Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach

Tutuncu, Havva Esra; Balcı, Nurgül; Tüter, Melek; Karagüler, Nevin Gül

doi:10.1007/s00792-019-01103-w

Cited by 13 publications

(9 citation statements)

References 60 publications

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“…Especially, in the presence of 20% formaldehyde and ethanol, the residual enzyme activity was only 1.1-1.5%. In contrast, DMSO had little effect on the activity of Est19, as observed for other esterases [6,8]. Metal ions can have different effects on the activity of esterases.…”

Section: Discussionmentioning

confidence: 77%

“…Lipolytic enzymes are widely distributed in nature (i.e., animals, plants, and microorganisms), and a relatively large number has been isolated from metagenomes and bacteria [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 ]. The latter includes enzymes with different biological activities isolated from genera such as Pseudomonas [ 1 ], Psychrobacter [ 5 ], Salinisphaera [ 9 ], Serratia [ 11 ], Burkholderia [ 12 ], and Staphylococcus [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

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Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

et al. 2021

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Esterases represent an important class of enzymes with a wide variety of industrial applications. A novel hormone-sensitive lipase (HSL) family esterase, Est19, from the Antarctic bacterium Pseudomonas sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG motif containing an active serine (S) located within a highly conserved catalytic triad of Ser155, Asp253, and His282 residues. The catalytic efficiency (kcat/Km) of Est19 for the pNPC6 substrate is 148.68 s−1mM−1 at 40 °C. Replacing Glu154 juxtaposed to the critical catalytic serine with Asp (E154→D substitution) reduced the activity and catalytic efficiency of the enzyme two-fold, with little change in the substrate affinity. The wild-type enzyme retained near complete activity over a temperature range of 10–60 °C, while ~50% of its activity was retained at 0 °C. A phylogenetic analysis suggested that Est19 and its homologs may represent a new subfamily of HSL. The thermal stability and stereo-specificity suggest that the Est19 esterase may be useful for cold and chiral catalyses.

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Section: Discussionmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 99%

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

et al. 2021

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“…Using simple homology-based comparison can help understand enzymes structure, properties and similarity to enzymes from other taxon's. As an example, Hypersaline lake "Acıgöl" esterase (hAGEst) and GH11 xylanase Xyn22 can be mentioned [113,114]. Both them were identified and purified based on functional metagenomics methods.…”

Section: In Silico Methods For Identification Of Novel Halophiles Bioproductsmentioning

confidence: 99%

“…It is characterised by high activity at low temperatures, high tolerance to DMSO, and metal ions (majority of analysed metal ions in a concentration of 1 mM improve the activity of the esterase where in the case of other esterases, the presence of these ions cause a reduction in the activity of an enzyme). These features can be important in various industrial applications such as detergent formulations, pharmaceutical production and other fine chemicals [113]. On the other hand, GH11 xylanase Xyn22 has very high halotolerance and thermal stability.…”

Section: In Silico Methods For Identification Of Novel Halophiles Bioproductsmentioning

confidence: 99%

“…Culture-independent methods are the primary investigation tools for looking into the microbial "dark matter" based on the sequencing of nucleic acids for both entire microbial communities (metagenomics and metatranscriptomics) and single cells (single-cell sequencing) [110,112]. Furthermore, functional metagenomics can be used, where it is possible to screen environmental samples for the production of substances of interest with potential industrial applications [113,114]. Finally, metatranscriptomic analyses enable the assessment of the gene expression in the studied environment.…”

Section: Experiments Strategies Used In Halophiles Researchmentioning

confidence: 99%

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The Methods of Digging for “Gold” within the Salt: Characterization of Halophilic Prokaryotes and Identification of Their Valuable Biological Products Using Sequencing and Genome Mining Tools

Lach

Jecz

Strapagiel

et al. 2021

Genes

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Halophiles, the salt-loving organisms, have been investigated for at least a hundred years. They are found in all three domains of life, namely Archaea, Bacteria, and Eukarya, and occur in saline and hypersaline environments worldwide. They are already a valuable source of various biomolecules for biotechnological, pharmaceutical, cosmetological and industrial applications. In the present era of multidrug-resistant bacteria, cancer expansion, and extreme environmental pollution, the demand for new, effective compounds is higher and more urgent than ever before. Thus, the unique metabolism of halophilic microorganisms, their low nutritional requirements and their ability to adapt to harsh conditions (high salinity, high pressure and UV radiation, low oxygen concentration, hydrophobic conditions, extreme temperatures and pH, toxic compounds and heavy metals) make them promising candidates as a fruitful source of bioactive compounds. The main aim of this review is to highlight the nucleic acid sequencing experimental strategies used in halophile studies in concert with the presentation of recent examples of bioproducts and functions discovered in silico in the halophile’s genomes. We point out methodological gaps and solutions based on in silico methods that are helpful in the identification of valuable bioproducts synthesized by halophiles. We also show the potential of an increasing number of publicly available genomic and metagenomic data for halophilic organisms that can be analysed to identify such new bioproducts and their producers.

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Characterization of a Novel Esterase Belonging to Family V from Marinobacter flavimaris

He,

Zhang,

et al. 2024

J. Ocean Univ. China

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Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach

Cited by 13 publications

References 60 publications

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

The Methods of Digging for “Gold” within the Salt: Characterization of Halophilic Prokaryotes and Identification of Their Valuable Biological Products Using Sequencing and Genome Mining Tools

Characterization of a Novel Esterase Belonging to Family V from Marinobacter flavimaris

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