Purification and characterization of lipase from a thermoactinomyces species. (c2006)
Includes bibliographical references.
محفوظ في:
| المؤلف الرئيسي: | |
|---|---|
| التنسيق: | masterThesis |
| منشور في: |
2006
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| الموضوعات: | |
| الوصول للمادة أونلاين: | http://hdl.handle.net/10725/1017 https://doi.org/10.26756/th.2006.65 |
| الوسوم: |
إضافة وسم
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| _version_ | 1864513455722070016 |
|---|---|
| author | Thoumy, Jana Joseph |
| author_facet | Thoumy, Jana Joseph |
| author_role | author |
| dc.creator.none.fl_str_mv | Thoumy, Jana Joseph |
| dc.date.none.fl_str_mv | 2006 2006-02-10 2011-11-21T11:53:49Z 2011-11-21T11:53:49Z 2011-11-21 |
| dc.identifier.none.fl_str_mv | http://hdl.handle.net/10725/1017 https://doi.org/10.26756/th.2006.65 |
| dc.language.none.fl_str_mv | en |
| dc.publisher.none.fl_str_mv | Lebanese American University |
| dc.rights.*.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Lipase Enzymes -- Purification |
| dc.title.none.fl_str_mv | Purification and characterization of lipase from a thermoactinomyces species. (c2006) |
| dc.type.none.fl_str_mv | Thesis info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/masterThesis |
| description | Includes bibliographical references. |
| eu_rights_str_mv | openAccess |
| format | masterThesis |
| id | LAURepo_d6091ce6b91ed9210232eeb74cba9df7 |
| language_invalid_str_mv | en |
| network_acronym_str | LAURepo |
| network_name_str | Lebanese American University repository |
| oai_identifier_str | oai:laur.lau.edu.lb:10725/1017 |
| publishDate | 2006 |
| publisher.none.fl_str_mv | Lebanese American University |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| spelling | Purification and characterization of lipase from a thermoactinomyces species. (c2006)Thoumy, Jana JosephLipaseEnzymes -- PurificationIncludes bibliographical references.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+.1 bound copy: viii, 37 leaves; col. ill.; 30 cm. Available at RNL.Lebanese American University2011-11-21T11:53:49Z2011-11-21T11:53:49Z20062011-11-212006-02-10Thesisinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesishttp://hdl.handle.net/10725/1017https://doi.org/10.26756/th.2006.65eninfo:eu-repo/semantics/openAccessoai:laur.lau.edu.lb:10725/10172020-05-18T14:53:48Z |
| spellingShingle | Purification and characterization of lipase from a thermoactinomyces species. (c2006) Thoumy, Jana Joseph Lipase Enzymes -- Purification |
| status_str | publishedVersion |
| title | Purification and characterization of lipase from a thermoactinomyces species. (c2006) |
| title_full | Purification and characterization of lipase from a thermoactinomyces species. (c2006) |
| title_fullStr | Purification and characterization of lipase from a thermoactinomyces species. (c2006) |
| title_full_unstemmed | Purification and characterization of lipase from a thermoactinomyces species. (c2006) |
| title_short | Purification and characterization of lipase from a thermoactinomyces species. (c2006) |
| title_sort | Purification and characterization of lipase from a thermoactinomyces species. (c2006) |
| topic | Lipase Enzymes -- Purification |
| url | http://hdl.handle.net/10725/1017 https://doi.org/10.26756/th.2006.65 |