Biochemical characterization of an alkaline and detergent-stable Lipase from Fusarium annulatum Bugnicourt strain CBS associated with olive tree dieback
This work describes a novel extracellular lipolytic carboxylester hydrolase named FAL, with lipase and phospholipase A1 (PLA1) activity, from a newly isolated filamentous fungus Ascomycota CBS strain, identified as Fusarium annulatum Bunigcourt. FAL was purified to about 62-fold using ammonium sulph...
Gespeichert in:
| Veröffentlicht in: | PloS one 2023-05, Vol.18 (5), p.e0286091-e0286091 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | e0286091 |
|---|---|
| container_issue | 5 |
| container_start_page | e0286091 |
| container_title | PloS one |
| container_volume | 18 |
| creator | Dab, Ahlem Hasnaoui, Ismail Mechri, Sondes Allala, Fawzi Bouacem, Khelifa Noiriel, Alexandre Bouanane-Darenfed, Amel Saalaoui, Ennouamane Asehraou, Abdeslam Wang, Fanghua Abousalham, Abdelkarim Jaouadi, Bassem |
| description | This work describes a novel extracellular lipolytic carboxylester hydrolase named FAL, with lipase and phospholipase A1 (PLA1) activity, from a newly isolated filamentous fungus Ascomycota CBS strain, identified as Fusarium annulatum Bunigcourt. FAL was purified to about 62-fold using ammonium sulphate precipitation, Superdex® 200 Increase gel filtration and Q-Sepharose Fast Flow columns, with a total yield of 21%. The specific activity of FAL was found to be 3500 U/mg at pH 9 and 40°C and 5000 U/mg at pH 11 and 45°C, on emulsions of triocanoin and egg yolk phosphatidylcholine, respectively. SDS-PAGE and zymography analysis estimated the molecular weight of FAL to be 33 kDa. FAL was shown to be a PLA1 with a regioselectivity to the sn-1 position of surface-coated phospholipids esterified with α-eleostearic acid. FAL is a serine enzyme since its activity on triglycerides and phospholipids was completely inhibited by the lipase inhibitor Orlistat (40 μM). Interestingly, compared to Fusarium graminearum lipase (GZEL) and the Thermomyces lanuginosus lipase (Lipolase®), this novel fungal (phospho)lipase showed extreme tolerance to the presence of non-polar organic solvents, non-ionic and anionic surfactants, and oxidants, in addition to significant compatibility and stability with some available laundry detergents. The analysis of washing performance showed that it has the capability to efficiently eliminate oil-stains. Overall, FAL could be an ideal choice for application in detergents. |
| doi_str_mv | 10.1371/journal.pone.0286091 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_2815933715</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A749857565</galeid><doaj_id>oai_doaj_org_article_6f786c1b4bba4dacb7398b3e4d7cc644</doaj_id><sourcerecordid>A749857565</sourcerecordid><originalsourceid>FETCH-LOGICAL-c727t-7a33db79dcf6ab8846547ba30ae1d50ce1df40476c2aaf7f9a54836255a45db63</originalsourceid><addsrcrecordid>eNqNk99v0zAQxyMEYmPwHyCwhITYQ0scO3byhLaKsUqVJjHg1brYTuPNjTvbGT_-Ev5cnLWb1mkPKJJ9On_u6_PlLste43yKCccfL9zge7DTtev1NC8qltf4SbaPa1JMWJGTp_fsvexFCBd5XpKKsefZHuFFXrIS72d_j42TnV4ZCRbJDjzIqL35A9G4HrkWQY_AXoI1vU62Qkqn86Xu4yREaKxGC7OGoFHr3QqdDAG8GVaJ7AcLMVnHw7I3MuUaUYgeTI9mx-cIQnDSQNQK_TSxQ86aa42i1xopoxuQly-zZy3YoF9t94Ps-8nnb7PTyeLsy3x2tJhIXvA44UCIanitZMugqSrKSsobIDlorMpcprWlOeVMFgAtb2soaUVYUZZAS9UwcpC93eiurQtiW9QgigqXNUl1LhMx3xDKwYVYe7MC_1s4MOLG4fxSgI9GWi1YyysmcUObBqgC2XBSVw3RVHEpGaVJ69P2tqFZaSVTHT3YHdHdk950YumuBc5xXZWcJIXDjUL3IO70aCFGX04ZoZTxa5zYD9vbvLsadIhiZYLU1kKv3XDzSMYZTVtC3z1AHy_FllpCeq3pW5eSlKOoOOJ0TDB1VaKmj1DpU2OfpXZtTfLvBBzuBCQm6l9xCUMIYn7-9f_Zsx-77Pt7bKfBxi44O4y9HXZBugGldyF43d5VFudinLbbaohx2sR22lLYm_t_8y7odrzIP4ZkJ0c</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2815933715</pqid></control><display><type>article</type><title>Biochemical