Solvent-Free Enzyme Activity: Quick, High-Yielding Mechanoenzymatic Hydrolysis of Cellulose into Glucose

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.

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Further Stabilization of Alcalase Immobilized on Glyoxyl Supports: Amination Plus Modification with Glutaraldehyde

Molecules ◽

10.3390/molecules23123188 ◽

2018 ◽

Vol 23 (12) ◽

pp. 3188 ◽

Cited By ~ 8

Author(s):

Fouzia Hussain ◽

Sara Arana-Peña ◽

Roberto Morellon-Sterling ◽

Oveimar Barbosa ◽

Sabrina Ait Braham ◽

...

Keyword(s):

Enzyme Activity ◽

Immobilized Enzyme ◽

Free Enzyme ◽

Agarose Beads ◽

Modified Enzyme ◽

Hydrolysis Of ◽

Nitrophenyl Ester

Alcalase was immobilized on glyoxyl 4% CL agarose beads. This permitted to have Alcalase preparations with 50% activity retention versus Boc-l-alanine 4-nitrophenyl ester. However, the recovered activity versus casein was under 20% at 50 °C, as it may be expected from the most likely area of the protein involved in the immobilization. The situation was different at 60 °C, where the activities of immobilized and free enzyme became similar. The chemical amination of the immobilized enzyme or the treatment of the enzyme with glutaraldehyde did not produce any significant stabilization (a factor of 2) with high costs in terms of activity. However, the modification with glutaraldehyde of the previously aminated enzyme permitted to give a jump in Alcalase stability (e.g., with most than 80% of enzyme activity retention for the modified enzyme and less than 30% for the just immobilized enzyme in stress inactivation at pH 7 or 9). This preparation could be used in the hydrolysis of casein at pH 9 even at 67 °C, retaining around 50% of the activity after 5 hydrolytic cycles when the just immobilized preparation was almost inactive after 3 cycles. The modified enzyme can be reused in hydrolysis of casein at 45 °C and pH 9 for 6 cycles (6 h) without any decrease in enzyme activity.

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Effect of furfural on the enzyme activity during enzymatic hydrolysis of cellulose isolated from poplar wood (Populus sp.) Wpływ furfuralu na aktywność enzymu podczas hydrolizy celulozy wyodrębnionej z drewna topoli (Populus sp.)

PRZEMYSŁ CHEMICZNY ◽

10.15199/62.2015.11.7 ◽

2015 ◽

Vol 1 (11) ◽

pp. 67-70

Author(s):

Janusz Zawadzki

Keyword(s):

Enzyme Activity ◽

Enzymatic Hydrolysis ◽

Poplar Wood ◽

Enzymatic Hydrolysis Of Cellulose ◽

Hydrolysis Of Cellulose ◽

Hydrolysis Of

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Impact of tensile and compressive forces on hydrolysis of cellulose and chitin

Physical Chemistry Chemical Physics ◽

10.1039/d1cp01650d ◽

2021 ◽

Author(s):

Hirokazu Kobayashi ◽

Yusuke Suzuki ◽

Takuya Sagawa ◽

Kyoichi Kuroki ◽

Jun-ya Hasegawa ◽

...

Keyword(s):

Solvent Free ◽

Reaction Pathways ◽

Selective Hydrolysis ◽

Thermal Reactions ◽

Unique Reaction ◽

Hydrolysis Of Cellulose ◽

Hydrolysis Of

Mechanochemistry enables unique reaction pathways in comparison to conventional thermal reactions. Notably, it can achieve selective hydrolysis of cellulose and chitin, a set of abundant and recalcitrant biomass, by solvent-free...

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Regulation of cellulase from Ruminococcus

Canadian Journal of Microbiology ◽

10.1139/m72-053 ◽

1972 ◽

Vol 18 (3) ◽

pp. 347-353 ◽

Cited By ~ 23

Author(s):

M. C. Fusee ◽

J. M. Leatherwood

Keyword(s):

Enzyme Activity ◽

Cell Growth ◽

Catabolite Repression ◽

Specific Activity ◽

Product Inhibition ◽

Enzyme Synthesis ◽

Energy Sources ◽

Low Concentrations ◽

Hydrolysis Of Cellulose ◽

Hydrolysis Of

The regulation of cellulase was examined in Ruminococcus albus and R. flavefaciens. Hydrolysis of cellulose, as shown by the formation of clear zones around the colonies of bacteria grown in cellulose-agar roll tubes, was inhibited by moderate levels of cellobiose. An intermediate in the metabolism of cellobiose may be responsible for the inhibition since strains which can use either sucrose or lactose were similarly inhibited by these energy sources. The inhibition of cellulase was examined in relation to either repression of enzyme synthesis or product inhibition of the enzyme activity. There was no inhibition by cellobiose added either to the routine enzymatic assay or to assays using low concentrations of carboxymethylcellulose. A repression mechanism was indicated by the decrease in specific activity of cultures grown in higher concentrations of cellobiose. The specific activity was calculated as the enzymatic activity on carboxymethylcellulose with respect to cell growth. The mechanism of repression was not distinguished between the model proposed by Jacob and Monod and catabolite repression. The growth of R. albus cultured in cellobiose–cellulose liquid medium exhibited a diauxic pattern similar to that described by Monod.

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