Production and Characterization of Tyrosinase Activity in Pycnoporus sanguineus CCT-4518 Crude Extract

Author: mycolabadmin
2012-06-01
View Source

Summary

This research focused on producing and studying an important enzyme called tyrosinase from an Amazonian fungus. This enzyme has significant industrial applications and potential environmental benefits. Here’s how this research impacts everyday life: • Could lead to more effective treatment of wastewater containing harmful chemicals and dyes • May improve food processing techniques through better protein cross-linking methods • Could enhance the production of certain pharmaceutical compounds • Offers potential for developing new biosensors for environmental monitoring • Could contribute to more environmentally friendly industrial processes

Background

Tyrosinase is an enzyme that catalyzes the o-hydroxylation of monophenols and oxidation of o-diphenols to reactive o-quinones using molecular oxygen. In fungi, tyrosinases are associated with melanin production, which provides defense against environmental stresses and contributes to cell wall resistance. The enzyme has various biotechnological applications including wastewater treatment, drug synthesis, and protein cross-linking in food technology.

Objective

To investigate and optimize the production conditions of tyrosinase from Pycnoporus sanguineus CCT-4518, an Amazonian fungal strain, and characterize the enzyme’s properties. This included studying the effects of inductors, luminosity, inoculum size, culture medium conditions, and enzyme inhibitors on tyrosinase production and activity.

Results

Optimal conditions for intracellular tyrosinase production were achieved after 2 days using 0.15% L-tyrosine as inducer, with light presence, 10 mycelium discs as inoculum, in 2% malt extract broth medium at 30°C with 150 rpm agitation. The enzyme showed optimal activity at pH 6.6 and 45°C. Tyrosinase activity was completely inhibited by 6 mM salicylhydroxamic acid or phenylthiourea, while showing minimal inhibition by sodium azide. The enzyme remained stable at 45°C for 15 minutes but lost activity at higher temperatures.

Conclusion

P. sanguineus CCT-4518 produces one intracellular protein with tyrosinase activity when induced with L-tyrosine under specific cultivation conditions. The enzyme shows distinct characteristics in terms of optimal pH, temperature, and stability compared to other known fungal tyrosinases. Further research is needed to investigate its potential applications in biotransformation, bioremediation, and biosensor development.

Published in:Brazilian Journal of Microbiology,
Study Type:Laboratory Research,
Source: 10.1590/S1517-83822012000100003