Results 11 to 20 of about 11,695 (199)
Stability/activity tradeoffs in Thermusthermophilus HB27 laccase [PDF]
JBIC Journal of Biological Inorganic Chemistry, 2020 We report the temperature dependence of the formal potential of type 1 copper (CuT1) in Thermusthermophilus HB27 laccase. Employing [Ru(NH3)4(bpy)](PF6)2 (0.505 vs. NHE) as the redox titrant, we found that the CuT12+/+ potential decreased from approximately 480 to 420 mV (vs. NHE) as the temperature was raised from 20 to 65 °C.
Shin, Jieun +2 more
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Enzymatic Characteristics of Laccase from Lactobacillus plantarum and Its Effect on Degradation of Biogenic Amines [PDF]
Shipin Kexue, 2023 In order to study the enzymatic properties of laccase derived from Lactobacillus and its potential application in biogenic amine degradation, the gene encoding laccase from Lactobacillus plantarum was heterologously expressed and the recombinant laccase ...
CAO Yuying, WANG Shuang, LIU Yining, GAO Manman, DU Liping, MA Lijuan, ZHANG Huiling, TIAN Xiaoju, YANG Weiming
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Hayati Journal of Biosciences, 2023 The antibacterial agent can be extracted from plants, animals, and microorganisms such as fungi. The potential antibacterial activity of laccase derived from fungi remains limited in current reports.
Sita Heris Anita +6 more
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Laccase Activation in Deep Eutectic Solvents [PDF]
ACS Sustainable Chemistry & Engineering, 2019 The research on alternative solvents and cosolvents is relevant when envisioning the improvement of biocatalytic reactions.
Mariah L. Toledo +5 more
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PEGylation Greatly Enhances Laccase Polymerase Activity [PDF]
ChemCatChem, 2017 AbstractLaccase catalyzes the oxidation and polymerization of phenolic compounds in the presence of oxygen. Herein, we report for the first time that a previous PEGylation of laccase enhances the polymerase activity 3‐fold compared with the reaction of the native enzyme, as confirmed by UV/Vis spectroscopy. The polymerization of catechol increased only
Jing Su +8 more
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BMC Biotechnology, 2021 Background Although laccase has a good catalytic oxidation ability, free laccase shows a poor stability. Enzyme immobilization is a common method to improve enzyme stability and endow the enzyme with reusability.
Zhaobo Wang +7 more
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Journal of Fungi, 2023 Phlebia radiata is a widespread white-rot basidiomycete fungus with significance in diverse biotechnological applications due to its ability to degrade aromatic compounds, xenobiotics, and lignin using an assortment of oxidative enzymes including laccase.
Matthew P. Hirakawa +7 more
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Frontiers in Microbiology, 2021 Enzymatic biocathodes have the potential to replace platinum as an expensive catalyst for the oxygen reduction reaction in microbial fuel cells (MFCs). However, enzymes are fragile and prone to loss of activity with time.
Priyadharshini Mani +4 more
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Laccase immobilized on magnetic nanoparticles by dopamine polymerization for 4-chlorophenol removal
Green Energy & Environment, 2017 In this work, a new immobilization method based on dopamine (DA) self-polymerization was developed for laccase immobilization on magnetic nanoparticles (Fe3O4 NPs).
Di Zhang +4 more
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Testing for the ability to modify antibiotics of Panus tigrinus 8/18 Lentinus strigosus 1566 laccase [PDF]
Brazilian Journal of Biology, 2022 In advanced biotechnology, the utilization of enzymes to achieve new or modified compounds with antibacterial, fungicidal, and anti-cancer specifications is crucial.
U. A. Krut +4 more
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