Results 61 to 70 of about 368 (86)
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Structure elucidation of a multi-modular recombinant endoglucanase, AtGH9C-CBM3A-CBM3B from Acetivibrio thermocellus ATCC 27405 and its substrate binding analysis

International Journal of Biological Macromolecules
Cellulases from GH9 family show endo-, exo- or processive endocellulase activity, but the reason behind the variation is unclear. A GH9 recombinant endoglucanase, AtGH9C-CBM3A-CBM3B from Acetivibrio thermocellus was structurally characterized for conformation, binding and dynamics assessment.
Arun Goyal, Jebin Ahmed
exaly   +3 more sources

Role of carbohydrate binding modules, CBM3A and CBM3B in stability and catalysis by a β-1,4 endoglucanase, AtGH9C-CBM3A-CBM3B from Acetivibrio thermocellus ATCC 27405

International Journal of Biological Macromolecules, 2023
A recombinant β-1,4 endoglucanase, AtGH9C-CBM3A-CBM3B from Acetivibrio thermocellus ATCC27405 was explored for biochemical properties and the role of its associated CBMs in catalysis. The gene expressing full-length multi-modular β-1,4-endoglucanase (AtGH9C-CBM3A-CBM3B) and its truncated derivatives (AtGH9C-CBM3A, AtGH9C, CBM3A and CBM3B) were ...
Ardhendu, Mandal   +2 more
openaire   +2 more sources

Rational design facilitates the improvement of glucose tolerance and catalytic properties of a β‐glucosidase from Acetivibrio thermocellus

The FEBS Journal
Cellulases are an ensemble of enzymes that hydrolyze cellulose chains into fermentable glucose and hence are widely used in bioethanol production. The last enzyme of the cellulose degradation pathway, β‐glucosidase, is inhibited by its product, glucose.
Chinmay Kamale   +2 more
openaire   +2 more sources

Synergistic carbon-rich biomass adjustment and Acetivibrio thermocellus bioaugmentation to enhance hydrogen and methane production in two-phase anaerobic digestion of food waste

Bioresource Technology
In anaerobic digestion (AD) of food waste (FW), an imbalance in the proportion of highly biodegradable waste can lead to the accumulation of organic acids or ammonia, which in turn affects the stability of the system. Using garden waste (GW) to co-digest with FW will reduce the biodegradable organic loading, while carbon-rich GW may impact the ...
Xing Yan   +4 more
openaire   +2 more sources

Mutational and structural analysis of ribose 5-phosphate isomerase B from Acetivibrio thermocellus: relationship between transformation efficiency and substrate binding pocket conformation

Enzyme and Microbial Technology
D-allose is a rare hexose sugar with a variety of potential application in food, medicine and other fields. Ribose 5-phosphate isomerase(RPI) plays a pivotal role in the synthesis of D-allose. AtRpiB from Acetivibrio thermocellus can convert D-psicose to D-allose; however, improvements in its stability, optimal temperature, and conversion efficiency ...
Shitong, Dong   +5 more
openaire   +2 more sources

Construction of an efficient thermostable cellulolytic chimera of β-glucosidase and β-1,4-endoglucanase from Acetivibrio thermocellus ATCC 27405 and its application in lignocellulose saccharification

International Journal of Biological Macromolecules
Genes encoding β-glucosidase, AtGH1 and β-1,4-endoglucanase, AtGH8 were fused via natural linker (L1) from cellulosomal gene celH from Acetivibrio thermocellus to construct cellulolytic chimera, AtGH1-L1-AtGH8. PCR amplified gene encoding chimera on ligation to pET-28a(+) vector expressed as soluble protein by E. coli BL-21(DE3) cells.
Akshita, Kanwar   +2 more
openaire   +2 more sources

Ethanol production from lignocellulose using novel modified acetivibrio thermocellus

Theoretical and Natural Science
Ignocellulose is an abundant renewable biomass with great potential as a feedstock for biofuel production. In this study, we designed a plasmid through the online tool Benchling to improve the ability of the acetivibrio thermocellus to degrade native lignocellulose.
openaire   +1 more source

A unique highly efficient, thermostable and multi-substrate specific galactanase (AtGH53) from Acetivibrio thermocellus cleaving both β (1,4)- and β (1,6)- linked galactans

Enzyme and Microbial Technology
The gene encoding endo-β-1,4-galactanase, AtGH53 from Acetivibrio thermocellus was cloned, expressed and the encoded soluble protein was biochemically characterized. Purified AtGH53 showed molecular mass of approximately, 36 kDa, an optimum temperature 70°C and half-life of 15 h at 70°C. AtGH53 displayed stability in acidic and alkaline pH ranges, with
Shreya, Biswas   +3 more
openaire   +2 more sources

Thermal resilience unveils the heat-specific molecular engineering in the nitrogenase Mo-Fe α subunit of Acetivibrio thermocellus

Increasing temperatures are a concern for global agriculture because they inhibit the activity of the Nitrogenase enzyme, which is crucial for N2 fixation. The study reveals how the nitrogenase Mo-Fe α subunit adapts to high temperatures by comparing thermophilic and mesophilic bacteria.
Arpan Raut   +5 more
openaire   +1 more source

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