The tale of a versatile enzyme: Alpha-amylase evolution, structure, and potential biotechnological applications for the bioremediation of n-alkanes

Pinto, Éderson Sales Moreira; Dorn, Márcio; Feltes, Bruno César

doi:10.1016/j.chemosphere.2020.126202

Cited by 26 publications

(22 citation statements)

References 210 publications

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“…The alkaline adaptation of extracellular enzymes produced by microorganisms is rare since the intracellular medium has neutral pH. However, remodeling of amino acid pairs such as Arg-Asp in α-amylase was shown to increase alkaline performance, while Lys-Asp pairing was linked to non-alkaline resistance [ 37 ]. The latter configuration could be linked to the nature of the α-amylase produced by B. licheniformis strain LB04.…”

Section: Discussionmentioning

confidence: 99%

Novel Thermotolerant Amylase from Bacillus licheniformis Strain LB04: Purification, Characterization and Agar-Agarose

et al. 2021

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This study analyzed the thermostability and effect of calcium ions on the enzymatic activity of α-amylase produced by Bacillus licheniformis strain LB04 isolated from Espinazo Hot springs in Nuevo Leon, Mexico. The enzyme was immobilized by entrapment on agar-agarose beads, with an entrapment yield of 19.9%. The identification of the bacteria was carried out using 16s rDNA sequencing. The enzyme was purified through ion exchange chromatography (IEX) in a DEAE-Sephadex column, revealing a protein with a molecular weight of ≈130 kDa. The enzyme was stable at pH 3.0 and heat stable up to 80 °C. However, the optimum conditions were reached at 65 °C and pH 3.0, with a specific activity of 1851.7 U mg−1 ± 1.3. The agar-agarose immobilized α-amylase had a hydrolytic activity nearly 25% higher when compared to the free enzyme. This study provides critical information for the understanding of the enzymatic profile of B. licheniformis strain LB04 and the potential application of the microorganisms at an industrial level, specifically in the food industry.

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Section: Discussionmentioning

confidence: 99%

Novel Thermotolerant Amylase from Bacillus licheniformis Strain LB04: Purification, Characterization and Agar-Agarose

et al. 2021

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“…16 As a matter of fact, in previous work, we demonstrated that α-amylase is one of the most well-known enzymes, with decades of structural and physical-chemical knowledge, adapted to a multitude of temperatures, pH, and even salinity. 17 Our study showed that there is enough available α-amylase data to allow it to be virtually adapted to any environment, which is fundamental to the bioremediation process. Therefore, this enzyme's ability to promiscuously degrade nalkanes is a remarkable trait that should be further explored.…”

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confidence: 81%

Modifying the catalytic preference of alpha‐amylase toward n‐alkanes for bioremediation purposes using in silico strategies

et al. 2021

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Since the beginning of oil exploration, whole ecosystems have been affected by accidents and bad practices involving petroleum compounds. In this sense, bioremediation stands out as the cheapest and most eco-friendly alternatives to reverse the damage done in oil-impacted areas. However, more efforts must be made to engineer enzymes that could be used in the bioremediation process. Interestingly, a recent work described that α-amylase, one of the most evolutionary conserved enzymes, was able to promiscuously degrade n-alkanes, a class of molecules abundant in the petroleum admixture. Considering that α-amylase is expressed in almost all known organisms, and employed in numerous biotechnological processes, using it can be a great leap toward more efficient applications of enzyme or microorganism-consortia bioremediation approaches. In this work, we employed a strict computational approach to design new α-amylase mutants with potentially enhanced catalytic efficiency toward n-alkanes. Using in silico techniques, such as molecular docking, molecular dynamics, metadynamics, and residue-residue interaction networks, we generated mutants potentially more efficient for degrading n-alkanes, L183Y, and N314A. Our results indicate that the new mutants have an increased binding rate for tetradecane, the longest n-alkane previously tested, which can reside in the catalytic center for more extended periods. Additionally, molecular dynamics and network analysis showed that the new mutations have no negative impact on protein structure than the WT. Our results aid in solidifying this enzyme as one more tool in the petroleum bioremediation toolbox.

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“…While bacterial CYPs are attractive because of their solubility, easy and low-cost production, and self-efficiency (their electron transfer reductases, e.g., FMN, FAD, and p450 monooxygenase, are on a single peptide), mammalian CYPs are membrane-bounded, dependent on a redox partner (e.g., NADPH) and have expansive applications [ 65 ]. Bacterial and eukaryotic CYPs can oxidize aliphatic hydrocarbons with 5–16 and 10–16 carbon lengths, respectively [ 66 ]. Notably, eukaryotic CYPs need modification at N-terminal, but prokaryotic ones are active in the native form [ 64 ].…”

Section: Enzymes For Organic Substratesmentioning

confidence: 99%

Recent Advances in Enzymes for the Bioremediation of Pollutants

Mousavi

Hashemi

Moezzi

et al. 2021

Biochemistry Research International

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Nowadays, pollution of the environment is a huge problem for humans and other organisms’ health. Conventional methods of pollutant removal like membrane filtration or ion exchange are not efficient enough to lower the number of pollutants to standard levels. Biological methods, because of their higher efficiency and biocompatibility, are preferred for the remediation of pollutants. These cost-effective and environment-friendly methods of reducing pollutants are called bioremediation. In bioremediation methods, enzymes play the most crucial role. Enzymes can remedy different types of organic and inorganic pollutants, including PAHs, azo dyes, polymers, organocyanides, lead, chromium, and mercury. Different enzymes isolated from various species have been used for the bioremediation of pollutants. Discovering new enzymes and new subtypes with specific physicochemical characteristics would be a promising way to find more efficient and cost-effective tools for the remediation of pollutants.

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The tale of a versatile enzyme: Alpha-amylase evolution, structure, and potential biotechnological applications for the bioremediation of n-alkanes

Cited by 26 publications

References 210 publications

Novel Thermotolerant Amylase from Bacillus licheniformis Strain LB04: Purification, Characterization and Agar-Agarose

Novel Thermotolerant Amylase from Bacillus licheniformis Strain LB04: Purification, Characterization and Agar-Agarose

Modifying the catalytic preference of alpha‐amylase toward n‐alkanes for bioremediation purposes using in silico strategies

Recent Advances in Enzymes for the Bioremediation of Pollutants

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