Interaction of silver nanoparticles with catechol O-methyltransferase: Spectroscopic and simulation analyses
- Usman, Aminu, Lobb, Kevin A, Pletschke, Brett I, Whiteley, Christopher G, Wilhelmi, Brendan S
- Authors: Usman, Aminu , Lobb, Kevin A , Pletschke, Brett I , Whiteley, Christopher G , Wilhelmi, Brendan S
- Date: 2021
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/451095 , vital:75018 , xlink:href=" https://doi.org/10.1016/j.bbrep.2021.101013"
- Description: Catechol O-methyltransferase, an enzyme involved in the metabolism of catechol containing compounds, catalyzes the transfer of a methyl group between S-adenosylmethionine and the hydroxyl groups of the catechol. Furthermore it is considered a potential drug target for Parkinson’s disease as it metabolizes the drug levodopa. Consequently inhibitors of the enzyme would increase levels of levodopa. In this study, absorption, fluorescence and infrared spectroscopy as well as computational simulation studies investigated human soluble catechol Omethyltransferase interaction with silver nanoparticles. The nanoparticles form a corona with the enzyme and quenches the fluorescence of Trp143. This amino acid maintains the correct structural orientation for the catechol ring during catalysis through a static mechanism supported by a non-fluorescent fluorophore–nanoparticle complex. The enzyme has one binding site for AgNPs in a thermodynamically spontaneous binding driven by electrostatic interactions as confirmed by negative ΔG and ΔH and positive ΔS values. Fourier transform infrared spectroscopy within the amide I region of the enzyme indicated that the interaction causes relaxation of its β− structures, while simulation studies indicated the involvement of six polar amino acids. These findings suggest AgNPs influence the catalytic activity of catechol O-methyltransferase, and therefore have potential in controlling the activity of the enzyme.
- Full Text:
- Date Issued: 2021
- Authors: Usman, Aminu , Lobb, Kevin A , Pletschke, Brett I , Whiteley, Christopher G , Wilhelmi, Brendan S
- Date: 2021
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/451095 , vital:75018 , xlink:href=" https://doi.org/10.1016/j.bbrep.2021.101013"
- Description: Catechol O-methyltransferase, an enzyme involved in the metabolism of catechol containing compounds, catalyzes the transfer of a methyl group between S-adenosylmethionine and the hydroxyl groups of the catechol. Furthermore it is considered a potential drug target for Parkinson’s disease as it metabolizes the drug levodopa. Consequently inhibitors of the enzyme would increase levels of levodopa. In this study, absorption, fluorescence and infrared spectroscopy as well as computational simulation studies investigated human soluble catechol Omethyltransferase interaction with silver nanoparticles. The nanoparticles form a corona with the enzyme and quenches the fluorescence of Trp143. This amino acid maintains the correct structural orientation for the catechol ring during catalysis through a static mechanism supported by a non-fluorescent fluorophore–nanoparticle complex. The enzyme has one binding site for AgNPs in a thermodynamically spontaneous binding driven by electrostatic interactions as confirmed by negative ΔG and ΔH and positive ΔS values. Fourier transform infrared spectroscopy within the amide I region of the enzyme indicated that the interaction causes relaxation of its β− structures, while simulation studies indicated the involvement of six polar amino acids. These findings suggest AgNPs influence the catalytic activity of catechol O-methyltransferase, and therefore have potential in controlling the activity of the enzyme.
- Full Text:
- Date Issued: 2021
Evaluating Feruloyl Esterase—Xylanase Synergism for Hydroxycinnamic Acid and Xylo-Oligosaccharide Production from Untreated, Hydrothermally Pre-Treated and Dilute-Acid Pre-Treated Corn Cobs:
- Mkabayi, Lithalethu, Malgas, Samkelo, Wilhelmi, Brendan S, Pletschke, Brett I
- Authors: Mkabayi, Lithalethu , Malgas, Samkelo , Wilhelmi, Brendan S , Pletschke, Brett I
- Date: 2020
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/149240 , vital:38818 , https://doi.org/10.3390/agronomy10050688
- Description: Agricultural residues are considered the most promising option as a renewable feedstock for biofuel and high valued-added chemical production due to their availability and low cost. The efficient enzymatic hydrolysis of agricultural residues into value-added products such as sugars and hydroxycinnamic acids is a challenge because of the recalcitrant properties of the native biomass. Development of synergistic enzyme cocktails is required to overcome biomass residue recalcitrance, and achieve high yields of potential value-added products. In this study, the synergistic action of two termite metagenome-derived feruloyl esterases (FAE5 and FAE6), and an endo-xylanase (Xyn11) from Thermomyces lanuginosus, was optimized using 0.5% (w/v) insoluble wheat arabinoxylan (a model substrate) and then applied to 1% (w/v) corn cobs for the efficient production of xylo-oligosaccharides (XOS) and hydroxycinnamic acids.
