Novel Transaminase and Laccase from Streptomyces spp. Using Combined Identification Approaches

Three Streptomyces sp. strains with a multitude of target enzymatic activities confirmed by functional screening, namely BV129, BV286 and BV333, were subjected to genome sequencing aiming at the annotation genes interest, in-depth bioinformatics characterization expression biocatalysts. A whole-genome shotgun followed de novo assembly was performed revealing genomes 6.4, 9.4 7.3 Mbp, respectively. Functional proteins interest resulted in between 2047 2763 putative targets. Among various that three demonstrated produce we focused our attention on transaminases (TAs) laccases due their high biocatalytic potential. Bioinformatics search allowed identification TA from BV333 as potentially novel broad substrate scope laccase blue multicopper oxidase. The two sequences cloned overexpressed Escherichia coli enzymes, transaminase Sbv333-TA Sbv286-LAC, characterized. Interestingly, both enzymes be exceptionally thermostable, showing melting temperature (TM = 85 °C) only slightly lower compared TM most thermostable described date (87–88 Sbv286-LAC being even thermoactivated >60 °C. Moreover, showed remarkably active transamination ?-ketoesters, which are rarely accepted currently known TAs. On other hand, an improved activity presence cosolvent acetonitrile. Overall, it shown combination approaches standard microbiological biochemical screens analysis is required afford