Recycle of the cellulase— enzyme complex after hydrolysis of steam-exploded wood

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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Optimizing the composition of cellulase enzyme complex from Penicillium verruculosum: Enhancing hydrolytic capabilities via genetic engineering

Catalysis in Industry ◽

10.1134/s2070050416010128 ◽

2016 ◽

Vol 8 (1) ◽

pp. 101-106 ◽

Cited By ~ 3

Author(s):

A. P. Sinitsyn ◽

O. G. Korotkova ◽

O. A. Sinitsyna ◽

A. M. Rozhkova ◽

G. S. Dotsenko ◽

...

Keyword(s):

Genetic Engineering ◽

Enzyme Complex ◽

Penicillium Verruculosum ◽

Cellulase Enzyme

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MECHANISM OF ACTIVATION OF HOG PANCREATIC LIPASE BY SODIUM TAUROCHOLATE

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y63-083 ◽

1963 ◽

Vol 41 (1) ◽

pp. 719-730 ◽

Cited By ~ 4

Author(s):

Paul J. Fritz ◽

Paul Melius

Keyword(s):

Activation Energy ◽

Enzymatic Hydrolysis ◽

Pancreatic Lipase ◽

Sodium Taurocholate ◽

Enzyme Complex ◽

Temperature Dependent ◽

Fast Reaction ◽

Presence And Absence ◽

Hydrolysis Of

A new preparation of hog pancreatic lipase is described which is evidently the most stable one of its kind. From the composition of the reaction mixtures after enzymatic hydrolysis with and without sodium taurocholate, it appears that the hydrolysis of triglyceride to diglyceride is facilitated and the hydrolysis of diglyceride to monoglyceride is depressed in the presence of taurocholate. The differences in the curves showing the rates of hydrolysis of triolein, monoolein, tributyrin, and monobutyrin in the presence and absence of taurocholate also indicate that the taurocholate acts to split the diglyceride–enzyme complex and thus increases the action of the enzyme on the triglyceride ester. The hydrolysis of the triglyceride is a fast reaction whereas the di- and mono-glycerides are hydrolyzed at much slower rates. The activation energy for the lipolysis of the triolein and tributyrin has been calculated in the presence and absence of taurocholate. This was possible because in spite of earlier reports that the lipolysis of triolein was not temperature dependent between 10 and 40 degrees, we found these reactions to be temperature dependent. The lesser activating effect at the highest taurocholate concentrations indicates this is not a simple emulsifying effect.

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Hydrolysis of Soybean Proteins with Kamchatka Crab Hepatopancreas Enzyme Complex

Applied Biochemistry and Microbiology ◽

10.1134/s0003683818010076 ◽

2018 ◽

Vol 54 (1) ◽

pp. 76-82 ◽

Cited By ~ 5

Author(s):

T. A. Muranova ◽

D. V. Zinchenko ◽

L. A. Melanyina ◽

A. I. Miroshnikov

Keyword(s):

Enzyme Complex ◽

Soybean Proteins ◽

Kamchatka Crab ◽

Crab Hepatopancreas ◽

Hydrolysis Of

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Autolysis of Penicillium oxalicum with special reference to its cell walls

Canadian Journal of Microbiology ◽

10.1139/m82-192 ◽

1982 ◽

Vol 28 (12) ◽

pp. 1289-1295 ◽

Cited By ~ 23

Author(s):

M. I. Perez-Leblic ◽

Fuensanta Reyes ◽

R. Lahoz ◽

S. A. Archer

Keyword(s):

Cell Walls ◽

Schizophyllum Commune ◽

Dry Weight ◽

Penicillium Oxalicum ◽

Lytic Enzyme ◽

Enzyme Complex ◽

Fungal Cell ◽

Rapid Hydrolysis ◽

And Storage ◽

Hydrolysis Of

Cultures of Penicillium oxalicum growing on a denned medium supplemented with yeast extract reached the onset of autolysis after 3 days at 25 °C. Thenceforth, autolysis was progressive and eventual reductions in dry weight of 96% were recorded by day 47. The pH of the medium fluctuated between 4.0 during the exponential phase of growth and 9.0 during autolysis. Electron microscopy of autolyzing cultures revealed a progressive loss of cytoplasmic ultrastructure. Digestion of the cell walls, with a rapid hydrolysis of the three external layers and a low hydrolysis of the two inner layers, was accompanied by deep pitting and by loss of the distinct five-layered structure. A lytic enzyme complex was obtained from the filtrates of extensively autolyzed cultures. It was rich in (1 → 3)-β-glucanase and other enzymes active against a range of fungal cell wall and storage polysaccharides. This enzyme complex degraded extensively isolated cell walls of P. oxalicum and three other Ascomycetes but had less effect on walls isolated from Mucor mucedo or Schizophyllum commune. In the case of P. oxalicum, cell walls harvested from young cultures were more readily digested than were the walls from older cultures.

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