Please use this identifier to cite or link to this item: https://biore.bio.bg.ac.rs/handle/123456789/5851
Title: Screening of the laccase, manganese peroxidase, and versatile peroxidase activities of the genus Pleurotus in media with some raw plant materials as carbon sources
Authors: Stajić, Mirjana 
Persky, Limor
Cohen, Emanuel
Hadar, Yitzhak
Brceski, Ilija
Wasser, Solomon P.
Nevo, Eviatar
Issue Date: Jun-2004
Rank: M23
Publisher: MDPI
Journal: Applied Biochemistry and Biotechnology
Volume: 117
Issue: 3
Start page: 155
End page: 164
Abstract: 
Species of the genus Pleurotus are among the most efficient natural species in lignin degradation belonging to the subclass of ligninolytic organisms that produce laccase (Lac), Mn-dependent peroxidase (MnP), versatile peroxidase (VP), and the H2O2-generating enzyme aryl-alcohol oxidase, but not lignin peroxidases. Production of Lac and oxidation of 2,6-dimethoxyphenol (DMP) in the presence and absence of Mn2+ were detected both in submerged fermentation (SF) of dry ground mandarine peels and in solid-state fermentation (SSF) of grapevine sawdust in all investigated Pleurotus species and strains. Evidence of cultivation methods having a distinct influence on the level of enzyme activities has been demonstrated. Most of the species and strains had higher Lac activity under SSF conditions than under SF conditions. DMP oxidation in the presence and absence of Mn2+ was detected in all investigated species and strains, but was lower under SF conditions than under SSF conditions for most of them. However, relative activities of DMP oxidation in the absence of Mn2+, as percentages of activity against DMP in the presence of Mn2+, were higher under conditions of SF than in SSF cultures in most of the investigated species and strains. The obtained results showed that strains of different origins have different efficiently ligninolytic systems and that conditions of SSF are more favorable for ligninolytic activity than those in SF owing to their similarity to natural conditions on wood substrates.
URI: https://biore.bio.bg.ac.rs/handle/123456789/5851
ISSN: 0273-2289
DOI: 10.1385/abab:117:3:155
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