ArticleScientific reports2022
Cellobiose phosphorylase from Caldicellulosiruptor bescii catalyzes reversible phosphorolysis via different kinetic mechanisms.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 26 citations in OpenAlex.
- A highly conserved ABC transporter mediates cello-oligosaccharide uptake in the extremely thermophilic, lignocellulolytic bacteriumApplied and environmental microbiology · 2026Article
- Integrated omics analysis of the cellulose co-degradation network of Chaetomium thermophilum.Biotechnology for biofuels and bioproducts · 2026Article
- Metabolome and transcriptome analyses reveal changes of rapeseed in response to ABA signal during early seedling development.BMC plant biology · 2024Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
In the process of yielding biofuels from cellulose degradation, traditional enzymatic hydrolysis, such as β-glucosidase catalyzing cellobiose, can barely resolve the contradiction between cellulose degradation and bioenergy conservation. However, it has been shown that cellobiose phosphorylase provides energetic advantages for cellobiose degradation through a phosphorolytic pathway, which has attracted wide attention. Here, the cellobiose phosphorylase gene from Caldicellulosiruptor bescii (CbCBP) was cloned, expressed, and purified. Analysis of the enzymatic properties and kinetic mechanisms indicated that CbCBP catalyzed reversible phosphorolysis and had good thermal stability and broad substrate selectivity. In addition, the phosphorolytic reaction of cellobiose by CbCBP proceeded via an ordered Bi Bi mechanism, while the synthetic reaction proceeded via a ping pong Bi Bi mechanism. The present study lays the foundation for optimizing the degradation of cellulose and the synthesis of functional oligosaccharides.
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