Please use this identifier to cite or link to this item: https://biore.bio.bg.ac.rs/handle/123456789/2170
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dc.contributor.authorĆilerdžić, Jasminaen_US
dc.contributor.authorStajić, Mirjanaen_US
dc.contributor.authorVukojević, Jelenaen_US
dc.contributor.authorDuletić Laušević, Sonjaen_US
dc.contributor.authorKnežević, Aleksandaren_US
dc.date.accessioned2019-10-22T14:39:49Z-
dc.date.available2019-10-22T14:39:49Z-
dc.date.issued2011-06-15-
dc.identifier.urihttps://biore.bio.bg.ac.rs/handle/123456789/2170-
dc.description.abstractTrametes hirsuta is an efficient lignin-degrading species due to its ability to produce laccase and Mn-dependent peroxidase. Agricultural residues represent prospective substrates for the bioconversion into fungal biomass and lignocellulolytic enzymes, but also they could be potential environmental pollutants. Evaluation of the potential of T. hirsuta to produce ligninolytic enzymes during solid-state fermentation of selected plant raw materials was the goal of the study. The highest level of laccase activity (3827.0 ± 219.0 U/L) was noted in mandarin orange peels medium, while wheat straw and glucose-enriched mandarin orange peels media were the optimum for Mn-dependent peroxidase (1971.5 ± 23.0 U/L) and versatile peroxidase (1173.0 ± 100.0 U/L), respectively. Levels of veratryl alcohol oxidation in the presence of H2O2 were similar to those in its absence during fermentation of all selected agricultural residues, and the highest values were obtained in glucose-enriched mandarin orange peels medium. The obtained results demonstrated the potential of T. hirsuta to produce ligninolytic enzymes and mineralize various plant wastes to low-molecular weight compounds that could be further used in food, feed, and other industries.en_US
dc.language.isoenen_US
dc.relation.ispartofBioresourcesen_US
dc.subjectAgricultural wastesen_US
dc.subjectLaccaseen_US
dc.subjectMn-oxidizing peroxidasesen_US
dc.subjectTrametes hirsutaen_US
dc.subjectVeratryl alcohol oxidation.en_US
dc.titlePotential of Trametes hirsuta to produce ligninolytic enzymes during degradation of agricultural residuesen_US
dc.typeArticleen_US
dc.identifier.doi10.15376/biores.6.3.2885-2895-
dc.description.rankM21en_US
dc.description.impact1.691en_US
dc.description.startpage2855en_US
dc.description.endpage2895en_US
dc.description.volume6en_US
dc.description.issue3en_US
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.openairetypeArticle-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
crisitem.author.deptChair of Algology, Mycology and Lichenology-
crisitem.author.deptChair of Algology, Mycology and Lichenology-
crisitem.author.deptChair of Algology, Mycology and Lichenology-
crisitem.author.deptChair of Plant Morphology and Systematics-
crisitem.author.deptChair of Algology, Mycology and Lichenology-
crisitem.author.orcid0000-0001-6273-6409-
crisitem.author.orcid0000-0003-3781-246x-
crisitem.author.orcid0000-0002-6396-9789-
crisitem.author.orcid0000-0002-4777-3989-
crisitem.author.orcid0000-0002-2776-9675-
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