- Full Text:
- Date Issued: 2020
- Authors: Mkabayi, Lithalethu , Malgas, Samkelo , Wilhelmi, Brendan S , Pletschke, Brett I
- Date: 2020
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/149240 , vital:38818 , https://doi.org/10.3390/agronomy10050688
- Description: Agricultural residues are considered the most promising option as a renewable feedstock for biofuel and high valued-added chemical production due to their availability and low cost. The efficient enzymatic hydrolysis of agricultural residues into value-added products such as sugars and hydroxycinnamic acids is a challenge because of the recalcitrant properties of the native biomass. Development of synergistic enzyme cocktails is required to overcome biomass residue recalcitrance, and achieve high yields of potential value-added products. In this study, the synergistic action of two termite metagenome-derived feruloyl esterases (FAE5 and FAE6), and an endo-xylanase (Xyn11) from Thermomyces lanuginosus, was optimized using 0.5% (w/v) insoluble wheat arabinoxylan (a model substrate) and then applied to 1% (w/v) corn cobs for the efficient production of xylo-oligosaccharides (XOS) and hydroxycinnamic acids.
- Full Text:
- Date Issued: 2020
Cellulases (CMCases) and polyphenol oxidases from thermophilic Bacillus spp
- Mayende, Lungisa, Wilhelmi, Brendan S, Pletschke, Brett I
- Authors: Mayende, Lungisa , Wilhelmi, Brendan S , Pletschke, Brett I
- Date: 2006
- Language: English
- Type: Article
- Identifier: vital:6462 , http://hdl.handle.net/10962/d1005791 , http://dx.doi.org/10.1016/j.soilbio.2006.03.019
- Description: In composting, organic matter is degraded by cellulases and ligninolytic enzymes at temperatures typically above 50 °C. This study isolated thermophilic microorganisms from a compost system that were then screened for cellulase and polyphenol oxidase activity. Temperature optima for the cellulases and polyphenol oxidases were determined as 70 and 40 °C, respectively. Maximal cellulase activity was determined as 1.333 mg glucose released ml[superscript −1] min[superscript −1]. Maximal polyphenol oxidase activity attained was 5.111 nmol phenol ml[superscript −1] min[superscript −1]. Cellulases were found to be stable over a period of 1 h. The isolated compost microorganisms were identified as strains of Bacillus using 16S ribosomal DNA sequence analysis.
- Full Text:
- Date Issued: 2006
- Authors: Mayende, Lungisa , Wilhelmi, Brendan S , Pletschke, Brett I
- Date: 2006
- Language: English
- Type: Article
- Identifier: vital:6462 , http://hdl.handle.net/10962/d1005791 , http://dx.doi.org/10.1016/j.soilbio.2006.03.019
- Description: In composting, organic matter is degraded by cellulases and ligninolytic enzymes at temperatures typically above 50 °C. This study isolated thermophilic microorganisms from a compost system that were then screened for cellulase and polyphenol oxidase activity. Temperature optima for the cellulases and polyphenol oxidases were determined as 70 and 40 °C, respectively. Maximal cellulase activity was determined as 1.333 mg glucose released ml[superscript −1] min[superscript −1]. Maximal polyphenol oxidase activity attained was 5.111 nmol phenol ml[superscript −1] min[superscript −1]. Cellulases were found to be stable over a period of 1 h. The isolated compost microorganisms were identified as strains of Bacillus using 16S ribosomal DNA sequence analysis.
- Full Text:
- Date Issued: 2006
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