characterization of an alkaline and detergent-stable Lipase from Fusarium annulatum Bugnicourt strain CBS associated with olive tree dieback</title><source>PubMed Central Free</source><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Public Library of Science (PLoS) Journals Open Access</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Dab, Ahlem ; Hasnaoui, Ismail ; Mechri, Sondes ; Allala, Fawzi ; Bouacem, Khelifa ; Noiriel, Alexandre ; Bouanane-Darenfed, Amel ; Saalaoui, Ennouamane ; Asehraou, Abdeslam ; Wang, Fanghua ; Abousalham, Abdelkarim ; Jaouadi, Bassem</creator><contributor>Nevárez-Moorillón, Guadalupe Virginia</contributor><creatorcontrib>Dab, Ahlem ; Hasnaoui, Ismail ; Mechri, Sondes ; Allala, Fawzi ; Bouacem, Khelifa ; Noiriel, Alexandre ; Bouanane-Darenfed, Amel ; Saalaoui, Ennouamane ; Asehraou, Abdeslam ; Wang, Fanghua ; Abousalham, Abdelkarim ; Jaouadi, Bassem ; Nevárez-Moorillón, Guadalupe Virginia</creatorcontrib><description>This work describes a novel extracellular lipolytic carboxylester hydrolase named FAL, with lipase and phospholipase A1 (PLA1) activity, from a newly isolated filamentous fungus Ascomycota CBS strain, identified as Fusarium annulatum Bunigcourt. FAL was purified to about 62-fold using ammonium sulphate precipitation, Superdex® 200 Increase gel filtration and Q-Sepharose Fast Flow columns, with a total yield of 21%. The specific activity of FAL was found to be 3500 U/mg at pH 9 and 40°C and 5000 U/mg at pH 11 and 45°C, on emulsions of triocanoin and egg yolk phosphatidylcholine, respectively. SDS-PAGE and zymography analysis estimated the molecular weight of FAL to be 33 kDa. FAL was shown to be a PLA1 with a regioselectivity to the sn-1 position of surface-coated phospholipids esterified with α-eleostearic acid. FAL is a serine enzyme since its activity on triglycerides and phospholipids was completely inhibited by the lipase inhibitor Orlistat (40 μM). Interestingly, compared to Fusarium graminearum lipase (GZEL) and the Thermomyces lanuginosus lipase (Lipolase®), this novel fungal (phospho)lipase showed extreme tolerance to the presence of non-polar organic solvents, non-ionic and anionic surfactants, and oxidants, in addition to significant compatibility and stability with some available laundry detergents. The analysis of washing performance showed that it has the capability to efficiently eliminate oil-stains. Overall, FAL could be an ideal choice for application in detergents.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0286091</identifier><identifier>PMID: 37205651</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Ammonium ; Ammonium sulfate ; Analysis ; Ascomycota ; Biochemistry ; Biochemistry, Molecular Biology ; Biology and Life Sciences ; Chemical properties ; Detergent industry ; Detergents ; Detergents - chemistry ; Detergents - pharmacology ; Detergents, Synthetic ; Dieback ; Diseases and pests ; Eleostearic acid ; Emulsions ; Enzyme Stability ; Enzymes ; Esterification ; Ethylenediaminetetraacetic acid ; Fruit trees ; Fungi ; Fungi, Phytopathogenic ; Fusarium annulatum ; Fusarium graminearum ; Gel filtration ; Hydrogen-Ion Concentration ; Laundry ; Lecithin ; Life Sciences ; Lipase ; Lipase - metabolism ; Lipids ; Lipolase ; Medicine and Health Sciences ; Microbial enzymes ; Microbiology and Parasitology ; Microorganisms ; Molecular weight ; Mycology ; Olea - metabolism ; Olive ; Organic solvents ; Oxidants ; Oxidizing agents ; Pathogens ; Phosphatidylcholine ; Phospholipase A1 ; Phospholipids ; Physical Sciences ; Physiological aspects ; Regioselectivity ; Stability analysis ; Sulfates ; Surface active agents ; Surfactants ; Temperature ; Testing ; Trees ; Triglycerides ; Washing powders ; Yolk</subject><ispartof>PloS one, 2023-05, Vol.18 (5), p.e0286091-e0286091</ispartof><rights>Copyright: © 2023 Dab et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.