Mathematical modeling of diffusion and reaction in the hydrolysis of vegetable protein in an immobilized enzyme recycle reactor

1984 ◽  
Vol 26 (2) ◽  
pp. 156-166 ◽  
Author(s):  
B. Adu-Amankwa ◽  
A. Constantinides
Keyword(s):  
Mathematical Modeling ◽  
Vegetable Protein ◽  
Immobilized Enzyme ◽  
Recycle Reactor ◽  
Hydrolysis Of ◽  
Enzyme Recycle

On the Preparation of Bovine α-Thrombin

1978 ◽  
Vol 39 (01) ◽  
pp. 193-200 ◽  
Author(s):  
Erwin F Workman ◽  
Roger L Lundblad
Keyword(s):  
Immobilized Enzyme ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Guanidine Hydrochloride ◽  
Low Molecular Weight ◽  
Reversible Process ◽  
Gel Beads ◽  
Tissue Thromboplastin ◽  
C 50 ◽  
Hydrolysis Of

SummaryAn improved method for the preparation of bovine α-thrombin is described. The procedure involves the activation of partially purified prothrombin with tissue thromboplastin followed by chromatography on Sulfopropyl-Sephadex C-50. The purified enzyme is homogeneous on polyacrylamide discontinuous gel electrophoresis and has a specific activity toward fibrinogen of 2,200–2,700 N.I.H. U/mg. Its stability on storage in liquid media is dependent on both ionic strenght and temperature. Increasing ionic strength and decreasing temperature result in optimal stability. The denaturation of α-thrombin by guanidine hydrochloride was found to be a partially reversible process with the renatured species possessing properties similar to “aged” thrombin. In addition, the catalytic properties of a-thrombin covalently attached to agarose gel beads were also examined. The activity of the immobilized enzyme toward fibrinogen was affected to a much greater extent than was the hydrolysis of low molecular weight, synthetic substrates.

Immobilized Nanoparticles-Mediated Enzymatic Hydrolysis of Cellulose for Clean Sugar Production: A Novel Approach

2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai
Keyword(s):  
Catalytic Activity ◽  
Enzymatic Hydrolysis ◽  
Immobilized Enzyme ◽  
Free Enzyme ◽  
Magnetic Nanomaterials ◽  
Sugar Production ◽  
Cellulase Enzyme ◽  
Enzymatic Hydrolysis Of Cellulose ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of

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.

Cellulase Adsorption and an Evaluation of Enzyme Recycle During Hydrolysis of Steam-Exploded Softwood Residues

2002 ◽  
pp. 641-654
Author(s):  
Yanpin Lu ◽  
Bin Yang ◽  
David Gregg ◽  
John N. Saddler ◽  
Shawn D. Mansfield
Keyword(s):  
Cellulase Adsorption ◽  
Hydrolysis Of ◽  
Enzyme Recycle

Modeling and Optimization of Lipase-Catalyzed Partial Hydrolysis for Diacylglycerol Production in Packed Bed Reactor

2016 ◽  
Vol 12 (7) ◽  
pp. 681-689 ◽  
Author(s):  
Eng-Tong Phuah ◽  
Yee-Ying Lee ◽  
Teck-Kim Tang ◽  
Oi-Ming Lai ◽  
Thomas Shean-Yaw Choong ◽  
...  
Keyword(s):  
Immobilized Enzyme ◽  
Rhizomucor Miehei ◽  
Packed Bed ◽  
Packed Bed Reactor ◽  
Partial Hydrolysis ◽  
Optimal Conditions ◽  
Lack Of Fit ◽  
Bed Height ◽  
Hydrolysis Of ◽  
Quadratic Models

Abstract Response surface methodology (RSM) was employed to optimize the process variables namely packed bed height (cm) and flow rates (ml/min) on diacylglycerol (DAG) production via partial hydrolysis of palm oil using immobilized Rhizomucor miehei lipase in packed bed reactor (PBR). Quadratic models were successfully developed for both DAG(y) and unhydrolyzed triacylglycerol ((un)TAG) with determination coefficient (R2) of 0.9931 and 0.9986, respectively coupled with insignificant lack of fit (p > 0.05). Optimal conditions for DAG synthesis were evaluated to be 10 cm packed bed height and 3.8 ml/min flow rate. Immobilized enzyme can be reused up to 10 times without significant changes in enzymatic activity. The partial hydrolysis under studied was found to be mass transfer-controlled.

Kinetics of the acid-catalyzed hydrolysis of tetraethoxysilane (TEOS) by 29Si NMR spectroscopy and mathematical modeling

2018 ◽  
Vol 86 (2) ◽  
pp. 316-328 ◽  
Author(s):  
J. C. Echeverría ◽  
P. Moriones ◽  
G. Arzamendi ◽  
J. J. Garrido ◽  
M. J. Gil ◽  
...  
Keyword(s):  
Mathematical Modeling ◽  
Nmr Spectroscopy ◽  
29Si Nmr ◽  
Acid Catalyzed ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
29Si Nmr Spectroscopy

Aroma Components of Acid-Hydrolyzed Vegetable Protein Made by Partial Hydrolysis of Rice Bran Protein

2007 ◽  
Vol 55 (8) ◽  
pp. 3044-3050 ◽  
Author(s):  
Arporn Jarunrattanasri ◽  
Chockchai Theerakulkait ◽  
Keith R. Cadwallader
Keyword(s):  
Rice Bran ◽  
Vegetable Protein ◽  
Partial Hydrolysis ◽  
Rice Bran Protein ◽  
Aroma Components ◽  
Hydrolysis Of

Effects of organic solvents on immobilized enzyme catalyses. Chymotrypsin immobilized on Sephadex

1980 ◽  
Vol 58 (23) ◽  
pp. 2633-2640 ◽  
Author(s):  
Diana H. Pliura ◽  
J. Bryan Jones
Keyword(s):  
Enzyme Activity ◽  
Organic Solvents ◽  
Immobilized Enzyme ◽  
Reaction Medium ◽  
Butyl Alcohol ◽  
Native Enzyme ◽  
Tert Butyl ◽  
Tert Butyl Alcohol ◽  
Catalytic Rate ◽  
Hydrolysis Of

The esterolytic activities of native chymotrypsin (CT) and immobilized CT-Sephadex have been studied in the presence of up to 20% of the organic solvents methanol, ethanol, 2-propanol, tert-butyl alcohol, dioxane, or DMSO. The general cosolvent-induced inhibition of the native enzyme was attenuated for immobilized CT. Most noticeably, the apparent catalytic rate constants for the CT-Sephadex-catalyzed hydrolysis of N-acetyl-L-tyrosine ethyl ester were invariant over the 2–20% dioxane concentration range surveyed. In contrast, the activity of the native enzyme in 20% dioxane was only 3% the activity recorded in the absence of cosolvent. Increasing the hydrophobic character of the protic cosolvents destabilized the native enzyme but stabilized CT-Sephadex. Both native and immobilized CT displayed remarkable stability in 20% aqueous DMSO [Formula: see text]. At least part of the DMSO-induced inhibition of native CT and CT-Sephadex was offset by increasing the apparent pH of the reaction medium. The altered kinetic patterns for CT-Sephadex are best explained by the effects of diffusional limitations on the apparent enzyme activity. The best compromise solvent for preparative applications of CT-Sephadex was found to be tert-butyl alcohol.

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