Subunit components of casein micelles from bovine, ovine, caprine and equine milks

Ono, Tomotada; Kohno, Hiromasa; Odagiri, Satoshi; Takagi, Toshio

doi:10.1017/s0022029900026224

Cited by 25 publications

(11 citation statements)

References 9 publications

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“…Evidence for the presence of a κ-likecasein in mare milk is still quite contradictory, despite several studies on the subject [18,21,25,28]. No protein bands that were homologous to bovine κ-casein could be detected in urea electrophoregrams in this study.…”

Section: Does a κ-Like-casein Exist In Mare Milk?contrasting

confidence: 75%

Characterization of mare caseins. Identification of $\alpha_{{\bf S1}}$- and $\alpha_{{\bf S2}}$- caseins

Ochirkhuyag

Chobert²,

Dalgalarrondo³

et al. 2000

Lait

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-Whole mare (Mongolian and French breeds) casein was obtained from skim milk by isoelectric precipitation (pH 4.6) at 22 °C. In another series of experiments, equine caseins were fractionated after isoelectric precipitation at 4 °C, according to their sensitivity to temperature, on one hand, the pH of the resulting pellet was adjusted to 6.5 before centrifugation (45 000 g for 30 min) at 4 °C; on the resulting casein fraction which precipitated was named the cold precipitated (CP) fraction. On the other hand, the supernatant obtained from the centrifugation of skim milk at pH 4.6 and 4 °C was warmed to 30 °C before being centrifuged at 30 °C, 45 000 g, for 30 min. The resulting casein fraction which precipitated was named the thermally precipitated (TP) fraction. Equine caseins were then purified by high resolution gel chromatography on an anion-exchange column followed by reversed phase-high performance liquid chromatography. The casein fractions were analyzed by urea-and SDS-polyacrylamide gel electrophoresis, their amino acid compositions were determined and their first 15 N-terminal amino acids were sequenced. This analysis showed the presence of α slike caseins isolated from the CP fraction. α s1 -Like-casein showed 4 major double bands by electrofocusing with a pI range of 4.3-4.8. In the same conditions, α s2 -like casein showed 2 major bands with a pI range of 4.3-5.1. The TP fraction revealed the existence in equine milk of 6 subfractions of β-like caseins, occurring in the following ratios: 1:5:18:20:15:10, differing at least in their degree of phosphorylation (as shown also by the action of acid phosphatase). Since no evidence of the presence of κ-casein was found in equine milk, it is proposed that part of its functions in the milk of the Equidae could be assumed by the population of less phosphorylated β-caseins.

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Section: Does a κ-Like-casein Exist In Mare Milk?contrasting

confidence: 75%

Characterization of mare caseins. Identification of $\alpha_{{\bf S1}}$- and $\alpha_{{\bf S2}}$- caseins

Ochirkhuyag

Chobert²,

Dalgalarrondo³

et al. 2000

Lait

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“…Nos résultats sont assez proches de ceux obtenus par quelques autres auteurs (Juarez et al, 1984 ;Anifantakis, 1986 ;Ono et al, 1989). En revanche, Brochet (1982), Law et al (1992) Ekstrand et al, 1980 ;Niki et Arima, 1984 ;Ford et Grandison, 1986).…”

Section: Caractéristiques Micellairesunclassified

“…Ainsi en est-il de la taille des micelles, mesurée par microscopie électronique (Richardson et al, 1974 ;Saleem et al, 1986) ou par diffusion lumineuse (Lemoine, 1990). De même, les données concernant les proportions relatives des caséines obtenues par électrophorèse (Brochet, 1982 ;Juarez et al, 1984) ou par des techniques chromatographiques (Ono et al, 1989;Law et al, 1992 ;Muir et al, 1993) présentent une certaine hétérogénéité.…”

Section: Introductionunclassified

Évolution des caractéristiques physico-chimiques et des paramètres de coagulation du lait de brebis collecté dans la région de Roquefort

Pellegrini¹,

Remeuf²,

Rivemale

1994

Lait

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(Reçu le 8 avril 1994; accepté le 22 août 1994) Résumé -Les caractéristiques physico-chimiques et l'aptitude à la coagulation par la présure du lait de brebis collecté dans la région de Roquefort ont été suivies au cours d'une période de lactation. Les résultats obtenus mettent en évidence une évolution nette de la composition globale du lait au cours de la période de production. L'étude de la répartition du calcium et du phosphore inorganique entre les phases soluble et colloïdale fait apparaître une augmentation de la fraction colloïdale. Concernant les caractéristiques micellaires, on note un accroissement du diamètre des micelles et une diminution de la minéralisation calcique. Le degré d'hydratation des micelles et les proportions relatives des caséines évoluent peu. Le suivi des paramètres de coagulation montre une augmentation nette du temps de prise, s'accompagnant d'une réduction de la vitesse de raffermissement. La fermeté du gel croît légè-rement et l'aptitude à l'exsudation du lactosérum diminue.

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“…Lactic starter bacteria, which produce high proteolytic enzyme activities, could also contribute to the texture scores by accumulating higher amounts of soluble N and PTA-N fractions as ripening progressed (Litopoulou et al, 1993). It could be explained by the markedly discriminative in the structure; primary (Fiat and Jolles, 1989) and tertiary structures (Ono et al, 1989), smaller size (Martin, 1993;Grosclaude, 1995) and regular shape (Remeuf and Lenoir, 1986) of the casein micelles of caprine milk.…”

Section: Texture Profile Analysis Of Feta Cheesementioning

confidence: 99%

Fatty Acid Compositions and Physicochemical Properties of Feta Cheese Made from Bovine Milk

2006

Journal of Animal Science and Technology

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Subunit components of casein micelles from bovine, ovine, caprine and equine milks

Cited by 25 publications

References 9 publications

Characterization of mare caseins. Identification of $\alpha_{{\bf S1}}$- and $\alpha_{{\bf S2}}$- caseins

Characterization of mare caseins. Identification of $\alpha_{{\bf S1}}$- and $\alpha_{{\bf S2}}$- caseins

Évolution des caractéristiques physico-chimiques et des paramètres de coagulation du lait de brebis collecté dans la région de Roquefort

Fatty Acid Compositions and Physicochemical Properties of Feta Cheese Made from Bovine Milk

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