Results 41 to 50 of about 352,568 (281)
Effect of Water Content on the Thermal Inactivation Kinetics of Horseradish Peroxidase Freeze-Dried from Alkaline pH [PDF]
, 2001 The thermal inactivation of horseradish peroxidase freeze-dried from solutions of different pH (8, 10 and 11.5, measured at 25 C) and equilibrated to different water contents was studied in the temperature range from 110 to 150 C.
Oliveira, J. C. +2 more
core +1 more source
, 2021 We described an analyte-activatable artificial peroxidase system (caged Mn-2(bpmp)) by caging a dimanganese complex, exhibiting peroxidase-like activity, with an analyte-reactive trigger.
Han, Min Su, Lee, Suji
core +1 more source
Frontiers in Microbiology, 2017 White-rot fungi (WRF) and their ligninolytic enzymes (laccases and peroxidases) are considered promising biotechnological tools to remove lignin related Persistent Organic Pollutants from industrial wastewaters and contaminated ecosystems.
Giselle Torres-Farradá +9 more
doaj +1 more source
Structural Determinants of Oxidative Stabilization in an Evolved Versatile Peroxidase [PDF]
ACS Catalysis, 2014 [EN] Versatile peroxidases (VP) are promiscuous biocatalysts with the highest fragility to hydroperoxides yet reported due to a complex molecular architecture, with three catalytic sites and several oxidation pathways. To improve the VP resistance to H2O2, an evolved version of this enzyme was subjected to a range of directed evolution and hybrid ...
David Gonzalez-Perez +4 more
openaire +2 more sources
Versatile Peroxidases: Super Peroxidases with Potential Biotechnological Applications-A Mini Review [PDF]
Journal of Dairy, Veterinary & Animal Research, 2016 Ligninolytic enzymes play a crucial role in the carbon cycle on account of their ability to degrade the macromolecule lignin. Versatile peroxidase is a high redox potential enzyme of the lignin degrading family of enzymes widely studied for its unique characteristics of degradation of aromatics without use of redox mediators and presence of polyvalent ...
openaire +1 more source
DyP-type Peroxidases: A Promising and Versatile Class of Enzymes [PDF]
Enzyme Engineering, 2012 Peroxidases (EC1.11.1.x) represent a large family of oxidoreductases that typically use hydrogen peroxide as an electron acceptor to catalyze the oxidation of substrate molecules. The vast majority of these enzymes contain heme as a cofactor [1], and are ubiquitously present in prokaryotes and eukaryotes.
W., Marco, Van, Edwin
openaire +3 more sources
Biotechnology for Biofuels, 2021 Lignin, the most abundant renewable aromatic compound in nature, is an excellent feedstock for value-added bioproducts manufacturing; while the intrinsic heterogeneity and recalcitrance of which hindered the efficient lignin biorefinery and utilization ...
Caihong Weng, Xiaowei Peng, Yejun Han
doaj +1 more source
Correction: Alkaline versatile peroxidase by directed evolution
Catalysis Science & Technology, 2016 Correction for ‘Alkaline versatile peroxidase by directed evolution’ by David Gonzalez-Perez et al. , Catal. Sci. Technol. , 2016, 6 , 6625–6636.
David Gonzalez-Perez +5 more
openaire +2 more sources
Widespread occurrence of expressed fungal secretory peroxidases in forest soils.
PLoS ONE, 2014 Fungal secretory peroxidases mediate fundamental ecological functions in the conversion and degradation of plant biomass. Many of these enzymes have strong oxidizing activities towards aromatic compounds and are involved in the degradation of plant cell ...
Harald Kellner +9 more
doaj +1 more source
Biosensors, 2023 Analytical methods for detecting neurotransmitters (NTs) and organophosphorus (OP) pesticides with high sensitivity are vitally necessary for the rapid identification of physical, mental, and neurological illnesses, as well as to ensure food safety and ...
Preeti Bhatt +3 more
doaj +1 more source