Polyphenol oxidases exhibit promiscuous proteolytic activity
Antonino Biundo, Verena Braunschmid, Matthias Pretzler, Ioannis Kampatsikas, Barbara Darnhofer, Ruth Birner‐Gruenberger, Annette Rompel, Doris Ribitsch, Georg M. Guebitz
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.