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Appl Environ Microbiol. 1994 February; 60(2): 569-575
Copyright © 1994, American Society for Microbiology. All Rights Reserved.

Secretion of Ligninolytic Enzymes and Mineralization of ¹⁴C-Ring-Labelled Synthetic Lignin by Three Phlebia tremellosa Strains

¹ Division of Microbiology, Department of Applied Chemistry and Microbiology, FIN 00014 University of Helsinki, Finland

ABSTRACT

Production of ligninolytic enzymes by three strains of the white rot fungus Phlebia tremellosa (syn. Merulius tremellosus) was studied in bioreactor cultivation under nitrogen-limiting conditions. The Mn(II) concentration of the growth medium strongly affected the secretion patterns of lignin peroxidase and laccase. Two major lignin peroxidase isoenzymes were expressed in all strains. In addition, laccase and glyoxal oxidase were purified and characterized in one strain of P. tremellosa. In contrast, manganese peroxidase was not found in fast protein liquid chromatography profiles of extracellular proteins under either low (2.4 µM) or elevated (24 and 120 µM) Mn(II) concentrations. However, H₂O₂- and Mn-dependent phenol red-oxidizing activity was detected in cultures supplemented with higher Mn(II) levels. Mineralization rates of ¹⁴C-ring-labelled synthetic lignin (i.e., dehydrogenation polymerizate) by all strains under a low basal Mn(II) level were similar to those obtained for Phanerochaete chrysosporium and Phlebia radiata. A high manganese concentration repressed the evolution of ¹⁴CO₂ even when a chelating agent, sodium malonate, was included in the medium.

^* Corresponding author. Mailing address: Division of Microbiology, Department of Applied Chemistry and Microbiology, P.O. Box 27, FIN-00014 University of Helsinki, Finland. Phone: 358-0-7085279. Fax: 358-0-7085212. Electronic mail address (Internet): AHATAKKA@VIIKKI.HELSINKI.FI.

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