Identification and application of a novel patulin degrading enzyme from Cyberlindnera fabianii

Patulin (PAT) is a mycotoxin commonly found in fruits and vegetables, prompting the need for effective removal and detoxification methods, which have garnered significant research attention in recent years. Among these methods, the utilization of microbial-derived enzymes stands out due to their mild operating conditions, specificity in targeted functional groups, and the production of non-toxic by-products, making it a preferred degradation approach. In this study, a novel PAT-degrading enzyme derived from Cyberlindnera fabianii (Cyfa-SDR) was identified, demonstrating its highest catalytic activity at pH 7.0 and 80 °C against PAT. This temperature tolerance level represents the highest reported for PAT-degrading enzymes to date. The enzyme was further characterized as a short-chain dehydrogenase through analysis of its amino acid composition, conserved GXXXGXG motif, and dependency on NADPH. Moreover, the study evaluated the efficiency of PAT degradation by Cyfa-SDR at varying substrate and enzyme concentrations, surpassing the performance of other PAT-degrading enzymes, thus highlighting its substantial potential for the biological control of PAT. In conclusion, the enzymatic treatment using the PAT-degrading enzyme Cyfa-SDR presents a viable and promising solution for enhancing the quality and safety of fruit juice.