Purification and characterization of lipase from a thermoactinomyces species. (c2006)

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dc.contributor.author Thoumy, Jana Joseph
dc.date.accessioned 2011-11-21T11:53:49Z
dc.date.available 2011-11-21T11:53:49Z
dc.date.copyright 2006 en_US
dc.date.issued 2011-11-21
dc.date.submitted 2006-02-10
dc.identifier.uri http://hdl.handle.net/10725/1017
dc.description Includes bibliographical references. en_US
dc.description.abstract An extracellular lipase with a molecular weight of 99 KDa from a Thermoactinomycete sp. isolated from an olive oil contaminated soil (Al Koura, Lebanon) was purified using ammonium sulphate, Sephadex G-25 and ion exchange chromatography (DEAE cellulose). The enzyme had more affinity to p- nitrophenyllaurate than to 0- nitrophenyllaurate and it was stable after boiling for 1 hour while the purified fraction showed activity only at 60°C. Enzyme activity was measured in the presence of different substrates and a high affinity to p- nitrophenyl palmitate and p- nitrophenyl laurate, was detected. However, the enzyme didn't react at all with tripalmitin, trierucin, trielaidin, 1,3 diolein and triolein. The presence of metal ions like Ca2+ and Fe3+ activated the enzyme, while Co2+, Mg2+, Zn2+, and Fe2+ totally inhibited the lipase activity. Finally, the lipase had a short shelf life, even in the presence of Ca2+. en_US
dc.language.iso en en_US
dc.subject Lipase en_US
dc.subject Enzymes -- Purification en_US
dc.title Purification and characterization of lipase from a thermoactinomyces species. (c2006) en_US
dc.type Thesis en_US
dc.term.submitted Fall en_US
dc.author.degree MS in Molecular Biology en_US
dc.author.school Arts and Sciences en_US
dc.author.idnumber 199831500 en_US
dc.author.commembers Dr. Costantine Daher
dc.author.commembers Dr. Sima Tokajian
dc.author.woa OA en_US
dc.description.physdesc 1 bound copy: viii, 37 leaves; col. ill.; 30 cm. Available at RNL. en_US
dc.author.division Biology en_US
dc.author.advisor Dr. Fuad Hashwa
dc.identifier.doi https://doi.org/10.26756/th.2006.65 en_US
dc.publisher.institution Lebanese American University en_US

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