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Chemical Modification of Cellulose and Its Reinforcement Effects on the Properties of PLA-Based Composites
Published in Jyotishkumar Parameswaranpillai, Suchart Siengchin, Nisa V. Salim, Jinu Jacob George, Aiswarya Poulose, Polylactic Acid-Based Nanocellulose and Cellulose Composites, 2022
Jesús Rubén Rodríguez-Núñez, Heidy Burrola-Núñez, Luis Ángel Val-Félix, Tomás Jesús Madera-Santana
Biological treatments often use cellulase to hydrolyze the cellulose chains and allow the formation of nanofibers. Cellulases are enzymes that break down cellulose's β-1,4-glycosidic linkages. Cellulases are a multi-component enzyme system that usually consists of three enzymes that work together to hydrolyze cellulose: endoglucanase (EC 3.2.1.4), cellobiohydrolase (EC 3.2.1.91), and cellobiase (-glucosidase, EC 3.2.1.21). The first two enzymes operate directly on cellulose, converting it to cellobiose and glucose. Soluble cellodextrins and amorphous cellulose are degraded by endoglucanases and cellobiohydrolases. Cellobiohydrolases, on the other hand, are best degrading crystalline cellulose (Howard et al., 2003; Wanmolee et al. 2016). However, enzymatic treatment is expensive and requires very specific conditions and stability (Durham and Sastry, 2020). Banvillet et al. (2021) reported the use of enzymatic treatment in combination with alkaline treatment to obtain cellulose nanofibers from eucalyptus. However, they found that the mechanical properties were affected when combining the treatments compared to the nanofibers that only received alkaline treatment.
Biochemical characteristics of Myceliophthora thermophila recombinant β -glucosidase (MtBgl3c) applicable in cellulose bioconversion
Published in Preparative Biochemistry & Biotechnology, 2023
Anica Dadwal, Shilpa Sharma, Tulasi Satyanarayana
In this era of global warming and depletion of fossil fuels, it is evident that the second-generation biofuels hold a promise as they utilize renewable and abundantly available lignocellulosic biomass.[1,2] The deconstruction of cellulose component of lignocellulosics involves multi-enzyme cellulase system comprising endo-1,4-β-glucanases (Egls), cellobiohydrolases (Cbhs) and β-1,4-glucosidases (Bgls).[3] The first two enzymes work in a concerted manner to produce cellodextrins and cellobiose as major end products, which are subsequently hydrolyzed by Bgls to generate monomeric sugar (glucose) that is fermented to ethanol.[4] β-Glucosidase is, therefore, a crucial component of the cellulase complex that cleaves β-1,4-glycosidic linkages in cellodextrins and cellobiose.[5] During this conversion process, the accumulated glucose (end-product) causes feedback inhibition that results in inhibiting the enzyme activity and thus lead to inefficient biomass conversion[6] that limits its industrial application. Thus, Bgl is a key enzyme in determining the cellulase efficiency and requires tolerance to higher glucose concentrations.[7,8]
Microbial and functional characterization of granulated sludge from full-scale UASB thermophilic reactor applied to sugarcane vinasse treatment
Published in Environmental Technology, 2022
Franciele Pereira Camargo, Isabel Kimiko Sakamoto, Tiago Palladino Delforno, Cédric Midoux, Iolanda Cristina Silveira Duarte, Edson Luiz Silva, Ariane Bize, Maria Bernadete Amâncio Varesche
The K01179 was observed in proportions of 0.017%. This enzyme is an endoglucanase (GH5 family) active in the Starch and sucrose metabolism and cellulose degradation pathway, converting the cellulose to its first intermediate, the cellodextrin, and also the cellodextrin to cellobiose. Other KO observed in lower proportions and mostly related with Defluviitoga genus were the β-glucosidase K05350 (0.012%), the endo-1,4-β-xylanase K01181 (0.008%) active in xylose degradation pathway, the chitinase K01183 (0.007%) and the α-L-arabinofuranosidase K01209 (0.011%), being this last one in association with the species D. tunisiensis.
Production of cellulases by Thermomucor indicae-seudaticae: characterization of a thermophilic β-glucosidase
Published in Preparative Biochemistry and Biotechnology, 2019
Eduardo da Silva Martins, Eleni Gomes, Roberto da Silva, Rodolfo Bizarria Junior
Complete cellulose hydrolysis is mediated in nature by three main types of cellulases combined: endoglucanases (EC 3.2.1.4), exoglucanases, (EC 3.2.1.91) and β-glucosidases (EC 3.2.1.21), releasing shorter chain polysaccharides, such as cellodextrin, cellobiose, and glucose.[1]