NDLI: Production of recombinant Agaricus bisporus tyrosinase in Saccharomyces cerevisiae cells

Content Provider	Springer Nature Link
Author	Lezzi, Chiara Bleve, Gianluca Spaglo, Stefa Perrotta, Carla Grieco, Francesco
Copyright Year	2012
Abstract	It has been demonstrated that Agaricus bisporus tyrosinase is able to oxidize various phenolic compounds, thus being an enzyme of great importance for a number of biotechnological applications. The tyrosinase-coding PPO2 gene was isolated by reverse-transcription polymerase chain reaction (RT-PCR) using total RNA extracted from the mushroom fruit bodies as template. The gene was sequenced and cloned into pYES2 plasmid, and the resulting pY-PPO2 recombinant vector was then used to transform Saccharomyces cerevisiae cells. Native polyacrylamide gel electrophoresis followed by enzymatic activity staining with l-3,4-dihydroxyphenylalanine (l-DOPA) indicated that the recombinant tyrosinase is biologically active. The recombinant enzyme was overexpressed and biochemically characterized, showing that the catalytic constants of the recombinant tyrosinase were higher than those obtained when a commercial tyrosinase was used, for all the tested substrates. The present study describes the recombinant production of A. bisporus tyrosinase in active form. The produced enzyme has similar properties to the one produced in the native A. bisporus host, and its expression in S. cerevisiae provides good potential for protein engineering and functional studies of this important enzyme.
Starting Page	1875
Ending Page	1880
Page Count	6
File Format	PDF
ISSN	13675435
Journal	Journal of Industrial Microbiology and Biotechnology
Volume Number	39
Issue Number	12
e-ISSN	14765535
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-09-21
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Agaricus bisporus Tyrosinase Saccharomyces cerevisiae Heterologous expression Inorganic Chemistry Biotechnology Genetic Engineering Biochemistry Bioinformatics Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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