<div class="csl-bib-body">
<div class="csl-entry">Biundo, A., Braunschmid, V., Pretzler, M., Kampatsikas, I., Darnhofer, B., Birner-Grünberger, R., Rompel, A., Ribitsch, D., & Guebitz, G. (2020). Polyphenol oxidases exhibit promiscuous proteolytic activity. <i>Communications Chemistry</i>, <i>3</i>(62). https://doi.org/10.1038/s42004-020-0305-2</div>
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dc.identifier.issn
2399-3669
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/141409
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dc.description.abstract
Tyrosinases catalyse both the cresolase and catecholase reactions for the formation of
reactive compounds which are very important for industrial applications. In this study, we
describe a proteolytic activity of tyrosinases. Two different tyrosinases originating from
mushroom and apple are able to cleave the carboxylesterase EstA. The cleavage reaction
correlates with the integrity of the active site of tyrosinase and is independent of other
possible influencing factors, which could be present in the reaction. Therefore, the cleavage of
EstA represents a novel functionality of tyrosinases. EstA was previously reported to degrade
synthetic polyesters, albeit slowly. However, the EstA truncated by tyrosinase shows higher
degradation activity on the non-biodegradable polyester polyethylene terephthalate (PET),
which is a well-established environmental threat.
