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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Autores principales: Florence Privé, Naheed N Kaderbhai, Susan Girdwood, Hilary J Worgan, Eric Pinloche, Nigel D Scollan, Sharon A Huws, C Jamie Newbold
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Publicado: Public Library of Science (PLoS) 2013
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spelling oai:doaj.org-article:6d67226e0eed4e4ab2f3345cbe82e8542021-11-18T09:00:20ZIdentification and characterization of three novel lipases belonging to families II and V from Anaerovibrio lipolyticus 5ST.1932-620310.1371/journal.pone.0069076https://doaj.org/article/6d67226e0eed4e4ab2f3345cbe82e8542013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23950883/?tool=EBIhttps://doaj.org/toc/1932-6203Following 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).Florence PrivéNaheed N KaderbhaiSusan GirdwoodHilary J WorganEric PinlocheNigel D ScollanSharon A HuwsC Jamie NewboldPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e69076 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
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.
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).
format article
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
title 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_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_sort identification and characterization of three novel lipases belonging to families ii and v from anaerovibrio lipolyticus 5st.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/6d67226e0eed4e4ab2f3345cbe82e854
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