ArticleBiochemistry and biophysics reports2016
A mutant β-glucosidase increases the rate of the cellulose enzymatic hydrolysis.
Article in Biochemistry and biophysics reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Direct synthesis of molecularly imprinted nanozymes with a biomimetic catalytic motif for glycosidic bond cleavage.Frontiers in chemistry · 2026Article
- Microalgal Bioethanol Production for Sustainable Development: Current Status and Future Prospects.Indian journal of microbiology · 2025Article
- Comparative Analysis of Structural Variations Due to Genome Shuffling of Bacillus Subtilis VS15 for Improved Cellulase Production.International journal of molecular sciences · 2020Article
- Temperature and pH effect on glucose production from pretreated bagasse by a novel species ofHeliyon · 2018Article
- When substrate inhibits and inhibitor activates: implications of β-glucosidases.Biotechnology for biofuels · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enzymatic hydrolysis of cellulose and lignocellulosic materials is marked by a rate decrease along the reaction time. Cellobiohydrolase slow dissociation from the substrate and its inhibition by the cellobiose produced are relevant factors associated to the rate decrease. In that sense, addition of β-glucosidases to the enzyme cocktails employed in cellulose enzymatic hydrolysis not only produces glucose as final product but also reduces the cellobiohydrolase inhibition by cellobiose. The digestive β-glucosidase GH1 from the fall armyworm
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