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
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.