Expression, purification and biochemical characterization of a family 6 carboxylesterase from Methylococcus capsulatus (bath)

Soni, Surabhi; Odaneth, Annamma A.; Lali, Arvind; Chandrayan, Sanjeev K.

doi:10.1016/j.pep.2016.02.007

Cited by 3 publications

(4 citation statements)

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“…The purified R-est6 was analyzed on superdex-75 column that was calibrated with known molecular weight markers to estimate the oligomeric state of the protein [1] . Presence of R-est6 in different peaks was confirmed on SDS-PAGE.…”

Section: Experimental Design Materials and Methodsmentioning

confidence: 99%

“… The data presented in this article are connected to the research article entitled “Expression, purification and biochemical characterization of a family 6 carboxylesterase from Methylococcus capsulatus (bath) ” (Soni et al, 2016 [1] ). The family 6 carboxylesterases are the smallest and display broad substrate specificity.…”

mentioning

confidence: 99%

“…The 1 kb gene encoding, a family 6 carboxylesterase – R-est6, was amplified from the genome of M. capsulatus (bath strain), and showed in the agarose gel. The corresponding purified protein, after overexpression in Escherichia coli , was biochemically studied in the research article (Soni et al, 2016 [1] ). R-est6 has hydrophobic patches on the surface so, it is expected to show oligimeric forms.…”

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confidence: 99%

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Dataset of gene cloning and gel filtration chromatography of R-est6

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The data presented in this article are connected to the research article entitled “Expression, purification and biochemical characterization of a family 6 carboxylesterase from Methylococcus capsulatus (bath)” (Soni et al., 2016 [1]). The family 6 carboxylesterases are the smallest and display broad substrate specificity. The 1 kb gene encoding, a family 6 carboxylesterase – R-est6, was amplified from the genome of M. capsulatus (bath strain), and showed in the agarose gel. The corresponding purified protein, after overexpression in Escherichia coli, was biochemically studied in the research article (Soni et al., 2016 [1]). R-est6 has hydrophobic patches on the surface so, it is expected to show oligimeric forms. Here, we have confirmed the presence of oligomers by gel filtration chromatography data and the proteins belonging to the different peaks are shown on a SDS-PAGE.

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Section: Experimental Design Materials and Methodsmentioning

confidence: 99%

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Dataset of gene cloning and gel filtration chromatography of R-est6

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“…In search of better enzymes with enhanced properties from those existing in the market, researchers have propositioned various techniques. Using the method of metagenomics screening, a plethora of unique enzymes with lipolytic activity have been taken from diverse environmental sources [6,7]. With the growing knowledge of the machinery for the modulation of gene expression, functional improvement of the expression systems is currently in progress, and new improved strains are regularly emerging.…”

Section: Introductionmentioning

confidence: 99%

Trends in lipase engineering for enhanced biocatalysis

Soni

2021

Biotech and App Biochem

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Lipases, also known as triacylglycerol hydrolases (E.C. No. 3.1.1.3), are considered as leading biocatalysts in the lipid modification business. With properties like ease of availability, capability to work in heterogeneous media, stability in organic solvents, property of catalyzing at the lipid-water interface and even in nonaqueous conditions, have made them a versatile choice for applications in the food, flavor, detergent, pharmaceutical, leather, textile, cosmetic, and paper industries [1]. The increasing alertness toward sustainable technologies, lesser waste generation and solvent usage and minimization of energy input has brought light toward the production and usage of recombinant/improved lipases. For example, Novozym 435, a broadly used recombinant lipase isolated from Candida antarctica, dominates the lipase industry and has even created a supplier bias in the market. This shows that there is a desperate need for novel, low-cost lipases with better properties. For this, mining of existing extremophilic genomes seems more rewarding. But considering the diversity of industrial requirements such as types of solvents used or carrier systems employed for enzyme immobilization, tailor-designed enzymes are an unrealized pressing priority. Therefore, protein engineering strategies in collaboration with the discovery of new lipases can serve as a vital tool to obtain tailor-made enzymes with specific characteristics.

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Characterization of a carboxylesterase with hyper-thermostability and alkali-stability from Streptomyces lividans TK24

Chang

Chen

et al. 2021

Extremophiles

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Expression, purification and biochemical characterization of a family 6 carboxylesterase from Methylococcus capsulatus (bath)

Cited by 3 publications

References 29 publications

Dataset of gene cloning and gel filtration chromatography of R-est6

Dataset of gene cloning and gel filtration chromatography of R-est6

Trends in lipase engineering for enhanced biocatalysis

Characterization of a carboxylesterase with hyper-thermostability and alkali-stability from Streptomyces lividans TK24

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