A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2
The gene encoding a cold-adapted, organic solvent stable lipase from a local soil-isolate, mesophilic Staphylococcus epidermidis AT2 was expressed in a prokaryotic system. A two-step purification of AT2 lipase was achieved using butyl sepharose and DEAE sepharose column chromatography. The final rec...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Springer
2014
|
| Online Access: | http://psasir.upm.edu.my/id/eprint/36194/1/A%20new%20cold.pdf |
| _version_ | 1825948794123976704 |
|---|---|
| author | Ahmad Kamarudin, Nor Hafizah Raja Abdul Rahman, Raja Noor Zaliha Mohamad Ali, Mohd Shukuri Leow, Adam Thean Chor Basri, Mahiran Salleh, Abu Bakar |
| author_facet | Ahmad Kamarudin, Nor Hafizah Raja Abdul Rahman, Raja Noor Zaliha Mohamad Ali, Mohd Shukuri Leow, Adam Thean Chor Basri, Mahiran Salleh, Abu Bakar |
| author_sort | Ahmad Kamarudin, Nor Hafizah |
| collection | UPM |
| description | The gene encoding a cold-adapted, organic solvent stable lipase from a local soil-isolate, mesophilic Staphylococcus epidermidis AT2 was expressed in a prokaryotic system. A two-step purification of AT2 lipase was achieved using butyl sepharose and DEAE sepharose column chromatography. The final recovery and purification fold were 47.09 % and 3.45, respectively. The molecular mass of the purified lipase was estimated to be 43 kDa. AT2 lipase was found to be optimally active at pH 8 and stable at pH 6–9. Interestingly, this enzyme demonstrated remarkable stability at cold temperature (<30 °C) and exhibited optimal activity at a temperature of 25 °C. A significant enhancement of the lipolytic activity was observed in the presence of Ca2+, Tween 60 and Tween 80. Phenylmethylsulfonylfluoride, a well known serine inhibitor did not cause complete inhibition of the enzymatic activity. AT2 lipase exhibited excellent preferences towards long chain triglycerides and natural oils. The lipolytic activity was stimulated by dimethylsulfoxide and diethyl ether, while more than 50 % of its activity was retained in methanol, ethanol, acetone, toluene, and n-hexane. Taken together, AT2 lipase revealed highly attractive biochemical properties especially because of its stability at low temperature and in organic solvents. |
| first_indexed | 2024-03-06T08:34:36Z |
| format | Article |
| id | upm.eprints-36194 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T08:34:36Z |
| publishDate | 2014 |
| publisher | Springer |
| record_format | dspace |
| spelling | upm.eprints-361942015-09-01T04:15:33Z http://psasir.upm.edu.my/id/eprint/36194/ A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2 Ahmad Kamarudin, Nor Hafizah Raja Abdul Rahman, Raja Noor Zaliha Mohamad Ali, Mohd Shukuri Leow, Adam Thean Chor Basri, Mahiran Salleh, Abu Bakar The gene encoding a cold-adapted, organic solvent stable lipase from a local soil-isolate, mesophilic Staphylococcus epidermidis AT2 was expressed in a prokaryotic system. A two-step purification of AT2 lipase was achieved using butyl sepharose and DEAE sepharose column chromatography. The final recovery and purification fold were 47.09 % and 3.45, respectively. The molecular mass of the purified lipase was estimated to be 43 kDa. AT2 lipase was found to be optimally active at pH 8 and stable at pH 6–9. Interestingly, this enzyme demonstrated remarkable stability at cold temperature (<30 °C) and exhibited optimal activity at a temperature of 25 °C. A significant enhancement of the lipolytic activity was observed in the presence of Ca2+, Tween 60 and Tween 80. Phenylmethylsulfonylfluoride, a well known serine inhibitor did not cause complete inhibition of the enzymatic activity. AT2 lipase exhibited excellent preferences towards long chain triglycerides and natural oils. The lipolytic activity was stimulated by dimethylsulfoxide and diethyl ether, while more than 50 % of its activity was retained in methanol, ethanol, acetone, toluene, and n-hexane. Taken together, AT2 lipase revealed highly attractive biochemical properties especially because of its stability at low temperature and in organic solvents. Springer 2014 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/36194/1/A%20new%20cold.pdf Ahmad Kamarudin, Nor Hafizah and Raja Abdul Rahman, Raja Noor Zaliha and Mohamad Ali, Mohd Shukuri and Leow, Adam Thean Chor and Basri, Mahiran and Salleh, Abu Bakar (2014) A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2. The Protein Journal, 33 (3). pp. 296-307. ISSN 1573-4943; ESSN: 1572-3887 10.1007/s10930-014-9560-3 |
| spellingShingle | Ahmad Kamarudin, Nor Hafizah Raja Abdul Rahman, Raja Noor Zaliha Mohamad Ali, Mohd Shukuri Leow, Adam Thean Chor Basri, Mahiran Salleh, Abu Bakar A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2 |
| title | A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2 |
| title_full | A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2 |
| title_fullStr | A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2 |
| title_full_unstemmed | A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2 |
| title_short | A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2 |
| title_sort | new cold adapted organic solvent stable lipase from mesophilic staphylococcus epidermidis at2 |
| url | http://psasir.upm.edu.my/id/eprint/36194/1/A%20new%20cold.pdf |
| work_keys_str_mv | AT ahmadkamarudinnorhafizah anewcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT rajaabdulrahmanrajanoorzaliha anewcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT mohamadalimohdshukuri anewcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT leowadamtheanchor anewcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT basrimahiran anewcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT sallehabubakar anewcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT ahmadkamarudinnorhafizah newcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT rajaabdulrahmanrajanoorzaliha newcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT mohamadalimohdshukuri newcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT leowadamtheanchor newcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT basrimahiran newcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 AT sallehabubakar newcoldadaptedorganicsolventstablelipasefrommesophilicstaphylococcusepidermidisat2 |