Isolation and analysis of a gene from the marine microalga Isochrysis galbana that encodes a lipase-like protein

Godet, Stéphanie; Hérault, Jósiane; Pencreach, Gaëlle; Ergan, F.; Loiseau, Céline

doi:10.1007/s10811-012-9815-3

Cited by 14 publications

(3 citation statements)

References 19 publications

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“…The presence of lipase activity has already been reported in Dunaliella salina (Cho and Thompson, 1986), Phaeodactylum tricornutum (Barka et al, 2016) and Spirulina platensis (Demir and Tükel, 2010). In Isochrysis galbana, Godet et al (2010Godet et al ( , 2012 and Kerviel et al (2014) isolated and characterized genes encoding for carboxylesterase and/or lipase-like enzymes for potential use in metabolic engineering to enhance lipid yields in microalgae.…”

Section: Nannochloropsis T-isochrysismentioning

confidence: 82%

Lipolysis in T-Isochrysis lutea during wet storage at different temperatures

et al. 2016

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Previously, it has been observed that lipolysis occurring during (even short term) wet storage of microalgal biomass causes high free fatty acid (FFA) concentrations in the biomass. These FFA have a negative impact for different applications of microalgal lipids, e.g. downstream processing problems in biodiesel production, off-flavors and loss of nutritional value for food applications. However, it is not clear which factors influence lipolysis in microalgal biomass and which lipid class are more susceptible to lipolysis. In this study, wet biomass of T-Isochrysis lutea was stored at 20°C, 4°C and -20°C during 3 weeks. The extent of lipolysis was followed by analyzing the lipid classes distribution by ultrahigh-performance liquid chromatography−accurate mass mass spectrometry (UHPLC-amMS) and the FFA content. It was observed that FFA were formed very rapidly during post-harvest storage of wet biomass at 20°C and 4°C, the rate of this process being faster at 20°C than at 4°C, while almost no lipolysis was observed at -20°C.However, the FFA content levelled off after several days of storage because FFA reacted with alcohols to form fatty acyl esters.

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Section: Nannochloropsis T-isochrysismentioning

confidence: 82%

Lipolysis in T-Isochrysis lutea during wet storage at different temperatures

et al. 2016

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“…The nucleotide sequences of the 3’- and 5’-ends of HaeCYP97A/B/C were amplified by the RACE method [112,113]. Gene-specific primers were designed from the amplified core cDNA sequence of HaeCYP97A/B/C and their 3’- and 5’-ends were obtained using SMARTTM RACE cDNA Amplification Kit (Clontech) according to the manual.…”

Section: Methodsmentioning

confidence: 99%

Evolutionary origins, molecular cloning and expression of carotenoid hydroxylases in eukaryotic photosynthetic algae

Cui

Wang

et al. 2013

BMC Genomics

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BackgroundXanthophylls, oxygenated derivatives of carotenes, play critical roles in photosynthetic apparatus of cyanobacteria, algae, and higher plants. Although the xanthophylls biosynthetic pathway of algae is largely unknown, it is of particular interest because they have a very complicated evolutionary history. Carotenoid hydroxylase (CHY) is an important protein that plays essential roles in xanthophylls biosynthesis. With the availability of 18 sequenced algal genomes, we performed a comprehensive comparative analysis of chy genes and explored their distribution, structure, evolution, origins, and expression.ResultsOverall 60 putative chy genes were identified and classified into two major subfamilies (bch and cyp97) according to their domain structures. Genes in the bch subfamily were found in 10 green algae and 1 red alga, but absent in other algae. In the phylogenetic tree, bch genes of green algae and higher plants share a common ancestor and are of non-cyanobacterial origin, whereas that of red algae is of cyanobacteria. The homologs of cyp97a/c genes were widespread only in green algae, while cyp97b paralogs were seen in most of algae. Phylogenetic analysis on cyp97 genes supported the hypothesis that cyp97b is an ancient gene originated before the formation of extant algal groups. The cyp97a gene is more closely related to cyp97c in evolution than to cyp97b. The two cyp97 genes were isolated from the green alga Haematococcus pluvialis, and transcriptional expression profiles of chy genes were observed under high light stress of different wavelength.ConclusionsGreen algae received a β-xanthophylls biosynthetic pathway from host organisms. Although red algae inherited the pathway from cyanobacteria during primary endosymbiosis, it remains unclear in Chromalveolates. The α-xanthophylls biosynthetic pathway is a common feature in green algae and higher plants. The origination of cyp97a/c is most likely due to gene duplication before divergence of green algae and higher plants. Protein domain structures and expression analyses in green alga H. pluvialis indicate that various chy genes are in different manners response to light. The knowledge of evolution of chy genes in photosynthetic eukaryotes provided information of gene cloning and functional investigation of chy genes in algae in the future.

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“…It was specific for the 3-position in the ester bond. Godet et al [ 10 ] isolated a new gene from the microalgae Isochrysis galbana encoding a 49 kDa lipase that shares similarities with fungal known lipase sequences. Chlorella vulgaris is a microalga belonging to the order of the Chlorococcales , which has a green color.…”

Section: Introductionmentioning

confidence: 99%

Molecular and Structural Characterizations of Lipases from Chlorella by Functional Genomics

et al. 2021

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Microalgae have been poorly investigated for new-lipolytic enzymes of biotechnological interest. In silico study combining analysis of sequences homologies and bioinformatic tools allowed the identification and preliminary characterization of 14 putative lipases expressed by Chlorella vulagaris. These proteins have different molecular weights, subcellular localizations, low instability index range and at least 40% of sequence identity with other microalgal lipases. Sequence comparison indicated that the catalytic triad corresponded to residues Ser, Asp and His, with the nucleophilic residue Ser positioned within the consensus GXSXG pentapeptide. 3D models were generated using different approaches and templates and demonstrated that these putative enzymes share a similar core with common α/β hydrolases fold belonging to family 3 lipases and class GX. Six lipases were predicted to have a transmembrane domain and a lysosomal acid lipase was identified. A similar mammalian enzyme plays an important role in breaking down cholesteryl esters and triglycerides and its deficiency causes serious digestive problems in human. More structural insight would provide important information on the enzyme characteristics.

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Isolation and analysis of a gene from the marine microalga Isochrysis galbana that encodes a lipase-like protein

Cited by 14 publications

References 19 publications

Lipolysis in T-Isochrysis lutea during wet storage at different temperatures

Lipolysis in T-Isochrysis lutea during wet storage at different temperatures

Evolutionary origins, molecular cloning and expression of carotenoid hydroxylases in eukaryotic photosynthetic algae

Molecular and Structural Characterizations of Lipases from Chlorella by Functional Genomics

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