</rights><rights>COPYRIGHT 2023 Public Library of Science</rights><rights>2023 Dab et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>2023 Dab et al 2023 Dab et al</rights><rights>2023 Dab et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c727t-7a33db79dcf6ab8846547ba30ae1d50ce1df40476c2aaf7f9a54836255a45db63</citedby><cites>FETCH-LOGICAL-c727t-7a33db79dcf6ab8846547ba30ae1d50ce1df40476c2aaf7f9a54836255a45db63</cites><orcidid>0000-0002-5182-7353 ; 0000-0003-0979-1614</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10198573/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10198573/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37205651$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04634467$$DView record in HAL$$Hfree_for_read</backlink></links><search><contributor>Nevárez-Moorillón, Guadalupe Virginia</contributor><creatorcontrib>Dab, Ahlem</creatorcontrib><creatorcontrib>Hasnaoui, Ismail</creatorcontrib><creatorcontrib>Mechri, Sondes</creatorcontrib><creatorcontrib>Allala, Fawzi</creatorcontrib><creatorcontrib>Bouacem, Khelifa</creatorcontrib><creatorcontrib>Noiriel, Alexandre</creatorcontrib><creatorcontrib>Bouanane-Darenfed, Amel</creatorcontrib><creatorcontrib>Saalaoui, Ennouamane</creatorcontrib><creatorcontrib>Asehraou, Abdeslam</creatorcontrib><creatorcontrib>Wang, Fanghua</creatorcontrib><creatorcontrib>Abousalham, Abdelkarim</creatorcontrib><creatorcontrib>Jaouadi, Bassem</creatorcontrib><title>Biochemical characterization of an alkaline and detergent-stable Lipase from Fusarium annulatum Bugnicourt strain CBS associated with olive tree dieback</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>This work describes a novel extracellular lipolytic carboxylester hydrolase named FAL, with lipase and phospholipase A1 (PLA1) activity, from a newly isolated filamentous fungus Ascomycota CBS strain, identified as Fusarium annulatum Bunigcourt. FAL was purified to about 62-fold using ammonium sulphate precipitation, Superdex® 200 Increase gel filtration and Q-Sepharose Fast Flow columns, with a total yield of 21%. The specific activity of FAL was found to be 3500 U/mg at pH 9 and 40°C and 5000 U/mg at pH 11 and 45°C, on emulsions of triocanoin and egg yolk phosphatidylcholine, respectively. SDS-PAGE and zymography analysis estimated the molecular weight of FAL to be 33 kDa. FAL was shown to be a PLA1 with a regioselectivity to the sn-1 position of surface-coated phospholipids esterified with α-eleostearic acid. FAL is a serine enzyme since its activity on triglycerides and phospholipids was completely inhibited by the lipase inhibitor Orlistat (40 μM). Interestingly, compared to Fusarium graminearum lipase (GZEL) and the Thermomyces lanuginosus lipase (Lipolase®), this novel fungal (phospho)lipase showed extreme tolerance to the presence of non-polar organic solvents, non-ionic and anionic surfactants, and oxidants, in addition to significant compatibility and stability with some available laundry detergents. The analysis of washing performance showed that it has the capability to efficiently eliminate oil-stains. Overall, FAL could be an ideal choice for application in detergents.