Cellulose is the world's most abundant natural polymer and it can be used as a substitute for fossil derived products. The work described here evaluated the use of mono-component enzyme treatment, using endoglucanase (EG) and lytic polysaccharide monooxygenase (LPMO), to improve the properties of micro-fibrillated cellulose (MFC) produced from mechanically refined kraft pulp. Endoglucanase treatment of the pulp significantly reduced the degree of polymerization (DP) of the cellulose by promoting fiber cutting. In contrast, LPMO treatment only slightly reduced the fiber length and pulp viscosity. However, the introduction of carboxylic acid groups by the action of LPMO appeared to enhance the accessible surface area of cellulose. Enzyme-treated MFC showed improved nano-fibrillation with transmittance and water retention values increased after both enzyme treatments. The cellulose films derived from enzyme-treated MFC showed enhanced mechanical properties with the LPMO-treated films showing superior tensile strength (77 MPa) and Young's modulus (3600 MPa). Thermogravimetric analysis (TGA) also indicated improved thermal stability for both enzyme-treated films. LPMO treatments proved more effective, promoting nano-fibrillation while maintaining fiber integrity and enhanced intermolecular interactions.
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http://dx.doi.org/10.1016/j.carbpol.2024.123037 | DOI Listing |
Int J Mol Sci
December 2024
Department of Molecular Biotechnology, Faculty of Chemistry, University of Gdansk, 80-309 Gdansk, Poland.
The increasing antibiotic resistance among bacteria challenges the biotech industry to search for new antibacterial molecules. Endolysin TP84_28 is a thermostable, lytic enzyme, encoded by the bacteriophage (phage) TP-84, and it effectively digests host bacteria cell wall. Biofilms, together with antibiotic resistance, are major problems in clinical medicine and industry.
View Article and Find Full Text PDFCarbohydr Polym
February 2025
Forest Product Biotechnology/Bioenergy Group, Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, V6T 1Z4, Canada. Electronic address:
Cellulose is the world's most abundant natural polymer and it can be used as a substitute for fossil derived products. The work described here evaluated the use of mono-component enzyme treatment, using endoglucanase (EG) and lytic polysaccharide monooxygenase (LPMO), to improve the properties of micro-fibrillated cellulose (MFC) produced from mechanically refined kraft pulp. Endoglucanase treatment of the pulp significantly reduced the degree of polymerization (DP) of the cellulose by promoting fiber cutting.
View Article and Find Full Text PDFInt J Biol Macromol
November 2024
Department of Geosciences and Natural Resource Management, University of Copenhagen, Rolighedsvej 23, 1958 Frederiksberg C, Denmark; Bigelow Laboratory for Ocean Sciences, 60 Bigelow Drive, 04544 East Boothbay, ME, USA.
It has been demonstrated that LPMO reactions can be driven by light, using the photosynthetic pigment chlorophyllin to achieve efficient oxidative degradation of cellulose. However, the effect of chlorophyllin on cellulases remains unclear. This study discovered that chlorophyllin does not affect the hydrolytic activity of cellulases under dark conditions.
View Article and Find Full Text PDFBiotechnol Biofuels Bioprod
October 2024
Division of Industrial Biotechnology, Department of Life Sciences, Chalmers University of Technology, Kemivägen 10, 412 96, Gothenburg, Sweden.
FEBS J
January 2025
Faculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.
Because of the association with other complex polysaccharides, extracting and utilizing cellulose from lignocellulosic materials requires the combined action of a broad range of carbohydrate-active enzymes, including multiple glycoside hydrolases (GHs) and lytic polysaccharide monooxygenases (LPMOs). The interplay between these enzymes and the way in which Nature orchestrates their co-existence and combined action are topics of great scientific and industrial interest. To gain more insight into these issues, we have studied the lignocellulose-degrading abilities of an enzyme from Caldibacillus cellulovorans (CcLPMO10-Man5), comprising an LPMO domain, a GH5 mannanase domain and two family 3 carbohydrate-binding modules (CBM3).
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