Batch Fractionation of Bovine Caseins with Diethylaminoethyl Cellulose

Wei, Tsao-Chen; Whitney, R.McL.

doi:10.3168/jds.s0022-0302(85)81006-7

Cited by 21 publications

(13 citation statements)

References 22 publications

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“…Non-conjugated maltodextrin was removed from the crude NaCN-Md100 conjugate by batch DEAE anion exchange chromatography as follows: the crude conjugate was dispersed at 5%, (w/v) in a 0.01 M Imidazole HCl buffer, pH 7.4, containing 3.3 M Urea, 2 mM dithiothreitol (DTT) and 0.01%, (w/v) sodium azide (Wei & Whitney, 1985). DEAE cellulose (50 g, dry weight) was preswollen and equilibrated in the same Imidazole HCl buffer (200 ml) by gentle stirring (300 rpm) for 30 min.…”

Section: Conjugate Purificationmentioning

confidence: 99%

Heat stability and freeze–thaw stability of oil-in-water emulsions stabilised by sodium caseinate–maltodextrin conjugates

O’Regan

Mulvihill

2010

Food Chemistry

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Section: Conjugate Purificationmentioning

confidence: 99%

Heat stability and freeze–thaw stability of oil-in-water emulsions stabilised by sodium caseinate–maltodextrin conjugates

O’Regan

Mulvihill

2010

Food Chemistry

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“…Batch fractionation with DEAE-cellulose (Sigma D-8382) by means of successive extractions with 0-035, 0-085, 0-12 and 0-175 M-NaCl, according to the method of Wei & Whitney (1985), was used to fractionate the ovine a s -, /?-and /c-caseins. The fractions thus obtained were repurified by appropriate recycling, dialysed thoroughly and lyophilized.…”

Section: Casein Model Systemsmentioning

confidence: 99%

Proteolytic activity of two commercial proteinases from Aspergillus oryzae and Bacillus subtilis on ovine and bovine caseins

López‐Fandiño

Ramos

Fernández-Garcı́a

et al. 1991

Journal of Dairy Research

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SummaryElectrophoretic analysis of the action of two commercial enzymes, Neutrase 0·5 and MKC Fungal Protease, on whole casein and αs-, β- and κ-caseins from cows' and ewes' milk showed that Neutrase 0·5 chiefly degraded β-casein, giving rise to peptides soluble at pH 4·6 detectable by PAGE. In contrast, although MKC Fungal Protease caused intense hydrolysis of bovine β-casein, in ovine casein it resulted in more active degradation of αs- than β-casein. The latter enzyme did not produce peptides soluble at pH 4·6 detectable by PAGE. Both enzymes degraded κ-casein, yielding a breakdown product that exhibited an electrophoretic mobility similar to that of the breakdown product produced by the action of commercial rennet.

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“…The top fat layer was removed after centrifugation (1800 g, 4 mC, 15 min). Whole casein was obtained from skim milk by isoelectric precipitation at pH 4n6 (Wei & Whitney, 1984).…”

Section:    Purification Of β-Caseinmentioning

confidence: 99%

ELISA for monitoring the cleavage of β-casein at site Lys²⁸–Lys²⁹ by plasmin during Comté cheese ripening

Senocq

Dupont

Rolet-Répécaud

et al. 2002

Journal of Dairy Research

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Proteolysis of casein is the principal cause of textural changes and flavour development in ripened cheese (Fox & McSweeney, 1996). Caseins are degraded into small peptides and free amino acids during a complex process, described by Grappin et al. (1985) as a two-step scheme. Caseins are initially broken down into large, well characterised fragments. This initial step, called primary proteolysis, is catalysed principally by the residual coagulant (chymosin and pepsin), and to a variable extent by endogenous milk proteases, such as plasmin, cathepsin D, and possibly somatic cell proteinases. Enzymes originating from either rennet or milk are active in most ripened cheese varieties. However, their relative contributions vary substantially depending on manufacturing practices. For instance, in Swiss-type cheeses, cooking the curd extensively inactivates the coagulant, and simultaneously enhances plasmin activity, which therefore becomes predominant (Ollikainen & Kivela, 1989).

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Batch Fractionation of Bovine Caseins with Diethylaminoethyl Cellulose

Cited by 21 publications

References 22 publications

Heat stability and freeze–thaw stability of oil-in-water emulsions stabilised by sodium caseinate–maltodextrin conjugates

Heat stability and freeze–thaw stability of oil-in-water emulsions stabilised by sodium caseinate–maltodextrin conjugates

Proteolytic activity of two commercial proteinases from Aspergillus oryzae and Bacillus subtilis on ovine and bovine caseins

ELISA for monitoring the cleavage of β-casein at site Lys²⁸–Lys²⁹ by plasmin during Comté cheese ripening

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Batch Fractionation of Bovine Caseins with Diethylaminoethyl Cellulose

Cited by 21 publications

References 22 publications

Heat stability and freeze–thaw stability of oil-in-water emulsions stabilised by sodium caseinate–maltodextrin conjugates

Heat stability and freeze–thaw stability of oil-in-water emulsions stabilised by sodium caseinate–maltodextrin conjugates

Proteolytic activity of two commercial proteinases from Aspergillus oryzae and Bacillus subtilis on ovine and bovine caseins

ELISA for monitoring the cleavage of β-casein at site Lys28–Lys29 by plasmin during Comté cheese ripening

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ELISA for monitoring the cleavage of β-casein at site Lys²⁸–Lys²⁹ by plasmin during Comté cheese ripening