Purification and characterization of an extracellular lipase from a novel strain Penicillium sp. DS-39 (DSM 23773)

[Display omitted] • An extracellular lipase (PEL) produced by Penicillium sp. DSM 23773 was purified. • A 129-fold purification, with a specific activity of 308.73 IU/mg, was achieved. • PEL showed high thermostability uncommon in lipases from mesophilic fungi. • PEL was stable, with activation, in...

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Veröffentlicht in:Journal of molecular catalysis. B, Enzymatic Enzymatic, 2011-11, Vol.72 (3), p.256-262
Hauptverfasser: Dheeman, Dharmendra S., Antony-Babu, Sanjay, Frías, Jesús M., Henehan, Gary T.M.
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container_issue 3
container_start_page 256
container_title Journal of molecular catalysis. B, Enzymatic
container_volume 72
creator Dheeman, Dharmendra S.
Antony-Babu, Sanjay
Frías, Jesús M.
Henehan, Gary T.M.
description [Display omitted] • An extracellular lipase (PEL) produced by Penicillium sp. DSM 23773 was purified. • A 129-fold purification, with a specific activity of 308.73 IU/mg, was achieved. • PEL showed high thermostability uncommon in lipases from mesophilic fungi. • PEL was stable, with activation, in organic solvents (50%, v/v) with log P ≥ 2.0. • PEL is a potentially useful biocatalyst for various industrial applications. A newly isolated fungal strain, Penicillium sp. DS-39 (DSM 23773), was found to produce an inducible extracellular lipase when grown in a medium containing 1.0% (v/v) olive oil. Maximum lipase activity was obtained after 120 h of incubation at 28 °C. The lipase was purified 129-fold with a final specific activity of 308.73 IU/mg. The molecular weight of the homogeneous lipase was 43 kDa as determined by SDS-PAGE. It was optimally active at pH 5.5 and 45 °C. The lipase was most active on triolein and exhibited a broad substrate range with a preference for triacylglycerols containing long chain unsaturated fatty acids. It showed no regio-specificity for the ester bond in triolein. It was activated by Ca 2+ and Mn 2+, while significant inhibition was observed with Hg 2+ and Zn 2+. The lipase showed significant stability and activation in the presence of organic solvents with log P ≥ 2.0. These features render Penicillium sp. DS-39 lipase (PEL) a potential biocatalyst for applications such as biodiesel production, enzymatic restructuring, by interesterification of different oils and fats, and biodegradation of oil spills in the environment.
doi_str_mv 10.1016/j.molcatb.2011.06.013
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The lipase was purified 129-fold with a final specific activity of 308.73 IU/mg. The molecular weight of the homogeneous lipase was 43 kDa as determined by SDS-PAGE. It was optimally active at pH 5.5 and 45 °C. The lipase was most active on triolein and exhibited a broad substrate range with a preference for triacylglycerols containing long chain unsaturated fatty acids. It showed no regio-specificity for the ester bond in triolein. It was activated by Ca 2+ and Mn 2+, while significant inhibition was observed with Hg 2+ and Zn 2+. The lipase showed significant stability and activation in the presence of organic solvents with log P ≥ 2.0. These features render Penicillium sp. 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DS-39 (DSM 23773)</title><title>Journal of molecular catalysis. B, Enzymatic</title><description>[Display omitted] • An extracellular lipase (PEL) produced by Penicillium sp. DSM 23773 was purified. • A 129-fold purification, with a specific activity of 308.73 IU/mg, was achieved. • PEL showed high thermostability uncommon in lipases from mesophilic fungi. • PEL was stable, with activation, in organic solvents (50%, v/v) with log P ≥ 2.0. • PEL is a potentially useful biocatalyst for various industrial applications. A newly isolated fungal strain, Penicillium sp. DS-39 (DSM 23773), was found to produce an inducible extracellular lipase when grown in a medium containing 1.0% (v/v) olive oil. Maximum lipase activity was obtained after 120 h of incubation at 28 °C. The lipase was purified 129-fold with a final specific activity of 308.73 IU/mg. The molecular weight of the homogeneous lipase was 43 kDa as determined by SDS-PAGE. It was optimally active at pH 5.5 and 45 °C. The lipase was most active on triolein and exhibited a broad substrate range with a preference for triacylglycerols containing long chain unsaturated fatty acids. It showed no regio-specificity for the ester bond in triolein. It was activated by Ca 2+ and Mn 2+, while significant inhibition was observed with Hg 2+ and Zn 2+. The lipase showed significant stability and activation in the presence of organic solvents with log P ≥ 2.0. These features render Penicillium sp. DS-39 lipase (PEL) a potential biocatalyst for applications such as biodiesel production, enzymatic restructuring, by interesterification of different oils and fats, and biodegradation of oil spills in the environment.