Charmian J. O'Connor, Peter Walde, Robert G. Wallace

Bile Salt Roles in Bile‐Salt‐Stimulated Lipase Activity

  • Gastroenterology
  • Pediatrics, Perinatology and Child Health

SummaryThe hydrolysis of 4‐nitrophenylacetate and phenylsalicylate, catalyzed by human milk lipase in the presence of a range of concentrations of sodium cholate, has been measured at pH 7.3 and 37.5°C, and maximum activity was observed for both substrates at 1 mmole/ dm−3 bile salt. Lineweaver‐Burk plots for the enzyme‐catalyzed hydrolysis of N‐methylindoxyl myristate and 4‐nitrophenyloctanoate yielded values of Km equal to 34 and 20 μmoles/dm−3, respectively. However, an increase in the concentration of the latter substrate beyond 10 μmoles/dm−3 was not accompanied by a corresponding increase in the rate of hydrolysis. Comparison of these hydrolysis data with literature data for a variety of hydrophobic substrates suggests that there are two roles for the bile salt in the enzyme‐catalyzed reaction—the first involving binding onto several sites on the enzyme, and the second solubilization of oil‐phase substrates.

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