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Method for the measurement of lipase activity in milk

Published online by Cambridge University Press:  01 August 1997

GERARD HUMBERT
Affiliation:
Laboratoire des BioSciences de l'Aliment, Unité associée INRA, Faculté des Sciences, Université Henri Poincaré-Nancy 1, BP 239, F-54506, Vandœuvre-lès-Nancy Cédex, France
MARIE-FRANCE GUINGAMP
Affiliation:
Laboratoire des BioSciences de l'Aliment, Unité associée INRA, Faculté des Sciences, Université Henri Poincaré-Nancy 1, BP 239, F-54506, Vandœuvre-lès-Nancy Cédex, France
GUY LINDEN
Affiliation:
Laboratoire des BioSciences de l'Aliment, Unité associée INRA, Faculté des Sciences, Université Henri Poincaré-Nancy 1, BP 239, F-54506, Vandœuvre-lès-Nancy Cédex, France
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Abstract

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Lipolysis has many effects in dairy technology. Undesirable consequences include deleterious effects on the organoleptic properties of milk and some cheeses; however, it is desirable in some other cheeses.

The usual methods for detecting lipolysis in milk measure the amounts of free fatty acids liberated from triacylglycerols (International Dairy Federation, 1991). Lipase activity is detected by incubation of samples with substrates such as tributyrin (Castberg et al. 1975) or triolein (Nilsson-Ehle & Schotz, 1976; Shirai et al. 1982). A few reports describe methods using synthetic chromogenic substrates, e.g. p-nitrophenyl butyrate (Shirai & Jackson, 1982), β-naphthyl caprylate (McKellar, 1986; McKellar & Cholette, 1986) or 4-methylumbelliferyl oleate (Stead, 1983). Tsakalidou et al. (1992) have developed the detection of esterase activities on electrophoresis gels.

Type
Research Article
Copyright
Proprietors of Journal of Dairy Research 1997