</description><subject>biocatalysts</subject><subject>Bioconversions. Hemisynthesis</subject><subject>biodegradation</subject><subject>biodiesel</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>calcium</subject><subject>catalytic activity</subject><subject>Characterization</subject><subject>Extracellular lipase</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>fungi</subject><subject>Life Sciences</subject><subject>long chain unsaturated fatty acids</subject><subject>manganese</subject><subject>mercury</subject><subject>Methods. Procedures. Technologies</subject><subject>molecular weight</subject><subject>oil spills</subject><subject>olive oil</subject><subject>Organic solvent-tolerant lipase</subject><subject>Penicillium</subject><subject>Penicillium sp. DS-39</subject><subject>polyacrylamide gel electrophoresis</subject><subject>Purification</subject><subject>solvents</subject><subject>triolein</subject><subject>zinc</subject><issn>1381-1177</issn><issn>1873-3158</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNqFkVFrFDEUhQdRsFZ_gpgXwT7MeG8yM8k8SWm1LaxYWPsc7mTu2CzZmSXZXdRfb5YpffUp4fCdQ_hSFO8RKgRsP2-q7Rwc7ftKAmIFbQWoXhRnaLQqFTbmZb4rgyWi1q-LNyltAEAimrMi3h-iH31u-3kSNA3CPVIkt-fo_y7hPOZc8O99jjmEQ6Aogt9RYjHGeStITPORg0gZ8JO458k7H4I_bEXaVeJ6XapOfLpefxdSaa0u3havRgqJ3z2d58XDt68_r27L1Y-bu6vLVelUp_elgd7IgVXdmV4z9cjECHXDA9ZErcRaghsc92boRw1GGoa6ZqX6TjoFgzovLpbdRwp2F_2W4h87k7e3lyt7ykC2dYe6OWJmm4V1cU4p8vhcQLAnyXZjnyTbk2QLrc2Sc-_j0ss6HIUx0uR8ei7LumlAm9P-h4Ubabb0K2bmYZ2H2vwRLUgJmfiyEJyVHD1Hm5znyfHgI7u9HWb_n7f8A03HnP0</recordid><startdate>20111101</startdate><enddate>20111101</enddate><creator>Dheeman, Dharmendra S.</creator><creator>Antony-Babu, Sanjay</creator><creator>Frías, Jesús M.</creator><creator>Henehan, Gary T.M.</creator><general>Elsevier B.V</general><general>Elsevier</general><general>Elsevier [1995, vol. 1, iss. 1-2016, vol. 134]</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope></search><sort><creationdate>20111101</creationdate><title>Purification and characterization of an extracellular lipase from a novel strain Penicillium sp. 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Technologies</topic><topic>molecular weight</topic><topic>oil spills</topic><topic>olive oil</topic><topic>Organic solvent-tolerant lipase</topic><topic>Penicillium</topic><topic>Penicillium sp. DS-39</topic><topic>polyacrylamide gel electrophoresis</topic><topic>Purification</topic><topic>solvents</topic><topic>triolein</topic><topic>zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dheeman, Dharmendra S.</creatorcontrib><creatorcontrib>Antony-Babu, Sanjay</creatorcontrib><creatorcontrib>Frías, Jesús M.</creatorcontrib><creatorcontrib>Henehan, Gary T.M.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of molecular catalysis. 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DSM 23773 was purified. • A 129-fold purification, with a specific activity of 308.73 IU/mg, was achieved. • PEL showed high thermostability uncommon in lipases from mesophilic fungi. • PEL was stable, with activation, in organic solvents (50%, v/v) with log P ≥ 2.0. • PEL is a potentially useful biocatalyst for various industrial applications. A newly isolated fungal strain, Penicillium sp. DS-39 (DSM 23773), was found to produce an inducible extracellular lipase when grown in a medium containing 1.0% (v/v) olive oil. Maximum lipase activity was obtained after 120 h of incubation at 28 °C. The lipase was purified 129-fold with a final specific activity of 308.73 IU/mg. The molecular weight of the homogeneous lipase was 43 kDa as determined by SDS-PAGE. It was optimally active at pH 5.5 and 45 °C. The lipase was most active on triolein and exhibited a broad substrate range with a preference for triacylglycerols containing long chain unsaturated fatty acids. It showed no regio-specificity for the ester bond in triolein. It was activated by Ca 2+ and Mn 2+, while significant inhibition was observed with Hg 2+ and Zn 2+. The lipase showed significant stability and activation in the presence of organic solvents with log P ≥ 2.0. These features render Penicillium sp. DS-39 lipase (PEL) a potential biocatalyst for applications such as biodiesel production, enzymatic restructuring, by interesterification of different oils and fats, and biodegradation of oil spills in the environment.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><doi>10.1016/j.molcatb.2011.06.013</doi><tpages>7</tpages></addata></record>
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identifier ISSN: 1381-1177
ispartof Journal of molecular catalysis. B, Enzymatic, 2011-11, Vol.72 (3), p.256-262
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1873-3158
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subjects biocatalysts
Bioconversions. Hemisynthesis
biodegradation
biodiesel
Biological and medical sciences
Biotechnology
calcium
catalytic activity
Characterization
Extracellular lipase
Fundamental and applied biological sciences. Psychology
fungi
Life Sciences
long chain unsaturated fatty acids
manganese
mercury
Methods. Procedures. Technologies
molecular weight
oil spills
olive oil
Organic solvent-tolerant lipase
Penicillium
Penicillium sp. DS-39
polyacrylamide gel electrophoresis
Purification
solvents
triolein
zinc
title Purification and characterization of an extracellular lipase from a novel strain Penicillium sp. DS-39 (DSM 23773)
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