Basidiomycetes laccase and manganese peroxidase activity in submerged fermentation of food industry wastes

The evaluation of eighteen strains of basidiomycetes laccase and manganese peroxidase (MnP) activity in submerged fermentation of mandarin peelings and ethanol production waste showed that the expression of enzyme activity is species- and strain-dependent. While all species of the genus Trametes expressed comparatively high laccase activity, the activity of this enzyme among species of the genus Ganoderma varied from 192 to 61,488 U l^-1. Phellinus robustus 250 appeared to be a promising producer of MnP, accumulating more than 4000 U l^-1 of enzyme activity. It has been shown for the first time that Omphalotus olearius 174 is capable of producing high levels of laccase and MnP, while Hypsizygus marmoreus produces only laccase. Laccase and MnP production proved to be very much dependent on the lignocellulosic growth substrate. Of eight complex substrates examined in submerged fermentation by Ganoderma lucidum 447, wheat bran and soy bran gave the highest laccase activity with a maximum value of 93-97 U ml^-1. Proof that both the titre and time of maximal enzyme activity are influenced by nutrient nitrogen is presented.