ArticleProtein science : a publication of the Protein Society2022
Bioplastic degradation by a polyhydroxybutyrate depolymerase from a thermophilic soil bacterium.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Microbial synthesis and degradation of bio-based biodegradable plastics.Nature reviews. Microbiology · 2026Review
- Trylons: Polyamide Surrogate Substrates Enable High-Throughput Screening of Nylon-Degrading Enzymes.Chembiochem : a European journal of chemical biology · 2026Article
- A multidomain hydrolase from the thermophile Thermanaeromonas toyohensis degrades high molecular mass forms of polyhydroxybutyrate.Protein science : a publication of the Protein Society · 2025Article
- Identification and structural characterization of a novel acetyl xylan esterase from Aspergillus oryzae.The FEBS journal · 2025Article
- The familyFrontiers in microbiology · 2025Review
- Biodegradation of polyhydroxyalkanoates: current state and future prospects.Frontiers in microbiology · 2025Review
- Structure and stability of an apo thermophilic esterase that hydrolyzes polyhydroxybutyrate.Acta crystallographica. Section D, Structural biology · 2024Article
- Insights into the biodegradation of polyhydroxyalkanoates by the tropical marine isolate,3 Biotech · 2024Article
- Autophagic Regulation of Adipogenesis Through TP53INP2: Insights from In Silico and In Vitro Analysis.Molecular biotechnology · 2024Article
- Purification and characterization of extracellular PHB depolymerase enzyme from Aeromonas caviae Kuk1-(34) and their biodegradation studies with polymer films.Biodegradation · 2024Article
- Bioplastic degradation by a polyhydroxybutyrate depolymerase from a thermophilic soil bacterium.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As the epidemic of single-use plastic worsens, it has become critical to identify fully renewable plastics such as those that can be degraded using enzymes. Here we describe the structure and biochemistry of an alkaline poly[(R)-3-hydroxybutyric acid] (PHB) depolymerase from the soil thermophile Lihuaxuella thermophila. Like other PHB depolymerases or PHBases, the Lihuaxuella enzyme is active against several different polyhydroxyalkanoates, including homo- and heteropolymers, but L. thermophila PHB depolymerase (LtPHBase) is unique in that it also hydrolyzes polylactic acid and polycaprolactone. LtPHBase exhibits optimal activity at 70°C, and retains 88% of activity upon incubation at 65°C for 3 days. The 1.2 Å resolution crystal structure reveals an α/β-hydrolase fold typical of PHBases, but with a shallow active site containing the catalytic Ser-His-Asp-triad that appears poised for broad substrate specificity. LtPHBase holds promise for the depolymerization of PHB and related bioplastics at high temperature, as would be required in bioindustrial operations like recycling or landfill management.
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