Production and characterization of tyrosinase activity in Pycnoporus sanguineus CCT-4518 crude extract

Brazilian Journal of Microbiology

Lívia Teixeira Duarte¹  Joyce Batista Tiba¹  Mariângela Fontes Santiago¹  Telma Alves Garcia¹  Maria Teresa Freitas Bara¹ 

[1] ,Universidade Federal de Goiás Faculdade de Farmácia Goiânia GO ,Brasil

关键词: Pycnoporus sanguineus;    white-rot fungi;    tyrosinase;    MBTH;    biotechnology;   

DOI  :  10.1590/S1517-83822012000100003

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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