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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...

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Main Authors: Ahmad Kamarudin, Nor Hafizah, Raja Abdul Rahman, Raja Noor Zaliha, Mohamad Ali, Mohd Shukuri, Leow, Adam Thean Chor, Basri, Mahiran, Salleh, Abu Bakar
Format: Article
Language:English
Published: Springer 2014
Online Access:http://psasir.upm.edu.my/id/eprint/36194/1/A%20new%20cold.pdf
http://psasir.upm.edu.my/id/eprint/36194/
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spelling my.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
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
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.
format Article
author Ahmad Kamarudin, Nor Hafizah
Raja Abdul Rahman, Raja Noor Zaliha
Mohamad Ali, Mohd Shukuri
Leow, Adam Thean Chor
Basri, Mahiran
Salleh, Abu Bakar
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
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
title 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_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_sort new cold-adapted, organic solvent stable lipase from mesophilic staphylococcus epidermidis at2
publisher Springer
publishDate 2014
url http://psasir.upm.edu.my/id/eprint/36194/1/A%20new%20cold.pdf
http://psasir.upm.edu.my/id/eprint/36194/
_version_ 1643831676418129920
score 13.211869

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