Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST
Following the isolation, cultivation and characterization of the rumen bacterium Anaerovibrio lipolyticus in the 1960s, it has been recognized as one of the major species involved in lipid hydrolysis in ruminant animals. However, there has been limited characterization of the lipases from the bacter...
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| creator | Privé, Florence Kaderbhai, Naheed N Girdwood, Susan Worgan, Hilary J Pinloche, Eric Scollan, Nigel D Huws, Sharon A Newbold, C Jamie |
| description | Following the isolation, cultivation and characterization of the rumen bacterium Anaerovibrio lipolyticus in the 1960s, it has been recognized as one of the major species involved in lipid hydrolysis in ruminant animals. However, there has been limited characterization of the lipases from the bacterium, despite the importance of understanding lipolysis and its impact on subsequent biohydrogenation of polyunsaturated fatty acids by rumen microbes. This study describes the draft genome of Anaerovibrio lipolytica 5ST, and the characterization of three lipolytic genes and their translated protein. The uncompleted draft genome was 2.83 Mbp and comprised of 2,673 coding sequences with a G+C content of 43.3%. Three putative lipase genes, alipA, alipB and alipC, encoding 492-, 438- and 248- amino acid peptides respectively, were identified using RAST. Phylogenetic analysis indicated that alipA and alipB clustered with the GDSL/SGNH family II, and alipC clustered with lipolytic enzymes from family V. Subsequent expression and purification of the enzymes showed that they were thermally unstable and had higher activities at neutral to alkaline pH. Substrate specificity assays indicated that the enzymes had higher hydrolytic activity against caprylate (C8), laurate (C12) and myristate (C14). |
| doi_str_mv | 10.1371/journal.pone.0069076 |
| format | Article |
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However, there has been limited characterization of the lipases from the bacterium, despite the importance of understanding lipolysis and its impact on subsequent biohydrogenation of polyunsaturated fatty acids by rumen microbes. This study describes the draft genome of Anaerovibrio lipolytica 5ST, and the characterization of three lipolytic genes and their translated protein. The uncompleted draft genome was 2.83 Mbp and comprised of 2,673 coding sequences with a G+C content of 43.3%. Three putative lipase genes, alipA, alipB and alipC, encoding 492-, 438- and 248- amino acid peptides respectively, were identified using RAST. Phylogenetic analysis indicated that alipA and alipB clustered with the GDSL/SGNH family II, and alipC clustered with lipolytic enzymes from family V. Subsequent expression and purification of the enzymes showed that they were thermally unstable and had higher activities at neutral to alkaline pH. Substrate specificity assays indicated that the enzymes had higher hydrolytic activity against caprylate (C8), laurate (C12) and myristate (C14).</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0069076</identifier><identifier>PMID: 23950883</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acetobacter pasteurianus ; Agriculture ; Amino Acid Motifs ; Amino Acid Sequence ; Amino acids ; Anaerovibrio lipolytica ; Anaerovibrio lipolyticus ; Animals ; Bacteria ; Biology ; Cladistic analysis ; Cloning ; Conserved Sequence ; Cultivation ; Deoxyribonucleic acid ; DNA ; Enzyme Activation ; Enzymes ; Fatty acids ; Gene Expression ; Gene sequencing ; Genes ; Genetic aspects ; Genomes ; Genomics ; Glycerol ; Hydrogen-Ion Concentration ; Hydrolysis ; Identification ; Life sciences ; Lipase ; Lipase - chemistry ; Lipase - genetics ; Lipase - isolation & purification ; Lipase - metabolism ; Lipids ; Lipolysis ; Metabolism ; Molecular Sequence Data ; Peptides ; pH effects ; Phylogeny ; Polyunsaturated fatty acids ; Proteins ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Rumen ; Sequence Alignment ; Studies ; Substrate Specificity ; Substrates ; Temperature ; Triglycerides ; Unsaturated fatty acids ; Veillonellaceae - classification ; Veillonellaceae - enzymology ; Veillonellaceae - genetics</subject><ispartof>PloS one, 2013-08, Vol.8 (8), p.e69076-e69076</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Privé et al. 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However, there has been limited characterization of the lipases from the bacterium, despite the importance of understanding lipolysis and its impact on subsequent biohydrogenation of polyunsaturated fatty acids by rumen microbes. This study describes the draft genome of Anaerovibrio lipolytica 5ST, and the characterization of three lipolytic genes and their translated protein. The uncompleted draft genome was 2.83 Mbp and comprised of 2,673 coding sequences with a G+C content of 43.3%. Three putative lipase genes, alipA, alipB and alipC, encoding 492-, 438- and 248- amino acid peptides respectively, were identified using RAST. Phylogenetic analysis indicated that alipA and alipB clustered with the GDSL/SGNH family II, and alipC clustered with lipolytic enzymes from family V. Subsequent expression and purification of the enzymes showed that they were thermally unstable and had higher activities at neutral to alkaline pH. Substrate specificity assays indicated that the enzymes had higher hydrolytic activity against caprylate (C8), laurate (C12) and myristate (C14).