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Screening of lipase inhibitors from marine algae
Author(s) -
Bitou Nozomu,
Ninomiya Masayori,
Tsujita Takahiro,
Okuda Hiromichi
Publication year - 1999
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/s11745-999-0383-7
Subject(s) - triolein , lipase , chromatography , ethyl acetate , chemistry , hydrolysis , thin layer chromatography , silica gel , algae , glyceride , enzyme , biochemistry , fatty acid , biology , botany
The possible presence of an inhibitor of pancreatic lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) was screened in 54 marine algae. An active inhibitor, caulerpenyne, was purified from an extract of Caulerpa taxifolia , using ethyl acetate extraction, followed by successive chromatographies on ODS and silica gel columns. The purified inhibitor was identified by thin‐layer chromatography, infrared and nuclear magnetic resonance spectroscopy. Caulerpenyne competitively inhibited lipase activities using emulsified triolein and dispersed 4‐methylumbelliferyl oleate (4‐MU oleate) as substrates. The concentrations producing 50% inhibition against triolein and 4‐MU oleate hydrolysis were 2 mM and 13 μM, respectively. In vivo , oral administration of corn oil with or without caulerpenyne to rats demonstrated a reduced and delayed peak plasma triacylglycerol concentration with caulerpenyne.