2002
DOI: 10.1016/s0141-0229(02)00021-2
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Production of lignin modifying enzymes by co-cultivated White-rot fungi Cerrena maxima and Coriolus hirsutus and characterization of laccase from Cerrena maxima

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Cited by 53 publications
(21 citation statements)
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“…Fungal laccases are secreted into the medium by the mycelium of filamentous fungi (Couto and Toca-Herrera 2007). Examples of microorganisms that produce laccase with high activity are Trametes pubescens (740,000 U/L) (Galhaup et al 2002), Coriolus hirsutus (83,830 U/L) (Koroleva et al 2002), Trametes hirsuta (19,400 U/L) (Rodríguez- Couto et al 2006), T. versicolor (16,000 U/L) (Font et al 2003), Pycnoporus cinnabarinus (10,000 U/L) (Meza et al 2006), Neurospora crassa (10,000 U/L) (Luke and Burton 2001), Pleurotus ostreatus (3,500 U/L) (Lenz and Hölker 2004). P. ostreatus belongs to a class of white-rot fungi that produces laccases, manganese peroxidases but not lignin peroxidases (Giardina et al 2000).…”
Section: Ligninolytic Enzymesmentioning
confidence: 99%
“…Fungal laccases are secreted into the medium by the mycelium of filamentous fungi (Couto and Toca-Herrera 2007). Examples of microorganisms that produce laccase with high activity are Trametes pubescens (740,000 U/L) (Galhaup et al 2002), Coriolus hirsutus (83,830 U/L) (Koroleva et al 2002), Trametes hirsuta (19,400 U/L) (Rodríguez- Couto et al 2006), T. versicolor (16,000 U/L) (Font et al 2003), Pycnoporus cinnabarinus (10,000 U/L) (Meza et al 2006), Neurospora crassa (10,000 U/L) (Luke and Burton 2001), Pleurotus ostreatus (3,500 U/L) (Lenz and Hölker 2004). P. ostreatus belongs to a class of white-rot fungi that produces laccases, manganese peroxidases but not lignin peroxidases (Giardina et al 2000).…”
Section: Ligninolytic Enzymesmentioning
confidence: 99%
“…For the biocathode construction, fungal Cerrena maxima (C. maxima) laccase with improved (thermo)stability and activity properties (tolerance towards chloride anions) as compared to the hitherto studied fungal laccases have been used [26,27]. C. maxima laccase is an extracellular 57 kDa acidic enzyme (pI 3.5), a monomer that provides the 4e À electroreduction of O 2 to H 2 O and retains 90-95% of its maximal activity at pH 3-5 [27].…”
Section: Introductionmentioning
confidence: 99%
“…C. maxima laccase is an extracellular 57 kDa acidic enzyme (pI 3.5), a monomer that provides the 4e À electroreduction of O 2 to H 2 O and retains 90-95% of its maximal activity at pH 3-5 [27]. Like other laccases, C. maxima laccase contains the first type of prosthetic copper ion (T1), so called blue copper, which is a primary acceptor of electrons from a substrate, from which electrons are transferred to the second type (T2) and third type (T3 being a binuclear copper site) copper cluster, where transformation of O 2 to water occurs [28] (Fig.…”
Section: Introductionmentioning
confidence: 99%
“…The co-cultures appeared to be advantageous over monocultures because of the potential for synergistic interactions, but the final result mainly depended on the particular microbe's combination, interactions between species, and the micro-environmental or nutritional conditions in the substrate under colonization [15]. Koroleva et al [16] reported that the co-cultivation of C. hirsutus (laccase is the predominant enzyme) and C. maxima (MnP the key enzyme) resulted in little or no increases in the production of LMEs.…”
Section: Introductionmentioning
confidence: 99%