ArticleBiotechnology and bioengineering2016
Alleviating product inhibition in cellulase enzyme Cel7A.
Article in Biotechnology and bioengineering, 2016. 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, 60 citations in OpenAlex.
- Advancing continuous enzymatic hydrolysis for improved biomass saccharification.Biotechnology for biofuels and bioproducts · 2025Article
- Structural and functional insights into cellulosomes: masters of plant cell wall degradation.Frontiers in microbiology · 2025Review
- Biochemical and inhibitor analysis of recombinant cellobiohydrolases from Phanerochaete chrysosporium.Biotechnology for biofuels and bioproducts · 2024Article
- Mining unique cysteine synthetases and computational study on thoroughly eliminating feedback inhibition through tunnel engineering.Protein science : a publication of the Protein Society · 2024Article
- Single-molecule tracking reveals dual front door/back door inhibition of Cel7A cellulase by its product cellobiose.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The S-S bridge mutation between the A2 and A4 loops (T416C-I432C) of Cel7A ofApplied and environmental microbiology · 2024Article
- Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023Review
- Production of phenylpyruvic acid by engineered L-amino acid deaminase from Proteus mirabilis.Biotechnology letters · 2022Review
- LPMOInternational journal of molecular sciences · 2020Article
- Penicillium janthinellum NCIM1366 shows improved biomass hydrolysis and a larger number of CAZymes with higher induction levels over Trichoderma reesei RUT-C30.Biotechnology for biofuels · 2020Article
- Bioethanol and lipid production from the enzymatic hydrolysate of wheat straw after furfural extraction.Applied microbiology and biotechnology · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes that degrade cellulose into glucose are one of the most expensive components of processes for converting cellulosic biomass to fuels and chemicals. Cellulase enzyme Cel7A is the most abundant enzyme naturally employed by fungi to depolymerize cellulose, and like other cellulases is inhibited by its product, cellobiose. There is thus great economic incentive for minimizing the detrimental effects of product inhibition on Cel7A. In this work, we experimentally generated 10 previously proposed site-directed mutant Cel7A enzymes expected to have reduced cellobiose binding energies (the majority of mutations were to alanine). We then tested their resilience to cellobiose as well as their hydrolytic activities on microcrystalline cellulose. Although every mutation tested conferred reduced product inhibition (and abolished it for some), our results confirm a trade-off between Cel7A tolerance to cellobiose and enzymatic activity: Reduced product inhibition was accompanied by lower overall enzymatic activity on crystalline cellulose for the mutants tested. The tempering effect of mutations on inhibition was nearly constant despite relatively large differences in activities of the mutants. Our work identifies an amino acid in the Cel7A product binding site of interest for further mutational studies, and highlights both the challenge and the opportunity of enzyme engineering toward improving product tolerance in Cel7A.
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