</description><subject>Ammonium</subject><subject>Ammonium sulfate</subject><subject>Analysis</subject><subject>Ascomycota</subject><subject>Biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biology and Life Sciences</subject><subject>Chemical properties</subject><subject>Detergent industry</subject><subject>Detergents</subject><subject>Detergents - chemistry</subject><subject>Detergents - pharmacology</subject><subject>Detergents, Synthetic</subject><subject>Dieback</subject><subject>Diseases and pests</subject><subject>Eleostearic acid</subject><subject>Emulsions</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Esterification</subject><subject>Ethylenediaminetetraacetic acid</subject><subject>Fruit trees</subject><subject>Fungi</subject><subject>Fungi, Phytopathogenic</subject><subject>Fusarium annulatum</subject><subject>Fusarium graminearum</subject><subject>Gel filtration</subject><subject>Hydrogen-Ion Concentration</subject><subject>Laundry</subject><subject>Lecithin</subject><subject>Life Sciences</subject><subject>Lipase</subject><subject>Lipase - metabolism</subject><subject>Lipids</subject><subject>Lipolase</subject><subject>Medicine and Health Sciences</subject><subject>Microbial enzymes</subject><subject>Microbiology and Parasitology</subject><subject>Microorganisms</subject><subject>Molecular weight</subject><subject>Mycology</subject><subject>Olea - metabolism</subject><subject>Olive</subject><subject>Organic solvents</subject><subject>Oxidants</subject><subject>Oxidizing agents</subject><subject>Pathogens</subject><subject>Phosphatidylcholine</subject><subject>Phospholipase A1</subject><subject>Phospholipids</subject><subject>Physical Sciences</subject><subject>Physiological aspects</subject><subject>Regioselectivity</subject><subject>Stability analysis</subject><subject>Sulfates</subject><subject>Surface active agents</subject><subject>Surfactants</subject><subject>Temperature</subject><subject>Testing</subject><subject>Trees</subject><subject>Triglycerides</subject><subject>Washing powders</subject><subject>Yolk</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk99v0zAQxyMEYmPwHyCwhITYQ0scO3byhLaKsUqVJjHg1brYTuPNjTvbGT_-Ev5cnLWb1mkPKJJ9On_u6_PlLste43yKCccfL9zge7DTtev1NC8qltf4SbaPa1JMWJGTp_fsvexFCBd5XpKKsefZHuFFXrIS72d_j42TnV4ZCRbJDjzIqL35A9G4HrkWQY_AXoI1vU62Qkqn86Xu4yREaKxGC7OGoFHr3QqdDAG8GVaJ7AcLMVnHw7I3MuUaUYgeTI9mx-cIQnDSQNQK_TSxQ86aa42i1xopoxuQly-zZy3YoF9t94Ps-8nnb7PTyeLsy3x2tJhIXvA44UCIanitZMugqSrKSsobIDlorMpcprWlOeVMFgAtb2soaUVYUZZAS9UwcpC93eiurQtiW9QgigqXNUl1LhMx3xDKwYVYe7MC_1s4MOLG4fxSgI9GWi1YyysmcUObBqgC2XBSVw3RVHEpGaVJ69P2tqFZaSVTHT3YHdHdk950YumuBc5xXZWcJIXDjUL3IO70aCFGX04ZoZTxa5zYD9vbvLsadIhiZYLU1kKv3XDzSMYZTVtC3z1AHy_FllpCeq3pW5eSlKOoOOJ0TDB1VaKmj1DpU2OfpXZtTfLvBBzuBCQm6l9xCUMIYn7-9f_Zsx-77Pt7bKfBxi44O4y9HXZBugGldyF43d5VFudinLbbaohx2sR22lLYm_t_8y7odrzIP4ZkJ0c</recordid><startdate>20230519</startdate><enddate>20230519</enddate><creator>Dab, Ahlem</creator><creator>Hasnaoui, Ismail</creator><creator>Mechri, Sondes</creator><creator>Allala, Fawzi</creator><creator>Bouacem, Khelifa</creator><creator>Noiriel, Alexandre</creator><creator>Bouanane-Darenfed, Amel</creator><creator>Saalaoui, Ennouamane</creator><creator>Asehraou, Abdeslam</creator><creator>Wang, Fanghua</creator><creator>Abousalham, Abdelkarim</creator><creator>Jaouadi, Bassem</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-5182-7353</orcidid><orcidid>https://orcid.org/0000-0003-0979-1614</orcidid></search><sort><creationdate>20230519</creationdate><title>Biochemical characterization of an alkaline and detergent-stable Lipase from Fusarium annulatum Bugnicourt strain CBS associated with olive tree dieback</title><author>Dab, Ahlem ; Hasnaoui, Ismail ; Mechri, Sondes ; Allala, Fawzi ; Bouacem, Khelifa ; Noiriel, Alexandre ; Bouanane-Darenfed, Amel ; Saalaoui, Ennouamane ; Asehraou, Abdeslam ; Wang, Fanghua ; Abousalham, Abdelkarim ; Jaouadi, Bassem</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c727t-7a33db79dcf6ab8846547ba30ae1d50ce1df40476c2aaf7f9a54836255a45db63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Ammonium</topic><topic>Ammonium sulfate</topic><topic>Analysis</topic><topic>Ascomycota</topic><topic>Biochemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biology and Life Sciences</topic><topic>Chemical properties</topic><topic>Detergent industry</topic><topic>Detergents</topic><topic>Detergents - chemistry</topic><topic>Detergents - pharmacology</topic><topic>Detergents, Synthetic</topic><topic>Dieback</topic><topic>Diseases and pests</topic><topic>Eleostearic acid</topic><topic>Emulsions</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Esterification</topic><topic>Ethylenediaminetetraacetic acid</topic><topic>Fruit trees</topic><topic>Fungi</topic><topic>Fungi, Phytopathogenic</topic><topic>Fusarium annulatum</topic><topic>Fusarium graminearum</topic><topic>Gel filtration</topic><topic>Hydrogen-Ion Concentration</topic><topic>Laundry</topic><topic>Lecithin</topic><topic>Life Sciences</topic><topic>Lipase</topic><topic>Lipase - metabolism</topic><topic>Lipids</topic><topic>Lipolase</topic><topic>Medicine and Health Sciences</topic><topic>Microbial enzymes</topic><topic>Microbiology and Parasitology</topic><topic>Microorganisms</topic><topic>Molecular weight</topic><topic>Mycology</topic><topic>Olea - metabolism</topic><topic>Olive</topic><topic>Organic solvents</topic><topic>Oxidants</topic><topic>Oxidizing agents</topic><topic>Pathogens</topic><topic>Phosphatidylcholine</topic><topic>Phospholipase A1</topic><topic>Phospholipids</topic><topic>Physical Sciences</topic><topic>Physiological aspects</topic><topic>Regioselectivity</topic><topic>Stability analysis</topic><topic>Sulfates</topic><topic>Surface active agents</topic><topic>Surfactants</topic><topic>Temperature</topic><topic>Testing</topic><topic>Trees</topic><topic>Triglycerides</topic><topic>Washing powders</topic><topic>Yolk</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dab, Ahlem</creatorcontrib><creatorcontrib>Hasnaoui, Ismail</creatorcontrib><creatorcontrib>Mechri, Sondes</creatorcontrib><creatorcontrib>Allala, Fawzi</creatorcontrib><creatorcontrib>Bouacem, Khelifa</creatorcontrib><creatorcontrib>Noiriel, Alexandre</creatorcontrib><creatorcontrib>Bouanane-Darenfed, Amel</creatorcontrib><creatorcontrib>Saalaoui, Ennouamane</creatorcontrib><creatorcontrib>Asehraou, Abdeslam</creatorcontrib><creatorcontrib>Wang, Fanghua</creatorcontrib><creatorcontrib>Abousalham, Abdelkarim</creatorcontrib><creatorcontrib>Jaouadi, Bassem</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Proquest Nursing & Allied Health Source</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dab, Ahlem</au><au>Hasnaoui, Ismail</au><au>Mechri, Sondes</au><au>Allala, Fawzi</au><au>Bouacem, Khelifa</au><au>Noiriel, Alexandre</au><au>Bouanane-Darenfed, Amel</au><au>Saalaoui, Ennouamane</au><au>Asehraou, Abdeslam</au><au>Wang, Fanghua</au><au>Abousalham, Abdelkarim</au><au>Jaouadi, Bassem</au><au>Nevárez-Moorillón, Guadalupe Virginia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical characterization of an alkaline and detergent-stable Lipase from Fusarium annulatum Bugnicourt strain CBS associated with olive tree dieback</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2023-05-19</date><risdate>2023</risdate><volume>18</volume><issue>5</issue><spage>e0286091</spage><epage>e0286091</epage><pages>e0286091-e0286091</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>This work describes a novel extracellular lipolytic carboxylester hydrolase named FAL, with lipase and phospholipase A1 (PLA1) activity, from a newly isolated filamentous fungus Ascomycota