from colostrum secretion to milk occurred 5 or 7 d postpartum.
O objetivo deste estudo foi correlacionar os métodos de Biuret, Lowry, Bradford e Mlikoscan utilizados para a determinação da proteína do leite de cabra e compará-los com o método de Kjeldahl. Dezoito amostras de leite das raças Saanen (n=5), Anglo-nubiana (n=4), Pardo-alpina (n=5) e crioula (n=4) foram analisadas. Correlação entre os diferentes métodos foram realizadas (teste de Pearson) e o conteúdo de proteína entre diferentes raças foi comparado por ANOVA. As concentrações de proteína total (PT) e caseína (CN) foram correlacionadas positivamente entre todos os métodos com o Kjeldahl (p0,01), mostrando Bradford a menor correlação. Todos os métodos, exceto Bradford, mostraram diferenças significativas na PT entre as raças Anglo-nubiana e pardo-alpina (p0,05) e na CN entre Saanen e Pardo-alpina (p0,05). Bradford mostrou diferenças significativas em PT entre Saanen e Pardo-alpina (p0,05); e não foram encontradas diferenças entre raças na CN. Em conclusão, o método de Bradford apresentou a menor correlação (TP e CN) com o Kjeldahl, e por Bradofrd não foi mostrado o mesmo padrão de diferenças entre raças em PT e CN, como foi evidenciado por todos os outros métodos. Portanto, sugere-se que o método de Bradford não seja recomendado para a determinação de proteínas no leite de cabra.
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