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Stability and structural changes of horseradish peroxidase: Microwave versus conventional heating treatment
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1016/0969-806x(94)00072-ropenalex-snapshot
Microwaves in chemistry: Another way of heating reaction mixtures
inferredcites →https://doi.org/10.1016/j.foodchem.2004.03.023openalex-snapshot
Role of peroxidase in anthocyanin degradation in litchi fruit pericarp
inferredcites →https://doi.org/10.1016/j.foodchem.2004.08.010openalex-snapshot
Inactivation and conformational change of horseradish peroxidase induced by pulsed electric field
inferredcites →https://doi.org/10.1016/j.foodchem.2005.05.028openalex-snapshot
Inactivation and structural change of horseradish peroxidase treated with supercritical carbon dioxide
inferredcites →https://doi.org/10.1016/j.foodchem.2010.06.052openalex-snapshot
Inhibition of polyphenol oxidase and peroxidase activities on fresh-cut apple by simultaneous treatment of ultrasound and ascorbic acid
inferredcites →https://doi.org/10.1016/j.foodchem.2011.01.034openalex-snapshot
The role of polyphenol oxidase and peroxidase in the browning of water caltrop pericarp during heat treatment
inferredcites →https://doi.org/10.1016/j.foodchem.2011.03.130openalex-snapshot
Effect of microwave pretreatment on the kinetics of ascorbic acid degradation and peroxidase inactivation in different parts of green asparagus (Asparagus officinalis L.) during water blanching
inferredcites →https://doi.org/10.1016/j.foodres.2012.02.013openalex-snapshot
Power ultrasound processing of cantaloupe melon juice: Effects on quality parameters
inferredcites →https://doi.org/10.1016/j.ifset.2011.10.013openalex-snapshot
Inactivation kinetics of peroxidase in zucchini (Cucurbita pepo L.) by heat and UV-C radiation
inferredcites →https://doi.org/10.1016/j.jfoodeng.2004.06.009openalex-snapshot
Kinetics and inactivation of carrot peroxidase by heat treatment
inferredcites →https://doi.org/10.1016/j.jfoodeng.2008.02.003openalex-snapshot
Inactivation kinetics of polyphenol oxidase and peroxidase in green coconut water by microwave processing
inferredcites →https://doi.org/10.1016/j.jfoodeng.2011.11.026openalex-snapshot
Microwave inactivation of red beet (Beta vulgaris L. var. conditiva) peroxidase and polyphenoloxidase and the effect of radiation on vegetable tissue quality
inferredcites →https://doi.org/10.1016/j.molcatb.2009.03.008openalex-snapshot
Biocatalytic reactions in hydrophobic ionic liquids
inferredcites →https://doi.org/10.1016/j.phytochem.2003.10.022openalex-snapshot
Horseradish peroxidase: a modern view of a classic enzyme
inferredcites →https://doi.org/10.1016/j.supflu.2005.11.019openalex-snapshot
Evaluation of radish (Raphanus sativus L.) peroxidase activity after high-pressure treatment with carbon dioxide
inferredcites →https://doi.org/10.1016/j.supflu.2009.04.014openalex-snapshot
Effects of compressed fluids on the activity and structure of horseradish peroxidase
inferredcites →https://doi.org/10.1016/j.tca.2004.01.018openalex-snapshot
Two-state irreversible thermal denaturation of anionic peanut (Arachis hypogaea L.) peroxidase
inferredcites →https://doi.org/10.1016/j.ultsonch.2010.09.014openalex-snapshot
Effect of ultrasound and temperature on tomato peroxidase
inferredcites →https://doi.org/10.1016/s0003-9861(03)00275-3openalex-snapshot
Heme and pH-dependent stability of an anionic horseradish peroxidase
inferredcites →https://doi.org/10.1016/s0040-4020(01)00905-xopenalex-snapshot
A tentative rationalization of microwave effects in organic synthesis according to the reaction medium, and mechanistic considerations
inferredcites →https://doi.org/10.1016/s0040-4020(02)00085-6openalex-snapshot
Solvent-free preparation of amides from acids and primary amines under microwave irradiation
inferredcites →https://doi.org/10.1016/s0167-4838(96)00190-2openalex-snapshot
The application of circular dichroism to studies of protein folding and unfolding
inferredcites →https://doi.org/10.1016/s1381-1177(01)00017-0openalex-snapshot
Stability of free and immobilised peroxidase in aqueous–organic solvents mixtures
inferredcites →https://doi.org/10.1021/ac0108111openalex-snapshot
Mechanistic and Molecular Investigations on Stabilization of Horseradish Peroxidase C
inferredcites →https://doi.org/10.1021/bi990729oopenalex-snapshot
Structural and Conformational Stability of Horseradish Peroxidase: Effect of Temperature and pH
inferredcites →https://doi.org/10.1021/cr960383copenalex-snapshot
Protein Structure and the Energetics of Protein Stability
