A5049955442- Enzyme Catalysis and Immobilization
- Microbial Metabolic Engineering and Bioproduction
- Electrochemical sensors and biosensors
- Advanced Nanomaterials in Catalysis
- Mesoporous Materials and Catalysis
- DNA and Nucleic Acid Chemistry
- RNA Interference and Gene Delivery
- Analytical chemistry methods development
- Heme Oxygenase-1 and Carbon Monoxide
- Hemoglobin structure and function
- Cancer, Hypoxia, and Metabolism
- Metabolomics and Mass Spectrometry Studies
- Proteins in Food Systems
- Advanced biosensing and bioanalysis techniques
- Biofuel production and bioconversion
- CRISPR and Genetic Engineering
- Innovative Microfluidic and Catalytic Techniques Innovation
- Nanoporous metals and alloys
- Aldose Reductase and Taurine
- Chemical and Physical Properties in Aqueous Solutions
- Alcohol Consumption and Health Effects
- Enhanced Oil Recovery Techniques
- Enzyme function and inhibition
- Metal-Organic Frameworks: Synthesis and Applications
- Enzyme-mediated dye degradation
University of Limerick
2021-2024
Metal organic frameworks (MOFs) have been used to encapsulate an array of enzymes in a rapid and facile manner; however, the stability MOFs as supports for has not examined detail. This study examines with different compositions (Fe-BTC, Co-TMA, Ni-TMA, Cu-TMA, ZIF-zni) buffered solutions commonly enzyme immobilization biocatalysis. Stability was assessed via quantification release metals by inductively coupled plasma optical emission spectroscopy. The buffers had varied effects on MOF...
An immobilized bi-enzymatic (ALDH Tt -LDH) flow reactor has been develeoped for the selective oxidation of aldehydes.
The development of an electrochemical biosensor utilising a hairpin DNA probe labelled with methylene blue for the detection TP53 gene is described. Structural rearrangement into linear double strand induced different rates electron transfer that enabled increase in current upon hybridization. observed hybridization was studied at surface densities, times, concentration and length target sequences. selectively detected single nucleotide polymorphism affecting residue 175 p53 protein,...
Aldehyde dehydrogenase enzymes (ALDHs) are widely studied for their roles in disease propagation and cell metabolism. Their use biocatalysis applications, the conversion of aldehydes to carboxylic acids, has also been recognized. Understanding structural features functions both prokaryotic eukaryotic ALDHs is key uncovering novel applications enzyme probing its role propagation. The thermostable ALDH
Peroxidases are promising catalysts for oxidation reactions, yet their practical utility has been hindered by the fact that they require hydrogen peroxide (H2O2), which at high concentrations can cause deactivation of enzymes. Practical processes involving use peroxidases frequent addition low H2O2. In situ generation H2O2 be achieved using oxidase-type this study, a three-enzyme cascade system comprised generator (glucose oxidase (GOx)), H2O2-dependent enzymes (chloroperoxidase (CPO) or...
Biotherapeutic development presents a myriad of challenges in relation to delivery, particular for protein therapeutics. Protein delivery is complicated due hydrophilicity, size, rate degradation vivo, low permeation through biological barriers, pH and temperature sensitivity, as well the need conserve its quaternary structure retain function. To preserve therapeutic levels proteins require frequent administration their short half-lives. Formulation strategies combining with lipid carriers...
Aldehyde dehydrogenases (ALDH), found in all kingdoms of life, form a superfamily enzymes that primarily catalyse the oxidation aldehydes to carboxylic acid products, while utilising cofactor NAD(P)+. Some members can also act as esterases using p-nitrophenyl esters substrates. The ALDHTt from Thermus thermophilus was recombinantly expressed E. coli and purified obtain high yields (approximately 15–20 mg/L) purity an efficient heat treatment step coupled with IMAC gel filtration...
Abstract The precise spatial control of the immobilisation enzymes is necessary for sequential localisation an enzymatic cascade. In this contribution, alcohol dehydrogenase (ADH), formaldehyde (FLDH) and formate (FoDH) on self‐assembled monolayer modified electrodes has been demonstrated. A range thiols were screened optimal activity was obtained with bearing ‐OH, a positively charged heterocyclic aromatic ring ‐COOH ADH, FLDH FoDH, respectively. Scanning applied potential utilised to...
Based on previous in-depth characterisation, aldehyde dehydrogenases (ALDH) are a diverse superfamily of enzymes, in terms both structure and function, present all kingdoms life. They catalyse the oxidation an to carboxylic acid using cofactor nicotinamide adenine dinucleotide (phosphate) (NAD(P)+), often not substrate-specific, but rather have broad range associated biological functions, including detoxification biosynthesis. We studied ALDHTt from Thermus thermophilus, as well performed...