[HTML][HTML] Biocatalysis with laccases: An updated overview
Laccases are multicopper oxidases, which have been widely investigated in recent decades
thanks to their ability to oxidize organic substrates to the corresponding radicals while …
thanks to their ability to oxidize organic substrates to the corresponding radicals while …
Structure–function relationship among bacterial, fungal and plant laccases
Laccases (benzenediol: oxygen oxidoreductase; EC 1.10. 3.2), a multicopper oxidase
enzyme, widely distributed in plants, fungi and bacteria have ability to catalyze oxidation of …
enzyme, widely distributed in plants, fungi and bacteria have ability to catalyze oxidation of …
Laccase and laccase‐mediated systems in the synthesis of organic compounds
M Mogharabi, MA Faramarzi - Advanced Synthesis & Catalysis, 2014 - Wiley Online Library
Laccase, a blue multicopper oxidase, has recently received considerable attention because
of its usefulness in oxidizing phenolic and non‐phenolic compounds, as well as its suitability …
of its usefulness in oxidizing phenolic and non‐phenolic compounds, as well as its suitability …
Potential applications of laccase-mediated coupling and grafting reactions: a review
Many industries are currently pursuing enzymatic approaches for developing green
chemistry technologies mainly due to shortcomings of physico-chemical methods, growing …
chemistry technologies mainly due to shortcomings of physico-chemical methods, growing …
Laccase catalysis for the synthesis of bioactive compounds
T Kudanga, B Nemadziva, M Le Roes-Hill - Applied Microbiology and …, 2017 - Springer
The demand for compounds of therapeutic value is increasing mainly because of new
applications of bioactive compounds in medicine, pharmaceutical, agricultural, and food …
applications of bioactive compounds in medicine, pharmaceutical, agricultural, and food …
Fungal laccases as tools for the synthesis of new hybrid molecules and biomaterials
A Mikolasch, F Schauer - Applied microbiology and biotechnology, 2009 - Springer
Laccase is a ligninolytic enzyme widely distributed in wood-rotting fungi and which is also
found in a variety of molds and insects as well as some plants and bacteria. Its biological …
found in a variety of molds and insects as well as some plants and bacteria. Its biological …
Functional metagenomic strategies for the discovery of novel enzymes and biosurfactants with biotechnological applications from marine ecosystems
Marine ecosystems are home to bacteria which are exposed to a wide variety of
environmental conditions, such as extremes in temperature, salinity, nutrient availability and …
environmental conditions, such as extremes in temperature, salinity, nutrient availability and …
Insights into laccase producing organisms, fermentation states, purification strategies, and biotechnological applications
H Forootanfar, MA Faramarzi - Biotechnology progress, 2015 - Wiley Online Library
Laccases are phenol oxidases belonging to the superfamily of multicopper oxidases and are
found in bacteria, fungi, lichens, higher plants, and insects. Over the past few decades …
found in bacteria, fungi, lichens, higher plants, and insects. Over the past few decades …
Tandem Rh (III)-catalyzed oxidative acylation of secondary benzamides with aldehydes and intramolecular cyclization: The direct synthesis of 3-hydroxyisoindolin-1 …
The rhodium-catalyzed oxidative acylation between secondary benzamides and aryl
aldehydes via sp2 C–H bond activation followed by an intramolecular cyclization is …
aldehydes via sp2 C–H bond activation followed by an intramolecular cyclization is …
[HTML][HTML] From discovery to production: biotechnology of marine fungi for the production of new antibiotics
J Silber, A Kramer, A Labes, D Tasdemir - Marine drugs, 2016 - mdpi.com
Filamentous fungi are well known for their capability of producing antibiotic natural products.
Recent studies have demonstrated the potential of antimicrobials with vast chemodiversity …
Recent studies have demonstrated the potential of antimicrobials with vast chemodiversity …