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Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus
Author(s) -
Papinutti Leandro,
Martínez María J
Publication year - 2006
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.1537
Subject(s) - laccase , manganese peroxidase , abts , peroxidase , chemistry , molecular mass , fomes , isozyme , enzyme , biochemistry , nuclear chemistry , botany , biology , antioxidant , dpph
Fomes sclerodermeus was grown on semi‐defined media based on yeast extract, peptone and glucose (YPG). The fungus produced a minimum basal level of laccase activity irrespective of culture medium. The highest laccase production (20 U cm −3 ) was obtained in cultures supplemented with CuSO 4 . Manganese peroxidase (MnP) could only be detected when MnSO 4 was added to the medium. None of the aromatic compounds tested stimulated further laccase or MnP production. Laccase and MnP stimulated by Cu 2+ or Mn 2+ respectively were purified. Two different laccase isoenzymes with the same molecular mass (67 kDa) and N‐linked carbohydrate content (3%) and a slight difference in their p I values (3.41 and 3.48) were characterized. In addition, two different MnP isoenzymes with the same molecular mass (47 kDa) and N‐linked carbohydrate content (4%) and different p I values (3.35 and 3.45) were characterized. Both enzymes showed good stability at 25 °C and over a wide range of pH. Both laccases oxidize ABTS (2,2′‐azino‐bis(3‐ethylbenzthiazoline‐6‐sulfonic acid) more efficiently than 2,6‐dimethoxyphenol (DMP) with similar efficiency values ( K cat / K m ) while the MnP I, the major peroxidase isoenzyme in the studied conditions, oxidizes the Mn 2+ and Mn‐mediated activity on DMP more efficiently than MnP II. Copyright © 2006 Society of Chemical Industry