ArticleProtein science : a publication of the Protein Society2025
A multidomain hydrolase from the thermophile Thermanaeromonas toyohensis degrades high molecular mass forms of polyhydroxybutyrate.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- A multidomain hydrolase from the thermophile Thermanaeromonas toyohensis degrades high molecular mass forms of polyhydroxybutyrate.Protein science : a publication of the Protein Society · 2025Article
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6 authors.
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Abstract
The use of polyhydroxybutyrate (PHB) bioplastics has the potential to create a circular and sustainable recycling plastic system. Here, we focus on PHB degradation and characterize the multidomain PHB hydrolyzing enzyme from the extremophile Thermanaeromonas tohohensis. The catalytic domain fold is conserved across a diverse taxonomic range, but the C-terminal domains are unique amongst PHBases and instead share similarities with carbohydrate degrading enzymes from human gut microbiota. The enzyme has a preference for higher molecular weight PHB. Hydrolysis of PHB films correlates with the ability of the enzyme to bind those films, most likely driven by its C-terminal substrate binding domain. The enzyme denatures in a highly cooperative manner over a short temperature range, and the kinetics of folding/unfolding are well described by Eyring theory. Finally, the study of this enzyme has been incorporated into an undergraduate biochemistry teaching laboratory that focuses on "real life" research problems with relevance to industry.
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