CBS strain, identified as Fusarium annulatum Bunigcourt. FAL was purified to about 62-fold using ammonium sulphate precipitation, Superdex® 200 Increase gel filtration and Q-Sepharose Fast Flow columns, with a total yield of 21%. The specific activity of FAL was found to be 3500 U/mg at pH 9 and 40°C and 5000 U/mg at pH 11 and 45°C, on emulsions of triocanoin and egg yolk phosphatidylcholine, respectively. SDS-PAGE and zymography analysis estimated the molecular weight of FAL to be 33 kDa. FAL was shown to be a PLA1 with a regioselectivity to the sn-1 position of surface-coated phospholipids esterified with α-eleostearic acid. FAL is a serine enzyme since its activity on triglycerides and phospholipids was completely inhibited by the lipase inhibitor Orlistat (40 μM). Interestingly, compared to Fusarium graminearum lipase (GZEL) and the Thermomyces lanuginosus lipase (Lipolase®), this novel fungal (phospho)lipase showed extreme tolerance to the presence of non-polar organic solvents, non-ionic and anionic surfactants, and oxidants, in addition to significant compatibility and stability with some available laundry detergents. The analysis of washing performance showed that it has the capability to efficiently eliminate oil-stains. Overall, FAL could be an ideal choice for application in detergents.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>37205651</pmid><doi>10.1371/journal.pone.0286091</doi><tpages>e0286091</tpages><orcidid>https://orcid.org/0000-0002-5182-7353</orcidid><orcidid>https://orcid.org/0000-0003-0979-1614</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2023-05, Vol.18 (5), p.e0286091-e0286091 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_2815933715 |
| source | PubMed Central Free; MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Ammonium Ammonium sulfate Analysis Ascomycota Biochemistry Biochemistry, Molecular Biology Biology and Life Sciences Chemical properties Detergent industry Detergents Detergents - chemistry Detergents - pharmacology Detergents, Synthetic Dieback Diseases and pests Eleostearic acid Emulsions Enzyme Stability Enzymes Esterification Ethylenediaminetetraacetic acid Fruit trees Fungi Fungi, Phytopathogenic Fusarium annulatum Fusarium graminearum Gel filtration Hydrogen-Ion Concentration Laundry Lecithin Life Sciences Lipase Lipase - metabolism Lipids Lipolase Medicine and Health Sciences Microbial enzymes Microbiology and Parasitology Microorganisms Molecular weight Mycology Olea - metabolism Olive Organic solvents Oxidants Oxidizing agents Pathogens Phosphatidylcholine Phospholipase A1 Phospholipids Physical Sciences Physiological aspects Regioselectivity Stability analysis Sulfates Surface active agents Surfactants Temperature Testing Trees Triglycerides Washing powders Yolk |
| title | Biochemical characterization of an alkaline and detergent-stable Lipase from Fusarium annulatum Bugnicourt strain CBS associated with olive tree dieback |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T03%3A54%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Biochemical%20characterization%20of%20an%20alkaline%20and%20detergent-stable%20Lipase%20from%20Fusarium%20annulatum%20Bugnicourt%20strain%20CBS%20associated%20with%20olive%20tree%20dieback&rft.jtitle=PloS%20one&rft.au=Dab,%20Ahlem&rft.date=2023-05-19&rft.volume=18&rft.issue=5&rft.spage=e0286091&rft.epage=e0286091&rft.pages=e0286091-e0286091&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0286091&rft_dat=%3Cgale_plos_%3EA749857565%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2815933715&rft_id=info:pmid/37205651&rft_galeid=A749857565&rft_doaj_id=oai_doaj_org_article_6f786c1b4bba4dacb7398b3e4d7cc644&rfr_iscdi=true |