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Occurrence of high tyrosinase activity in the non-Peltigeralean lichen Dermatocarponminiatum (L.) W. Mann

Published online by Cambridge University Press:  08 October 2012

Richard P. BECKETT ,
Farida V. MINIBAYEVA  and
Christiane LIERS
Richard P. BECKETT
Affiliation:
School of Biological and Conservation Sciences, University of KwaZulu-Natal, Private Bag X01, Pietermaritzburg, Scottsville 3209, South Africa. Email: [email protected]
Farida V. MINIBAYEVA
Affiliation:
Kazan Institute of Biochemistry and Biophysics, Russian Academy of Sciences, P O Box 30, Kazan 420111, Russia
Christiane LIERS
Affiliation:
Department of Environmental Biotechnology, International Graduate School of Zittau, Markt 23, 02763 Zittau, Germany
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Abstract

In our earlier work, we demonstrated the presence of the multicopper oxidases tyrosinase and laccase in the cell walls of lichens from the Peltigerales, while these enzymes appeared to be absent in lichens from other orders. Likely roles for tyrosinase in lichens include melanin synthesis, the generation of quinones needed for laccase-mediated redox cycling, and the removal of harmful reactive molecules formed by this cycling. Non-Peltigeralean lichens will not need tyrosinase to detoxify laccase-generated radicals. However, many non-Peltigeralean lichens are often heavily melanized. Apparent absence of tyrosinase activity in these species prompted us to suggest that, in these lichens, melanins are probably synthesized by the polyketide pathway, which does not involve tyrosinase. Here, we surveyed intracellular tyrosinase activity in thallus homogenates from a range of lichens. Results showed that Peltigeralean species generally have much higher activities than species from other orders. However, the non-Peltigeralean lichen Dermatocarpon miniatum displays significant tyrosinase activity. In D. miniatum, tyrosinase differs from the corresponding enzyme from Peltigeralean lichens with respect to cellular location, substratum specificity, stability and pH optimum. Furthermore, unlike Peltigeralean lichens, in D. miniatum tyrosinase activity increased strongly following the rehydration of dry thalli. These differences are possibly a consequence of the role of tyrosinase in melanin synthesis rather than laccase-mediated redox cycling.

Keywords

dessicationlaccasemelaninphenol oxidasepolyketide
Type
Research Article
Information
The Lichenologist , Volume 44 , Issue 6 , November 2012 , pp. 827 - 832
Copyright
Copyright © British Lichen Society 2012

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