1. Isolation and analysis of a gene from the marine microalga Isochrysis galbana that encodes a lipase-like protein
- Author
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Stéphanie Godet, Françoise Ergan, Josiane Hérault, Gaëlle Pencreac'h, Céline Loiseau, Institut de Recherche en Horticulture et Semences (IRHS), AGROCAMPUS OUEST-Institut National de la Recherche Agronomique (INRA)-Université d'Angers (UA), Université d'Angers (UA)-Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Laval Agglomeration, Conseil General de la Mayenne, AGROCAMPUS OUEST, and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut National de la Recherche Agronomique (INRA)-Université d'Angers (UA)
- Subjects
0106 biological sciences ,Plant Science ,Aquatic Science ,01 natural sciences ,Pentapeptide repeat ,rhizomucor-miehei lipase ,Isochrysis galbana ,03 medical and health sciences ,esters ,010608 biotechnology ,Complementary DNA ,Catalytic triad ,Microalgae ,Lipase ,MARINE & FRESHWATER BIOLOGY ,[SDV.SA.HORT]Life Sciences [q-bio]/Agricultural sciences/Horticulture ,Gene ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,biology ,dynamics ,biology.organism_classification ,Amino acid ,Open reading frame ,chemistry ,Biochemistry ,hydrolysis ,biology.protein ,Alpha/beta hydrolases - Abstract
Microalgae constitute a novel study area for characterising new lipolytic enzymes of biotechnological interest. A new gene from the microalga Isochrysis galbana has been isolated and a preliminary characterisation performed. The full-length cDNA contains 2,060 base pairs with an open reading frame of 1,374 nucleotides encoding a polypeptide of 457 amino acids with a predicted molecular mass of 49 kDa, and a theoretical pI of 5.65. The deduced protein includes highly conserved motifs found in alpha/beta fold hydrolases, and shares some similarities with putative or known lipases. Sequence comparison indicated that the catalytic triad corresponds to residues Ser(188), Asp(306) and His(391), with the nucleophilic residue Ser(188) positioned within the consensus G-X-S-188-X-G pentapeptide. Phylogenetic analyses established close relationships with fungal lipases and microalgal sequences.
- Published
- 2012
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