Production and characterization of tyrosinase activity in Pcnoporus sanguineus CCT-4518 crude extract
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Data
2012
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Resumo
Tyrosinase is an enzyme of industrial interest. The production and characterization of tyrosinase from P.
sanguineus CCT-4518 were investigated. The selection of inductors, luminosity influence, inoculum size
and type of culture medium on the production of tyrosinase and the effect of inhibitors on enzyme activity
were performed. Optimum conditions for intracellular tyrosinase production was observed after 2 days using
0.15% L-tyrosine as inducer, in the presence of light, with inoculum size of 10 mycelium discs, using 2%
malt extract broth medium, incubated at 30°C, and constant agitation of 150 rpm. Tyrosinase activity was
completely inhibited by the addition of 6 mM salicylhydroxamic acid or phenylthiourea, however an
inhibition of 4.15% was recorded by the addition of 0.1 mM sodium azide. No inhibition could be detected
in case of 0.1 mM phenyl methanesulfonyl fluoride addition. Optimal conditions for intracellular tyrosinase
activity using L-dopa as substrate were observed at pH 6.6 and 45°C. Thermal stability studies indicated that
the enzyme is stable at 45°C for 15 minutes. Higher temperatures decreased tyrosinase activity. Enzyme
production was confirmed by non-denaturing polyacrylamide gel electrophoresis and the protein profile was
investigated by denaturing polyacrylamide gel electrophoresis.
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Pycnoporus sanguineus, White-rot fungi, Tyrosinase, Biotechnology, MBTH
Citação
Duarte, Lívia Teixeira; TIBA, Joyce Batista; SANTIAGO, Mariangela Fontes; GARCIA, Telma Alves; BARA, Maria Teresa Freitas. Production and characterization of tyrosinase activity in Pcnoporus sanguineus CCT-4518 crude extract. Brazilian Journal of Microbiology, São Paulo, v. 43, p. 21-29, 2012.