Mathematical modeling of enzymatic syntheses of biosurfactants catalyzed by immobilized lipases

Torres, Alice de C.L.; Lima, Lionete Nunes de; Tardioli, Paulo Waldir; Sousa, Ruy

doi:10.1007/s11144-020-01812-w

Cited by 5 publications

(3 citation statements)

References 38 publications

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“…The occurrence probability of residue 240 for acidic residues in the catalytic triads, including glutamate and aspartate, was 23.88% and 74.13%, respectively. During the hydrolysis process, the position determination of H270 was assisted by E240 via a hydrogen-bond interaction [ 18 , 40 ]. Noteworthy, E240 and H270 belong to coupling evolutionary residue pairs according to the Ev-coupling analysis.…”

Section: Resultsmentioning

confidence: 99%

Computational Insights into the Allosteric Modulation of a Phthalate-Degrading Hydrolase by Distal Mutations

Bao

et al. 2023

Biomolecules

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Phthalate esters (PAEs) are a ubiquitous kind of environmental endocrine that disrupt chemicals, causing environmental and health issues. EstJ6 is an effective phthalate-degrading hydrolase, and its mutant with a combination of three non-conservative distal mutations has an improved activity against PAEs with unknown molecular mechanisms. Herein, we attempt to fill the significant gap between distal mutations and the activity of this enzyme using computational approaches. We found that mutations resulted in a redistribution of the enzyme’s preexisting conformational states and dynamic changes of key functional regions, especially the lid over the active site. The outward motion of the lid upon the mutations made it easier for substrates or products to enter or exit. Additionally, a stronger substrate binding affinity and conformational rearrangements of catalytic reaction-associated residues in the mutant, accompanied by the strengthened communication within the protein, could synergistically contribute to the elevated catalytic efficiency. Finally, an attempt was made to improve the thermostability of EstJ6 upon introducing a distal disulfide bond between residues A23 and A29, and the simulation results were as expected. Together, our work explored the allosteric effects caused by distal mutations, which could provide insights into the rational design of esterases for industrial applications in the future.

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Section: Resultsmentioning

confidence: 99%

Computational Insights into the Allosteric Modulation of a Phthalate-Degrading Hydrolase by Distal Mutations

Bao

et al. 2023

Biomolecules

View full text Add to dashboard Cite

show abstract

“…The occurrence probability of residue 240 for acidic residues in the catalytic triads including glutamate and aspartate is 23.88% and 74.13%, respectively. During the hydrolysis process, the position determination of H270 is assisted by E240 via hydrogen-bond interaction [18,40]. Noteworthy, E240 and H270 belong to coupling evolutionary residues pairs according to the Ev-coupling analysis.…”

Section: Sequential and Structural Analyses Of Estj6mentioning

confidence: 99%

Computational Insights into the Allosteric Modulation of a Phthalate-Degrading Hydrolase by Distal Mutations

Xu¹,

Bao²,

Li³

et al. 2023

Preprint

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Phthalate esters (PAEs) are a ubiquitous kind of environmental endocrine-disrupting chemicals, causing environmental and health issues. EstJ6 is an effective phthalate-degrading hydrolase, and its mutant with a combination of three non-conservative distal mutations has an improved activity against PAEs with unknown molecular mechanisms. Herein, we attempt to fill the significant gap between distal mutations and the activity of this enzyme using computational approaches. We find mutations result in a redistribution of enzyme’s preexisting conformational states and dynamics changes of key functional regions, especially the lid over the active site. The outward motion of the lid upon mutations should make it easier for substrates or products to enter or exit. Additionally, the stronger substrate binding affinity and conformational rearrangements of catalytic reaction-associated residues in mutant, accompanied by the strengthened communication within the protein, might contribute to the elevated catalytic efficiency. Finally, an attempt has been done to improve the thermostability of EstJ6 upon introducing a distal disulfide bond between residues A23 and A29, and the simulation results are as expected. Together, our work explored the allosteric effects caused by distal mutations, which could provide insights into the rational design of esterases for industrial applications in the future.

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“…Candida antarctica immobilized lipase B is the most employed biocatalyst in sugar esters synthesis [28,[31][32][33]. Other lipases have been used in the synthesis of SFAEs to a lesser extent including the lipase produced by Rhizomucor miehei [21,34,35]. Numerous studies from the literature deal with esterification and transesterification reactions catalyzed by lipases for hexoses acylation, in particular D-glucose [21,[36][37][38].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Production of Lauroyl and Stearoyl Monoesters of d-Xylose, l-Arabinose, and d-Glucose as Potential Lignocellulosic-Derived Products, and Their Evaluation as Antimicrobial Agents

Giorgi

Botto

Fontana³

et al. 2022

Catalysts

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Forestry and agricultural industries constitute highly relevant economic activities globally. They generate large amounts of residues rich in lignocellulose that have the potential to be valorized and used in different industrial processes. Producing renewable fuels and high-value-added compounds from lignocellulosic biomass is a key aspect of sustainable strategies and is central to the biorefinery concept. In this study, the use of biomass-derived monosaccharides for the enzymatic synthesis of sugar fatty acid esters (SFAEs) with antimicrobial activity was investigated to valorize these agro-industrial residues. With the aim to evaluate if lignocellulosic monosaccharides could be substrates for the synthesis of SFAEs, d-xylose, l-arabinose, and d-glucose, lauroyl and stearoyl monoesters were synthetized by transesterification reactions catalyzed by Lipozyme RM IM as biocatalyst. The reactions were performed using commercial d-xylose, l-arabinose, and d-glucose separately as substrates, and a 74:13:13 mixture of these sugars. The proportion of monosaccharides in the latter mixture corresponds to the composition found in hemicellulose from sugarcane bagasse and switchgrass, as previously described in the literature. Products were characterized using nuclear magnetic resonance (NMR) spectroscopy and showed that only the primary hydroxyl group of these monosaccharides is involved in the esterification reaction. Antimicrobial activity assay using several microorganisms showed that 5-O-lauroyl-d-xylofuranose and 5-O-lauroyl-l-arabinofuranose have the ability to inhibit the growth of Gram-positive bacteria separately and in the products mix. Furthermore, 5-O-lauroyl-l-arabinofuranose was the only product that exhibited activity against Candida albicans yeast, and the four tested filamentous fungi. These results suggest that sugar fatty acid esters obtained from sustainable and renewable resources and produced by green methods are promising antimicrobial agents.

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Mathematical modeling of enzymatic syntheses of biosurfactants catalyzed by immobilized lipases

Cited by 5 publications

References 38 publications

Computational Insights into the Allosteric Modulation of a Phthalate-Degrading Hydrolase by Distal Mutations

Computational Insights into the Allosteric Modulation of a Phthalate-Degrading Hydrolase by Distal Mutations

Computational Insights into the Allosteric Modulation of a Phthalate-Degrading Hydrolase by Distal Mutations

Enzymatic Production of Lauroyl and Stearoyl Monoesters of d-Xylose, l-Arabinose, and d-Glucose as Potential Lignocellulosic-Derived Products, and Their Evaluation as Antimicrobial Agents

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