Use of Extremophiles Microorganisms for Metal Removal

Díaz-Tena, E.; Rodríguez-Ezquerro, A.; Lacalle, Luís Norberto López de; Bustinduy, Luis Gurtubay; Saenz, Adrian

doi:10.1016/j.proeng.2013.08.197

Cited by 14 publications

(7 citation statements)

References 7 publications

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“…Today, environmental sustainability is one of the main objectives of all manufacturing processes (Diaz-Tena et al, 2013). So, new environmental laws for the protection of the environment are pushing industrial sectors to take ISSN (print): 1823-8262, ISSN (online): 2231-7538 into account the importance of creating new technologies that are more eco-friendly (Díaz-Tena et al, 2013). In this context, the current trend is to gradually replace chemical industrial molecules that pollute the environment with natural enzymes, particularly those extracted from extremophilic microorganisms (Adrio and Demain, 2014).…”

Section: Discussionmentioning

confidence: 99%

Screening and isolation of halophilic bacteria producing extracellular hydrolytic enzymes from salterns of the protected ecosystem Khnifiss Lagoon (Morocco)

Abdessamad¹,

Aicha²,

Abdellatif³

et al. 2023

MJM

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Aims:The present study was aimed to determine the diversity of the halophilic and halotolerant bacteria with hydrolase activities from salterns of the protected ecosystem Khnifiss lagoon (Morocco). Methodology and results: Bacteria were isolated from sediment samples collected at five hypersaline sites on three different growth media supplemented with various concentrations of NaCl. Thirty bacterial isolates were identified using the 16S rDNA sequencing method. Physiological characterization was examined on Columbia agar with different concentrations of NaCl and pH values and incubated at different temperatures. Enzymatic activities were tested in submerged cultures with appropriate substrates. A total of 246 halophilic bacterial isolates from the salines of the protected ecosystem of Khnifiss lagoon in the south of Morocco were able to produce different hydrolases (cellulases, amylases, DNases, lipases and proteases). Furthermore, the majority of the isolates were classified as moderately halophilic bacteria that grew optimally between 5% and 15% of NaCl, and they adapted to other extreme conditions than salt: some cases tolerated a pH range of 4.5 to 9.4, as well as a temperature range of 10 to 50 °C. The 16S rDNA sequencing and phylogenetic analysis results indicated that most of the bacteria isolated from the salt marshes studied belong to the genus Bacillus. Conclusion, significance and impact of study: Phenotypic and phylogenetic characterization of halophilic and halotolerant bacteria isolated from the salines of the protected ecosystem of Khnifiss lagoon has shown great diversity. Screening of hydrolytic enzymes produced by these bacteria suggests that the salines of the Khnifiss lagoon are a rich source of technologically interesting bacteria.

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Section: Discussionmentioning

confidence: 99%

Screening and isolation of halophilic bacteria producing extracellular hydrolytic enzymes from salterns of the protected ecosystem Khnifiss Lagoon (Morocco)

Abdessamad¹,

Aicha²,

Abdellatif³

et al. 2023

MJM

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“…AK activity was measured using an endpoint-coupled assay as previously optimized and employed in our laboratory. 40 The assay mixture contained buffer (25mM phosphate buffer pH 7.2, 5 mM MgCl2, 65 mM KCl), 1.4 mM AMP, and various ATP concentrations (5,10,25,50,100,250, 500, 1000 and 1400 μM). The reaction was started by the addition of AK enzyme to a final concentration of 10 nM (with the exception of BsAK-cp45, where 50 nM was used).…”

Section: Binding Assaysmentioning

confidence: 99%

“…AK homologs from extremophiles have been compared with those from mesophiles to study protein adaptation as well as the relationship between protein dynamics and function. 19,[22][23][24][25] The manipulation of AK genes in microorganisms has been additionally employed to demonstrate fitness adaptation to a variety of selection pressures. [26][27][28] Structural and kinetic studies performed on AKs from thermophilic, mesophilic, and psychrophilic organisms -Geobacillus stearothermophilus (GsAK), Bacillus subtilis (BsAK), Escherichia coli (EcAK), and Bacillus globisporus (BgAK), respectivelyhave revealed similar overall structures.…”

Section: Introductionmentioning

confidence: 99%

The biochemical impact of extracting an embedded adenylate kinase domain using circular permutation

Coleman,

Shin,

Silberg

et al. 2023

Preprint

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Adenylate kinases (AKs) are phosphotransferases that are frequently employed as models to investigate protein structure-function relationships. Prior studies have shown that AK homologs of different stabilities retain cellular activity in cells following circular permutation that split the AMP binding domain into fragments coded at different ends of the primary structure, such that this domain was no longer embedded as a continuous polypeptide within the core domain. Herein, we show mesophilic and thermophilic AKs having this topological restructuring retain activity and substrate-binding characteristics of the parental AK. While permutation decreased the activity of both AK homologs at physiological temperatures, the catalytic activity of the thermophilic AK increased upon permutation when assayed >30°C below the melting temperature of the native AK. The thermostabilities of the permuted AKs were uniformly lower than native AKs, and they exhibited multi-phasic unfolding transitions, unlike the native AKs, which presented cooperative thermal unfolding. In addition, proteolytic digestion revealed that permutation destabilized each AK, and mass spectrometry suggested that the new termini within the AMP binding domain were responsible for the increased proteolysis sensitivity. These findings illustrate how changes in contact order can be used to tune enzyme activity and alter folding dynamics in multidomain enzymes.

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“…The global market for industrial enzymes was nearly US$ 4.8 billion in 2013, and it is expected to reach US$ 7.1 billion by 2018, with a compound annual growth rate (CAGR) of 8% over the five-year period, according to BCC Research [ 3 ]. Besides their economic value, microbial enzymes are applied in technologies employing eco-friendly processes [ 4 ]. Microorganisms are easily cultivated in bioreactors with controllable growth conditions such as pH, temperature, aeration, medium composition and other parameters, leading to high reproducibility.…”

Section: Extremophiles From Marine Habitats: a Source Of Bioproducmentioning

confidence: 99%

Marine Extremophiles: A Source of Hydrolases for Biotechnological Applications

2015

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The marine environment covers almost three quarters of the planet and is where evolution took its first steps. Extremophile microorganisms are found in several extreme marine environments, such as hydrothermal vents, hot springs, salty lakes and deep-sea floors. The ability of these microorganisms to support extremes of temperature, salinity and pressure demonstrates their great potential for biotechnological processes. Hydrolases including amylases, cellulases, peptidases and lipases from hyperthermophiles, psychrophiles, halophiles and piezophiles have been investigated for these reasons. Extremozymes are adapted to work in harsh physical-chemical conditions and their use in various industrial applications such as the biofuel, pharmaceutical, fine chemicals and food industries has increased. The understanding of the specific factors that confer the ability to withstand extreme habitats on such enzymes has become a priority for their biotechnological use. The most studied marine extremophiles are prokaryotes and in this review, we present the most studied archaea and bacteria extremophiles and their hydrolases, and discuss their use for industrial applications.

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Use of Extremophiles Microorganisms for Metal Removal

Cited by 14 publications

References 7 publications

Screening and isolation of halophilic bacteria producing extracellular hydrolytic enzymes from salterns of the protected ecosystem Khnifiss Lagoon (Morocco)

Screening and isolation of halophilic bacteria producing extracellular hydrolytic enzymes from salterns of the protected ecosystem Khnifiss Lagoon (Morocco)

The biochemical impact of extracting an embedded adenylate kinase domain using circular permutation

Marine Extremophiles: A Source of Hydrolases for Biotechnological Applications

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