scholarly journals STUDIES ON THE MECHANISMS OF HYDROLYSIS OF CELLULOSE FIBERS

1963 ◽  
Vol 19 (5) ◽  
pp. 346-355
Author(s):  
Ichiro Sakurada ◽  
Yasuyoshi Sakaguchi ◽  
Yoko Tanaka
2021 ◽  
Author(s):  
G. Ramiro Escudero ◽  
González P. Jeovani ◽  
Pérez Ch. Rosa Elena

Deinking of Mixed Office Waste [MOW] paper was carried out by using a flotation device and adding enzymes as defibrillators. Employing the computational simulation of the molecular coupling between the cellulase enzyme obtained from Trichoderma sp. and cellulose, the enzyme-cellulose molecular complex and the main amino acids endo-β-1,4-D-glucanase of this molecule, responsible for the hydrolysis of cellulose, were obtained. Three of these amino acids were used for deinking. The deinked cellulose fibers were evaluated according to the standards of the paper industry (ISO whiteness [brightness], factor of reflectance, opacity, and tonality) to determine the efficiency of deinking. The experimental results show that the best optical characteristics of the sheets of deinked paper with amino acids are those where a mixture of aspartate, glutamate, and asparagine was applied, instead of their individual dosage. In addition to the aforesaid, the use of enzymes instead of the traditionally used reagent, such as sodium hydroxide, avoids the contamination of wastewater; additionally, the operation of the column is carried out easily, taking into consideration that the pH of the system goes from alkaline to neutral.


MRS Advances ◽  
2020 ◽  
Vol 5 (52-53) ◽  
pp. 2669-2678
Author(s):  
Jeovani González P. ◽  
Ramiro Escudero G

AbstractDeinking of recycled office (MOW) paper was carried out by using a flotation column and adding separately sodium hydroxide, and the enzyme Cellulase Thricodema Sp., as defibrillators.The de-inked cellulose fibers were characterized according to the standards of the paper industry, to compare the efficiency of the deinking of each chemical reagent used to hydrolyze the fibers and defibrillate them.The computational simulation of the molecular coupling between the enzyme and cellulose was performed, to establish the enzyme-cellulose molecular complex and then to identify the principal amino-acids of endo-β-1,4-D-glucanase in this molecular link, which are responsible for the hydrolysis of the cellulose.Experimental results show the feasibility to replace sodium hydroxide with the enzyme Cellulase Thricodema Sp., by obtaining deinked cellulose with similar optical and physical properties.The use of the enzyme instead of sodium hydroxide avoids the contamination of the residual water; in addition to that, the column is operated more easily, taking into consideration that the pH of the system goes from alkaline to neutral.


2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.


2013 ◽  
Vol 85 (17) ◽  
pp. 8121-8126 ◽  
Author(s):  
Britta Opitz ◽  
Andreas Prediger ◽  
Christian Lüder ◽  
Marrit Eckstein ◽  
Lutz Hilterhaus ◽  
...  

2021 ◽  
Author(s):  
Yuxiao Dong ◽  
Dongshen Tong ◽  
Laibin Ren ◽  
Xingtao Chen ◽  
Hao Zhang ◽  
...  

2013 ◽  
Vol 127 ◽  
pp. 500-507 ◽  
Author(s):  
Reeta Rani Singhania ◽  
Anil Kumar Patel ◽  
Rajeev K. Sukumaran ◽  
Christian Larroche ◽  
Ashok Pandey

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