ArticleBiotechnology for biofuels2019
Impacts of cellulase deactivation at the moving air-liquid interface on cellulose conversions at low enzyme loadings.
Article in Biotechnology for biofuels, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 35 citations in OpenAlex.
- Inactivation of PETase at Interfaces Inhibits PET Plastic Depolymerization.ACS sustainable chemistry & engineering · 2026Article
- Inactivation and process intensification of β-glucosidase in biomass utilization.Applied microbiology and biotechnology · 2023Review
- Constraints and advances in high-solids enzymatic hydrolysis of lignocellulosic biomass: a critical review.Biotechnology for biofuels · 2020Review
- Effect of residual extractable lignin on acetone-butanol-ethanol production in SHF and SSF processes.Biotechnology for biofuels · 2020Article
Corrections and comments
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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
backgroundWe recently confirmed that the deactivation of
resultsAvicel cellulose conversions at high solid loading were more than doubled by minimizing loss of cellulases to the air-liquid interface. Maximum cellulose conversions were high for surface-active supplemented shaken flasks or unshaken flasks because of low cellulase deactivation at the air-liquid interface. The nonionic surfactant Tween 20 was unable to completely prevent cellulase deactivation in shaken flasks and only reduced cellulose conversions at unreasonably high concentrations.
conclusionsHigh dynamic interfacial areas created through baffles in reactor vessels, low volumes in high-capacity vessels, or high shaking speeds severely limited cellulose conversions at low enzyme loadings. Precipitation of cellulases due to aggregation at the air-liquid interface caused their continuous deactivation in shaken flasks and severely limited solubilization of cellulose.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.