| Title : Efficient biodegradation of poly(butylene adipate-co-terephthalate) in mild temperature by cutinases derived from a marine fungus - Fei_2024_J.Hazard.Mater_480_136008 |
| Author(s) : Fei F , Su Z , Liu R , Gao R , Sun C |
| Ref : J Hazard Mater , 480 :136008 , 2024 |
|
Abstract :
Poly(butylene adipate-co-terephthalate) (PBAT) waste gradually accumulates in the environment, posing ecological risks. Enzymatic hydrolysis holds great potential in the end-of-life management of PBAT, but reported enzymes require high reaction temperatures, limiting their practical industrial applications. In this study, we discovered that the marine fungus Alternaria alternata FB1 can efficiently degrade PBAT at 28 degreesC. Two cutinases designated as AaCut4 and AaCut10, were identified and verified as key enzymes responsible for this degradation process. Notably, the recombinant AaCut10 was able to depolymerize 82.14 % PBAT within 24 h and fully decompose it within 48 h at 37 degreesC. Through protein engineering, the yield of terephthalic acid monomer was increased to 96.01 %, highlighting its potential for facilitating PBAT upcycling. Furthermore, based on the investigation of the distribution patterns of PBAT hydrolases, novel degradative agents have been identified within unique ecological niches, leading to the establishment of a comprehensive screening repository of PBAT hydrolases. Overall, our study provides new candidates for enzymatic PBAT recycling with low energy consumption and offers insights into the PBAT degradation manner in ecosystems. |
| PubMedSearch : Fei_2024_J.Hazard.Mater_480_136008 |
| PubMedID: 39368353 |
| Gene_locus related to this paper: altal-Aacut4 , altal-Aacut10 |
| Substrate | PBAT |
| Gene_locus | altal-Aacut4 altal-Aacut10 |
Fei F, Su Z, Liu R, Gao R, Sun C (2024)
Efficient biodegradation of poly(butylene adipate-co-terephthalate) in mild temperature by cutinases derived from a marine fungus
J Hazard Mater
480 :136008
Fei F, Su Z, Liu R, Gao R, Sun C (2024)
J Hazard Mater
480 :136008