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Abstract
The hydrolysis of ascorbate mono-, tri- and polyphosphates by trout intestinal alkaline phosphatase was examined. Km values were established as 1.19, 4.1 and 3.7 mM, respectively. The enzyme catalyzed ascorbate triphosphate hydrolysis with 60% efficiency of that for ascorbate monophosphate. With the Km value of 1.19 mM for ascorbate monophosphate the trout enzyme exhibits similar affinity with this substrate as with p-nitrophenyl phosphate (1.00–1.67 mM). Two Km values for micro- and millimolar ranges of ascorbate monophosphate concentrations ranges were calculated as: 27.9 μM and 1.19 mM, respectively. Specific intestinal alkaline phosphatase inhibitor L-phenylalanine (100 mM), inhibited reaction rate by 20% in 10 min. We conclude that alkaline phosphatase, which is in a great abundance in the trout intestine, serves as ascorbate esters hydrolase, thus releasing active ascorbic acid into circulation.
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