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In vitro proteolysis and functional properties of reductively alkylated β-casein derivatives

Published online by Cambridge University Press:  01 June 2009

Jean-Marc Chobert ,
Abdelmadjid Touati ,
Catherine Bertrand-Harb ,
Michele Dalgalarrondo ,
Marie-Georgette Nicolas  and
Tomasz Haertle
Jean-Marc Chobert
Affiliation:
Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, BP 527, 44026 Nantes Cédex 03, France
Abdelmadjid Touati
Affiliation:
Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, BP 527, 44026 Nantes Cédex 03, France
Catherine Bertrand-Harb
Affiliation:
Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, BP 527, 44026 Nantes Cédex 03, France
Michele Dalgalarrondo
Affiliation:
Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, BP 527, 44026 Nantes Cédex 03, France
Marie-Georgette Nicolas
Affiliation:
Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, BP 527, 44026 Nantes Cédex 03, France
Tomasz Haertle
Affiliation:
Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, BP 527, 44026 Nantes Cédex 03, France
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Summary

β-Casein amino groups were modified with aldehydes and dialdehydes via reductive alkylation at pH 8·0. The degree of alkylation was controlled by the amount of the alkylating reagent applied. The initial rates of α-chymotrypsin-catalysed hydrolysis of alkylated β-casein were inversely related to the size of the modifying group. Proteolysis of modified β-casein with trypsin (18 h) or with α-chymotrypsin (48 h) depended on the nature and size of the substituent applied. The measurements of tryptophan fluorescence indicate that the modifications also induced conformation change. Solubilities of methyl-, ethyl- or benzyl-β-casein slightly increased; solubilities of β-casein dialdehyde derivatives were significantly lower than that of native β-casein. Emulsion stability of methyl- or ethyl- β-casein was higher than that of native β-casein in the acidic pH range. After modification with glyoxal, the emulsifying activity and the emulsion stability of β-casein decreased. The emulsifying activity of benzyl- β-casein was lower than that of native β-casein. Phthalylated β-casein displayed the poorest emulsion stability.

Type
Original Articles
Information
Journal of Dairy Research , Volume 58 , Issue 3 , August 1991 , pp. 285 - 298
Copyright
Copyright © Proprietors of Journal of Dairy Research 1991

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