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Evaluation of a porous silica-based ion-exchange medium for the production of protein fractions from rennet- and acid-whey

Published online by Cambridge University Press:  01 June 2009

Paul J. Skudder
Paul J. Skudder
Affiliation:
*National Institute for Research in Dairying (University of Reading), Shinfield, Reading RG2 9 AT, UK
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Summary

The use of a silica-based ion-exchange medium for the recovery of protein from wheys prepared by treatment with rennet or with acid has been investigated. The protein capacity of the medium whilst maintaining an adsorption greater than 75% during the passage of rennet-and acid-whey was 0·079 and 0·053 g/g respectively. Bovine serum albumin (BSA), α-lactalbumin (α-la) and β-lactoglobulin (β-lg) adsorbed from acid-whey were mostly recovered in yields greater than 93% in an undenatured form essentially free of lactose and milk salts by elution using 0·1 M-HC1. With rennet-whey, BSA and part of the α-la were not recovered in the native form, probably because of proteolysis during elution by enzymes originating in the rennet used in the manufacture of the whey. There was, however, no effect on the recovery of native β-lg adsorbed by the medium. An unidentified proteinaceous fraction, thought to be of casein origin, was also adsorbed and recovered from rennet-whey. Fractions of the adsorbed proteins could not be obtained by eluting with a gradient increase in NaCl concentration. Nevertheless, purified β-lg was obtained by passing a large quantity of whey through the medium. This protein had a high affinity for the functional groups of the medium, to the extent that other proteins initially adsorbed were subsequently displaced. Unidentified proteinaceous material in rennet-whey also had a high affinity for the functional groups of the ion exchanger but most of this fraction could be removed by a pretreatment procedure which involved passing the whey through the medium at pH 5·0; unidentified material was selectively adsorbed at this pH. The medium could also be used to produce a fraction containing a mixture of BSA and α-la but it was not possible to separate these proteins.

Type
Original Articles
Information
Journal of Dairy Research , Volume 52 , Issue 1 , February 1985 , pp. 167 - 181
Copyright
Copyright © Proprietors of Journal of Dairy Research 1985

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