</description><subject>Acetobacter pasteurianus</subject><subject>Agriculture</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Anaerovibrio lipolytica</subject><subject>Anaerovibrio lipolyticus</subject><subject>Animals</subject><subject>Bacteria</subject><subject>Biology</subject><subject>Cladistic analysis</subject><subject>Cloning</subject><subject>Conserved Sequence</subject><subject>Cultivation</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Enzyme Activation</subject><subject>Enzymes</subject><subject>Fatty acids</subject><subject>Gene Expression</subject><subject>Gene sequencing</subject><subject>Genes</subject><subject>Genetic aspects</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Glycerol</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysis</subject><subject>Identification</subject><subject>Life sciences</subject><subject>Lipase</subject><subject>Lipase - chemistry</subject><subject>Lipase - genetics</subject><subject>Lipase - isolation & purification</subject><subject>Lipase - metabolism</subject><subject>Lipids</subject><subject>Lipolysis</subject><subject>Metabolism</subject><subject>Molecular Sequence Data</subject><subject>Peptides</subject><subject>pH effects</subject><subject>Phylogeny</subject><subject>Polyunsaturated fatty acids</subject><subject>Proteins</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Rumen</subject><subject>Sequence Alignment</subject><subject>Studies</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Temperature</subject><subject>Triglycerides</subject><subject>Unsaturated fatty acids</subject><subject>Veillonellaceae - classification</subject><subject>Veillonellaceae - enzymology</subject><subject>Veillonellaceae - 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and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST</title><author>Privé, Florence ; Kaderbhai, Naheed N ; Girdwood, Susan ; Worgan, Hilary J ; Pinloche, Eric ; Scollan, Nigel D ; Huws, Sharon A ; Newbold, C Jamie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-224683a20f36720ef066088cfc303833b0b841749feb71213e8288e71b9a34e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Acetobacter pasteurianus</topic><topic>Agriculture</topic><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Anaerovibrio lipolytica</topic><topic>Anaerovibrio lipolyticus</topic><topic>Animals</topic><topic>Bacteria</topic><topic>Biology</topic><topic>Cladistic analysis</topic><topic>Cloning</topic><topic>Conserved Sequence</topic><topic>Cultivation</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Enzyme Activation</topic><topic>Enzymes</topic><topic>Fatty acids</topic><topic>Gene Expression</topic><topic>Gene sequencing</topic><topic>Genes</topic><topic>Genetic aspects</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Glycerol</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolysis</topic><topic>Identification</topic><topic>Life sciences</topic><topic>Lipase</topic><topic>Lipase - chemistry</topic><topic>Lipase - genetics</topic><topic>Lipase - isolation & purification</topic><topic>Lipase - metabolism</topic><topic>Lipids</topic><topic>Lipolysis</topic><topic>Metabolism</topic><topic>Molecular Sequence Data</topic><topic>Peptides</topic><topic>pH effects</topic><topic>Phylogeny</topic><topic>Polyunsaturated fatty acids</topic><topic>Proteins</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - 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However, there has been limited characterization of the lipases from the bacterium, despite the importance of understanding lipolysis and its impact on subsequent biohydrogenation of polyunsaturated fatty acids by rumen microbes. This study describes the draft genome of Anaerovibrio lipolytica 5ST, and the characterization of three lipolytic genes and their translated protein. The uncompleted draft genome was 2.83 Mbp and comprised of 2,673 coding sequences with a G+C content of 43.3%. Three putative lipase genes, alipA, alipB and alipC, encoding 492-, 438- and 248- amino acid peptides respectively, were identified using RAST. Phylogenetic analysis indicated that alipA and alipB clustered with the GDSL/SGNH family II, and alipC clustered with lipolytic enzymes from family V. Subsequent expression and purification of the enzymes showed that they were thermally unstable and had higher activities at neutral to alkaline pH. Substrate specificity assays indicated that the enzymes had higher hydrolytic activity against caprylate (C8), laurate (C12) and myristate (C14).</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23950883</pmid><doi>10.1371/journal.pone.0069076</doi><tpages>e69076</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2013-08, Vol.8 (8), p.e69076-e69076 |
| issn | 1932-6203 1932-6203 |
| language | eng |
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| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Acetobacter pasteurianus Agriculture Amino Acid Motifs Amino Acid Sequence Amino acids Anaerovibrio lipolytica Anaerovibrio lipolyticus Animals Bacteria Biology Cladistic analysis Cloning Conserved Sequence Cultivation Deoxyribonucleic acid DNA Enzyme Activation Enzymes Fatty acids Gene Expression Gene sequencing Genes Genetic aspects Genomes Genomics Glycerol Hydrogen-Ion Concentration Hydrolysis Identification Life sciences Lipase Lipase - chemistry Lipase - genetics Lipase - isolation & purification Lipase - metabolism Lipids Lipolysis Metabolism Molecular Sequence Data Peptides pH effects Phylogeny Polyunsaturated fatty acids Proteins Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Rumen Sequence Alignment Studies Substrate Specificity Substrates Temperature Triglycerides Unsaturated fatty acids Veillonellaceae - classification Veillonellaceae - enzymology Veillonellaceae - genetics |
| title | Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T20%3A31%3A24IST&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=Identification%20and%20characterization%20of%20three%20novel%20lipases%20belonging%20to%20families%20II%20and%20V%20from%20Anaerovibrio%20lipolyticus%205ST&rft.jtitle=PloS%20one&rft.au=Priv%C3%A9,%20Florence&rft.date=2013-08-12&rft.volume=8&rft.issue=8&rft.spage=e69076&rft.epage=e69076&rft.pages=e69076-e69076&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0069076&rft_dat=%3Cgale_plos_%3EA478311012%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=1430420687&rft_id=info:pmid/23950883&rft_galeid=A478311012&rft_doaj_id=oai_doaj_org_article_6d67226e0eed4e4ab2f3345cbe82e854&rfr_iscdi=true |