| Purification and characterization of intracellular lipase from the polyunsaturated fatty acid-producing fungus Mortierella alliacea. | |
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MedLine Citation:
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PMID: 20932946 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Previous studies on an arachidonic acid-producing fungus, Mortierella alliacea YN-15, suggested that its intracellular lipase plays an important role in the metabolism of exogenous and storage lipids. The lipase purified in this study through acetone precipitation and three-step chromatography was estimated to be about 11kDa in size by SDS-PAGE and mass spectrometry, and it tended to form large aggregates in aqueous solution. The purified lipase retained its activity over wide ranges of pH (2-12) and temperature (20-80°C). Its activity was enhanced by the Ca(2+) ion and reduced by some heavy metal ions, such as Zn(2+) and Hg(2+), and diethylpyrocarbonate. Among the various substrates tested, monoacylglycerols containing long-chain unsaturated fatty acids and phosphatidylcholine were preferentially hydrolyzed over triacylglycerols and fatty acid methyl esters. The lipase strongly hydrolyzed the sn-1/3 ester bonds and weakly hydrolyzed the sn-2 ester bonds of triolein, and it also catalyzed the acylglycerol synthesis reaction in a solvent-free two-phase system. The results indicate that triacylglycerol may be formed via 2-monoacylglycerol. Thus, the highly stable M. alliacea lipase may be useful for the synthesis of structured lipids, particularly acylglycerols containing functional unsaturated fatty acids at the sn-2 position. |
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Authors:
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Worapol Jermsuntiea; Tsunehiro Aki; Rieko Toyoura; Kazuhiro Iwashita; Seiji Kawamoto; Kazuhisa Ono |
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Publication Detail:
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Type: Journal Article Date: 2010-10-12 |
Journal Detail:
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Title: New biotechnology Volume: 28 ISSN: 1876-4347 ISO Abbreviation: N Biotechnol Publication Date: 2011 Feb |
Date Detail:
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Created Date: 2011-02-07 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101465345 Medline TA: N Biotechnol Country: Netherlands |
Other Details:
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Languages: eng Pagination: 158-64 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier B.V. All rights reserved. |
Affiliation:
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Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8530, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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