Properties of the recombinant proteins derived from Fibrobacter succinogenes endoglucanase F (EGF), AD2 and AD4, were characterized using surface plasmon resonance. Because AD2, which contains two reiterated regions, showed stronger affinity to immobilized carboxymethylcellulose (CMC) than did AD4, which contains only the first reiterated region, it has been assumed that the reiterated regions of EGF are cellulose-binding modules. While calcium enhanced the binding of AD2 to the immobilized CMC, it did not enhance the binding of AD4. Moreover, the results obtained from experiments using cellooligosaccharides showed that the binding sites of AD4 and AD2 span approximately four and nine glucosyl units, respectively.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1111/j.1574-6968.2002.tb11359.x | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The Effect of CBM1 and Linker on the Oxidase, Peroxidase and Monooxygenase Activities of AA9 LPMOs: Insight into Their Correlation with the Nature of Reductants and Crystallinity of Celluloses.
Int J Mol Sci
November 2024
The Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Jiangsu Key Lab for the Chemistry & Utilization of Agricultural and Forest Biomass, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China.
This study explores the effect of carbohydrate-binding module 1 (CBM1) and the linker on the function of auxiliary activity 9 (AA9) lytic polysaccharide monooxygenases (LPMOs), with a particular focus on monooxygenase activity, using different crystallinity celluloses and electron donors. The tested C1/C4-oxidizing AA9 LPMOs exhibited higher oxidase and peroxidase activities compared to those of the C4-oxidizing AA9 LPMOs. While the presence of CBM1 promoted cellulose-binding affinity, it reduced the oxidase activity of modular AA9 LPMOs.
View Article and Find Full Text PDFA cellulose-binding domain specific for native crystalline cellulose in lytic polysaccharide monooxygenase from the brown-rot fungus Gloeophyllum trabeum.
Carbohydr Polym
January 2025
Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan; United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Tokyo, Japan; Institute of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan. Electronic address:
Cellulose-binding domains (CBDs) play a vital role in cellulose degradation by enzymes. Despite the strong ability of brown-rot fungi to degrade cellulose in wood, they have been considered to lack or have a low number of enzymes with CBD. Here, we report the C-terminal domain of a lytic polysaccharide monooxygenase from the brown-rot fungus Gloeophyllum trabeum (GtLPMO9A-2) functions as a CBD, classified as a new family of carbohydrate-binding module, CBM104.
View Article and Find Full Text PDFCellulose binding and the timing of expression influence protein targeting to the double-layered cyst wall of .
mSphere
September 2024
Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts, USA.
The cyst wall of the eye pathogen contains cellulose and has ectocyst and endocyst layers connected by conical ostioles. Cyst walls contain families of lectins that localize to the ectocyst layer (Jonah) or the endocyst layer and ostioles (Luke and Leo). How lectins and an abundant laccase bind cellulose and why proteins go to locations in the wall are not known and are the focus of the studies here.
View Article and Find Full Text PDFInvestigating Cellulose Binding of Peptides Derived from Carbohydrate Binding Module 1.
Biomacromolecules
September 2024
Biological Chemistry, Chemistry Department, Technical University of Darmstadt, Darmstadt 64278, Germany.
Carbohydrate-binding modules (CBM) have emerged as useful tools for a wide range of tasks, including the use as purification tags or for cellulose fiber modification. For this purpose, the CBM needs to be attached to a target protein leading to large constructs. We investigated if short peptides from the carbohydrate binding site of CBMs can bind in a similar way as native, full-length CBMs to nanocrystalline cellulose (NCC) or cotton linter paper.
View Article and Find Full Text PDFAcidothermus cellulolyticus E1 endoglucanase expressed in planta undergoes extensive hydroxyproline-O-glycosylation and exhibits enhanced impact on biomass digestibility.
Plant Cell Rep
July 2024
Arkansas Biosciences Institute, Arkansas State University, Jonesboro, AR, 72401, USA.
E1 holoenzyme was extensively Hyp-O-glycosylated at the proline rich linker region in plants, which substantially increased the molecular size and improved the enzymatic digestibility of the biomass of transgenic plants. Thermophilic E1 endo-1,4-β-glucanase derived from Acidothermus cellulolyticus has been frequently expressed in planta to reconstruct the plant cell wall to overcome biomass recalcitrance. However, the expressed holoenzyme exhibited a larger molecular size (~ 100 kDa) than the theoretical one (57 kDa), possibly due to posttranslational modifications in the recombinant enzyme within plant cells.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!