Litcius/Paper detail

Halopseudomonas sp. MFKK-1: A marine-derived bacterium capable of degrading poly(butylene succinate-co-adipate), poly(ε-caprolactone), and poly(butylene adipate-co-terephthalate) in marine ecosystems

Phouvilay Soulenthone, Miwa Suzuki, Yuya Tachibana, Maya Furukori, Taijiro Saito, Rina Kawamura, Paul Olusegun Bankole, Ken‐ichi Kasuya

2024Polymer Degradation and Stability11 citationsDOIOpen Access PDF

Abstract

• Halopseudomonas sp. MFKK-1 degrades polymers PBSA, PCL, and PBAT. • MFKK-1 utilizes 1,4-butanediol and adipate, monomeric components of PBSA, for growth. • Polymer degrading gene, aph Hsp , encoding a polyester hydrolase APH Hsp , was identified. • APH Hsp is a mesophilic enzyme with a catalytic triad of Ser 171 , Asp 217 , and His 249 . • APH Hsp degrades PBSA, PCL, and PBAT films in the presence of 0.5 m NaCl. Aliphatic and aliphatic-aromatic polyesters are potentially biodegradable polymers that have garnered attention as promising solutions to plastic waste menace, particularly in marine environments. Among these, poly(butylene succinate- co -adipate) (PBSA), which has polyethylene-like properties, is used as biodegradable packaging and mulch film. However, the slow degradation of PBSA in marine environments presents a challenge. We isolated a polyester-degrading bacterium, MFKK-1, from seawater collected from a quay and investigated its PBSA degradation potential in the marine environment. The isolate, identified as a member of the genus Halopseudomonas, demonstrated PBSA degradation potential at the salinity levels of seawater. In addition to PBSA, the strain could degrade poly( ε -caprolactone) (PCL) and the aliphatic-aromatic polyester poly(butylene adipate- co -terephthalate) (PBAT). The strain used 1,4-butanediol and adipate, monomeric components of PBSA, as carbon sources for growth. Moreover, the gene aph Hsp , responsible for the degradation of polyesters, was heterologously expressed in Escherichia coli . The purified recombinant APH Hsp was characterized. This enzyme belongs to the α/β hydrolase family, with a catalytic triad composed of Ser 171 , Asp 217 , and His 249 . It is a mesophilic enzyme that has shown the ability to degrade PBSA, PCL, and PBAT films in buffer supplemented with 0.5 M NaCl, a salinity comparable to that of seawater. Furthermore, the enzyme degraded amorphous poly(ethylene terephthalate) under 0.5 M NaCl conditions. The findings of this study enhance our knowledge of the microbial degradation of polyesters in marine environments, potentially supporting the sustainable application of biodegradable materials in ocean ecosystems.

Topics & Concepts

AdipatePolybutylene succinateCaprolactonePolymer chemistryChemistryMaterials scienceOrganic chemistryPolymerPolymerizationbiodegradable polymer synthesis and propertiesMicroplastics and Plastic PollutionBiopolymer Synthesis and Applications