Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/68107
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dc.contributor.authorLin, M.C.en_US
dc.contributor.authorHsieh, C.W.en_US
dc.contributor.authorTsai, H.J.en_US
dc.contributor.authorRo, Y.R.en_US
dc.contributor.authorLin, C.S.en_US
dc.contributor.authorLin, G.en_US
dc.date2008zh_TW
dc.date.accessioned2014-06-11T05:56:16Z-
dc.date.available2014-06-11T05:56:16Z-
dc.identifier.issn0970-7077zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/68107-
dc.description.abstractThe object of this work was to determine the enzyme kinetics for Pseudomonas species lipase catalyzed hydrolysis of substrate 4-nitrophenyl butyrate in the presence of nitro compounds such as nitroglycerin, 2,4,6-trinitrotoluene (TNT), picric acid, styphnic acid, hexahydro-1,3,5-trinitrotriazocine (RDX), octahydro-1,3,5,7-tetranitrotriazocine (HMX) and hexanitrohexaazaisowurtzitane (HNIW) in vitro. Kinetically, picric acid and styphnic acid were the mixed-type inhibitors but TNT, RDX and HNIW were the essential activators of the enzyme in the presence of a detergent triton-X 100. Interestingly, HMX and nitroglycerin were neither an inhibitor nor an activator of the enzyme. From chemical structure point of view, hydrophilic nitro compounds such as picric acid and styphnic acid are capable to enter, the hydrophilic active site of lipase and become inhibitors of the enzyme, while hydrophobic nitro compounds such as TNT, RDX and HNIW presumably mix with Triton-X-100 and bind to the co-lipase binding site of the enzyme and become the essential activators of the enzyme.en_US
dc.language.isoen_USzh_TW
dc.relationAsian Journal of Chemistryen_US
dc.relation.ispartofseriesAsian Journal of Chemistry, Volume 20, Issue 2, Page(s) 1217-1225.en_US
dc.subjectlipaseen_US
dc.subjectenzyme kineticsen_US
dc.subjectnitro compoundsen_US
dc.subjectenzyme activationen_US
dc.subjecttriacylglycerol lipaseen_US
dc.subjectlipolytic enzymesen_US
dc.subjectopen conformationen_US
dc.subjectcepaciaen_US
dc.subjectlipaseen_US
dc.subjectbinding siteen_US
dc.subjectcomplexen_US
dc.subjectinhibitionen_US
dc.subjectactivationen_US
dc.titleInteraction mechanism between Pseudomonas species lipase and nitro compoundsen_US
dc.typeJournal Articlezh_TW
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