Abstract
SUMMARYThe aim of this research is to isolate and identify fungi with high lignin-degrading abilities that are autochthonous to southern Serbian region. Two novel fungal isolates identified as Trametes hirsuta F13 and Stereum gausapatum F28 were selected to assess their ligninolytic enzyme activities and the efficiency of lignin removal from beech wood sawdust. Obtained results show that both isolates are good sources of industrially valuable enzymes with a potential for application in various biotechnological and industrial processes. Both isolates showed laccase, manganese-dependent peroxidase, and versatile peroxidase activities, while only S. gausapatum F28 had lignin peroxidase activity. This is the first record of the ability of S. gausapatum species to produce lignin peroxidase. T. hirsuta F13 showed higher laccase activity than S. gausapatum F28, while S. gausapatum F28 had higher manganese peroxidase activity. Also, T. hirsuta F13 exhibited much higher laccase activity under submerged cultivation conditions than solid-state cultivation conditions, which is rare for fungi. This is important for industrial processes since the submerged fermentation is a dominant technique in industry. The test of the efficiency of lignin removal showed that both isolates are efficient lignin decomposers. After five weeks of incubation on beech wood sawdust, the total lignin losses were 33.84% with T. hirsuta F13 and 28.8% with S. gausapatum F28.
Highlights
During the course of evolution, fungi have developed mechanisms to access energy incorporated in recalcitrant plant biomass in the form of polysaccharides
LMS gave significantly higher enzyme activities (p
We examined two novel fungal isolates able to efficiently degrade lignin
Summary
During the course of evolution, fungi have developed mechanisms to access energy incorporated in recalcitrant plant biomass in the form of polysaccharides. These mechanisms are based on the activity of various enzymes capable of breaking inter- and intrapolymer bonds of the lignocellulosic substrate, releasing fermentable sugars. According to the type of enzymatic activity required for a bond cleavage, lignocellulose-degrading mechanisms form two groups: hydrolytic and oxidative. Hydrolytic enzymes (cellulase and hemicellulases) break glycosidic bonds (β-1,4-, β-1,3-, β-1,2- and β-1,6-) that connect subunits of lignocellulose polysaccharides. Lignin subunits are mainly linked by ether-like or carbon-carbon bonds that cannot be hydrolyzed [1]. Its degradation occurs through oxidative processes catalyzed by fungal enzymes which include: manganese-dependent peroxidase (MnP, EC 1.11.1.13), lignin peroxidase (LiP, EC 1.11.1.14), versatile peroxidase (VP, manganese-independent peroxidase, EC 1.11.1.16) and laccase (benzenediol:oxygen oxidoreductase, EC 1.10.3.2) [2]
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