Bioinformatics-guided discovery and functional verification of fungal polyester hydrolases for polycaprolactone degradation
- 1Ames High School, 1801 Ridgewood Ave., Ames, United States
- 2Interdepartmental Microbiology Program, Iowa State University, 1071b Lebaron, 626 Morrill Rd., Ames, United States; Department of Apparel, Events, and Hospitality Management, Iowa State University, 1071b Lebaron, 626 Morrill Rd., Ames, United States; Corresponding author.
Abstract
Polycaprolactone (PCL) is a biodegradable polyester that can degrade slowly under ambient environmental conditions. Here, we explored natural fungal sequence diversity to identify cutinase-like enzymes (CLEs) with PCL-degrading activity. Using a previously reported Cryptococcus CLE as the query, bioinformatics analysis identified 14 fungal homologs that were subsequently expressed in the heterologous host Saccharomyces cerevisiae and screened using a plate-based assay. Nine homologs exhibited detectable PCL degradation, with three producing larger degradation zones than the Cryptococcus reference enzyme. These three homologs exhibited distinct apparent optimal temperatures of 30°C, 37°C, and 40°C, compared with 45°C for the reference enzyme under the tested conditions. Signal peptide replacement and GFP-based analyses suggested that native signal peptide recognition alone was unlikely to account for the five inactive homologs. Collectively, this study provides a practical bioinformatics-to-experiment strategy for screening natural enzyme diversity and prioritizing promising candidates for further biochemical characterization.
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BibTeX
@article{lu2026bioinformaticsguided,
title = {{Bioinformatics-guided discovery and functional verification of fungal polyester hydrolases for polycaprolactone degradation}},
author = {Claire Lu and Chloe Lu and Chunhui Xiang},
journal = {Biotechnology Reports},
year = {2026},
month = oct,
doi = {10.1016/j.btre.2026.e00985},
url = {https://doi.org/10.1016/j.btre.2026.e00985},
note = {CC BY-NC-ND},
}
RIS
TY - JOUR
TI - Bioinformatics-guided discovery and functional verification of fungal polyester hydrolases for polycaprolactone degradation
AU - Claire Lu
AU - Chloe Lu
AU - Chunhui Xiang
PY - 2026
DA - 2026/10/13
JO - Biotechnology Reports
DO - 10.1016/j.btre.2026.e00985
UR - https://doi.org/10.1016/j.btre.2026.e00985
AB - Polycaprolactone (PCL) is a biodegradable polyester that can degrade slowly under ambient environmental conditions. Here, we explored natural fungal sequence diversity to identify cutinase-like enzymes (CLEs) with PCL-degrading activity. Using a previously reported Cryptococcus CLE as the query, bioinformatics analysis identified 14 fungal homologs that were subsequently expressed in the heterologous host Saccharomyces cerevisiae and screened using a plate-based assay. Nine homologs exhibited detectable PCL degradation, with three producing larger degradation zones than the Cryptococcus reference enzyme. These three homologs exhibited distinct apparent optimal temperatures of 30°C, 37°C, and 40°C, compared with 45°C for the reference enzyme under the tested conditions. Signal peptide replacement and GFP-based analyses suggested that native signal peptide recognition alone was unlikely to account for the five inactive homologs. Collectively, this study provides a practical bioinformatics-to-experiment strategy for screening natural enzyme diversity and prioritizing promising candidates for further biochemical characterization.
SN - 2215-017X
ER -