inferredcites →https://doi.org/10.1021/jf0481610openalex-snapshot
Heat Inactivation and Reactivation of Broccoli Peroxidase
inferredcites →https://doi.org/10.1021/jo7022697openalex-snapshot
Nonthermal Microwave Effects Revisited: On the Importance of Internal Temperature Monitoring and Agitation in Microwave Chemistry
inferredcites →https://doi.org/10.1038/417463aopenalex-snapshot
The catalytic pathway of horseradish peroxidase at high resolution
inferredcites →https://doi.org/10.1038/nsb1297-1032openalex-snapshot
Crystal structure of horseradish peroxidase C at 2.15 Å resolution
inferredcites →https://doi.org/10.1046/j.1432-1033.2001.01855.xopenalex-snapshot
Thermally induced conformational changes in horseradish peroxidase
inferredcites →https://doi.org/10.1074/jbc.m408806200openalex-snapshot
Protein Stabilization by Osmolytes from Hyperthermophiles
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.0823p.xopenalex-snapshot
pH‐Induced Conformational Perturbation in Horseradish Peroxidase
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.0825a.xopenalex-snapshot
Structural Influence of Calcium on the Heme Cavity of Cationic Peanut Peroxidase as Determined by 1H‐NMR Spectroscopy
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.tb20207.xopenalex-snapshot
pH-Induced Conformational Perturbation in Horseradish Peroxidase. Picosecond Tryptophan Fluorescence Studies on Native and Cyanide-Modified Enzymes
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.tb20879.xopenalex-snapshot
Structural Influence of Calcium on the Heme Cavity of Cationic Peanut Peroxidase as Determined by 1H-NMR Spectroscopy
inferredcites →https://doi.org/10.1385/1592591930openalex-snapshot
Protein Structure, Stability, and Folding
inferredcites →https://doi.org/10.1590/s0100-40422006000300024openalex-snapshot
Efeito da composição do solvente sobre a estabilidade de proteínas em soluções aquosas
inferredcites →https://doi.org/10.4315/0362-028x-59.10.1065openalex-snapshot
Thermal Inactivation at High Temperatures and Regeneration of Green Asparagus Peroxidase
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Fatty Acids Activate Membrane-Bound Polyphenol Oxidase in Peach Fruit by Changing Enzyme Structure Conformation
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Inhibition of horseradish peroxidase activity through conformational change in surfactant solution
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Non-thermal effects of microwave and ohmic processing on microbial and enzyme inactivation: a critical review
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Effect of ultrasound combined with malic acid on the activity and conformation of mushroom (Agaricus bisporus) polyphenoloxidase
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Hyaluronic acid-coated chitosan nanoparticles as carrier for the enzyme/prodrug complex based on horseradish peroxidase/indole-3-acetic acid: Characterization and potential therapeutic for bladder cancer cells
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Activation mechanism of fatty acids on membrane-bound polyphenol oxidase in peach fruit: Conformational change analysis and molecular docking simulation
inferred← citeshttps://doi.org/10.1016/j.foodchem.2016.07.041openalex-snapshot
Aggregation and conformational change of mushroom ( Agaricus bisporus ) polyphenoloxidase subjected to thermal treatment
inferred← citeshttps://doi.org/10.1016/j.foodchem.2017.04.149openalex-snapshot
Effect of pulsed light on activity and structural changes of horseradish peroxidase
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Pulsed light inactivation of horseradish peroxidase and associated structural changes
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Effect of microwave-assisted processing on polyphenol oxidase and peroxidase inactivation kinetics of açai-berry (Euterpe oleracea) pulp
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Biosensor of horseradish peroxidase immobilized onto self-assembled monolayers: Optimization of the deposition enzyme concentration
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Horseradish peroxidase biocatalytic reaction monitoring using Near-Infrared (NIR) Spectroscopy
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Online monitoring of horseradish peroxidase structural changes by Near Infrared (NIR) Spectroscopy
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Immobilization and characterization of horseradish peroxidase into chitosan and chitosan/PEG nanoparticles: A comparative study
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