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Bile-Salt-Stimulated Human Milk Lipase: Interaction with Proteins

Chemistry Department University of Auckland Private Bag Auckland, New Zealand

Paul A.G. Butler

Chemistry Department University of Auckland Private Bag Auckland, New Zealand

Bridget M. Sutton

Chemistry Department University of Auckland Private Bag Auckland, New Zealand

The initial rates of hydrolysis of triolein, catalyzed by bile-salt-stimulated hu man milk lipase, BSSL, were measured at pH 7.5 and 37 ° C, in the presence of selected proteins, namely immunoglobulin A, -lactalbumin, lactoferrin, hen egg white lysozyme, pancreatic lipase, myoglobin and the very surface active protein melittin. The esterase activity of the enzyme against 4-nitro- phenylacetate was also measured in the presence of a number of different samples of lactoferrin. Under the conditions used, -lactalbumin and hen egg white lysozyme had almost no effect on the lipase activity. Immunoglobulin A was slightly inhibitory; lactoferrin, pancreatic lipase and myoglobin were all partially inhibitory; and melittin was capable of almost completely inac tivating the lipase.

Journal of Bioactive and Compatible Polymers, Vol. 3, No. 4, 390-402 (1988)
DOI: 10.1177/088391158800300405


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