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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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23950883/?tool=EBI |
| _version_ | 1818459691372511232 |
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| author | Florence Privé Naheed N Kaderbhai Susan Girdwood Hilary J Worgan Eric Pinloche Nigel D Scollan Sharon A Huws C Jamie Newbold |
| author_facet | Florence Privé Naheed N Kaderbhai Susan Girdwood Hilary J Worgan Eric Pinloche Nigel D Scollan Sharon A Huws C Jamie Newbold |
| author_sort | Florence Privé |
| collection | DOAJ |
| 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). |
| first_indexed | 2024-12-14T23:18:23Z |
| format | Article |
| id | doaj.art-6d67226e0eed4e4ab2f3345cbe82e854 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-14T23:18:23Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-6d67226e0eed4e4ab2f3345cbe82e8542022-12-21T22:44:01ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0188e6907610.1371/journal.pone.0069076Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST.Florence PrivéNaheed N KaderbhaiSusan GirdwoodHilary J WorganEric PinlocheNigel D ScollanSharon A HuwsC Jamie NewboldFollowing 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).https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23950883/?tool=EBI |
| spellingShingle | Florence Privé Naheed N Kaderbhai Susan Girdwood Hilary J Worgan Eric Pinloche Nigel D Scollan Sharon A Huws C Jamie Newbold Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST. PLoS ONE |
| title | Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST. |
| title_full | Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST. |
| title_fullStr | Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST. |
| title_full_unstemmed | Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST. |
| title_short | Identification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST. |
| title_sort | identification and characterization of three novel lipases belonging to families ii and v from anaerovibrio lipolyticus 5st |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23950883/?tool=EBI |
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