Purification and characterization of glycerolipid acyl-hydrolase from the red alga Gracilaria vermiculophylla |
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Authors: | Muhammad I Illijas Masaru Terasaki Ryo Nakamura Noriaki Iijima Akihiko Hara Nobuhiro Fusetani Yutaka Itabashi |
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Institution: | Faculty of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611, and;Gaduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima, Hiroshima 739-8528, Japan |
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Abstract: | ABSTRACT: A glycerolipid acyl-hydrolase was purified 19-fold with a yield of 11% from the prostaglandin-producing red alga Gracilaria vermiculophylla by ammonium sulfate precipitation, anion-exchange chromatoraphy and gel filtration chromatography. Sodium dodecylsulfate– polyacrylamide gel electrophoresis of the final preparation showed a single band corresponding to a molecular mass of 20 kDa, but Superdex 200 fast protein liquid chromatography exhibited a molecular mass of 40 kDa. Accordingly, it was suggested that the purified enzyme was a homodimer of a 20 kDa subunit. The optimal temperature and pH were 37°C and 7–8, respectively. The purified enzyme catalyzed hydrolysis of the acyl groups of both glycoglycerolipids and phospholipids, especially monogalactosyldiacylglycerol and phosphatidylcholine. These results suggest that the enzyme hydrolyze the membrane lipids of the alga to release various saturated and unsaturated fatty acids, including arachidonic acid as substrate for prostaglandin synthesis. |
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Keywords: | arachidonic acid glycerolipid acyl-hydrolase glycerophospholipids glycoglycerolipids Gracilaria vermiculophylla prostagalandins red alga |
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