ArticleRSC advances2020
The use of fluorescent protein-tagged carbohydrate-binding modules to evaluate the influence of drying on cellulose accessibility and enzymatic hydrolysis.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- Time-resolved tracking of cellulose biosynthesis and assembly during cell wall regeneration in liveScience advances · 2025Article
- Review
- Greater Importance of Structural Changes Over Lignin Removal in Impacting the Enzymatic Hydrolysis of Crop Straws.ACS omega · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The influence of drying on cellulose accessibility and enzymatic hydrolysis was assessed. Dissolving pulp was differentially dried by freeze-, air- and oven-drying at 50 °C and subsequently hydrolyzed using the commercial CTec 3 cellulase preparation. It was apparent that drying reduced the ease of enzymatic hydrolysis of all of the substrates with a pronounced reduction (48%) exhibited by the oven-dried pulp. To assess if the ease of hydrolysis was due to enzyme accessibility to the substrate, microscopy (SEM), FTIR spectroscopy, water retention value (WRV), fiber aspect ratio analysis, Simons' stain and the selective binding of Fluorescent Protein-tagged Carbohydrate Binding Modules (FP-CBMs): CBM3a (crystalline cellulose) and CBM17 (amorphous cellulose) in combination with confocal laser scanning microscopy (CLSM) were used. The combined methods indicated that, if the gross characteristics of the substrate limited enzyme accessibility, the cellulases, as represented by the FP-CBMs, could not in turn access the finer structural components of the cellulosic substrates.
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Registered trials
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