Effect of immobilized enzyme deactivation in fixed- and fluid-bed reactors

1978 ◽  
Vol 20 (6) ◽  
pp. 781-797 ◽  
Author(s):  
Ajit Sadana
Keyword(s):  
Immobilized Enzyme ◽  
Enzyme Deactivation ◽  
Fluid Bed

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.

ANALISIS KINERJA PABRIK TEH HITAM “PAHIT MADU”

2013 ◽  
Vol 13 (3) ◽  
Author(s):  
Djawardi Djawardi ◽  
Yustiar Gunawan
Keyword(s):  
Heat Exchanger ◽  
Production Process ◽  
Black Tea ◽  
Production Equipment ◽  
Standard Means ◽  
Fluid Bed ◽  
Calculation Results ◽  
Low Performance ◽  
Equipment Utilization

The business unit's black tea processing of Perkebunan Nusantara suffered a loss of approximately Rp.60 billion. This is caused by the failure to achieve the quality and quantity of production which has been targeted by the management. Black tea processing factory "Pahit Madu" is required to improve the performance of the production process. To improve the production of black tea starts from improved production equipment through improved equipment utilization. One method ofmeasuring the effectiveness of using an apparatus is Overall EquipmentEffectiveness (OEE). OEE calculation results show that black tea factory "Pahit Madu" for four (4) years under the standard. Means, the effectiveness of utilization of equipment in the factory black tea "Pahit Madu" was still very low. This was shown by the low performance equipment in the milling unit, drying unit and sortation unit. Toimprove the performance of the plant should begin by increasing the Cutting Tearing Curling (CTC) machine in milling stations, machines Fluid Bed Dryer (FBD) and Heat Exchanger (HE) at the drying stations, and Winnower machines at the sortation stations.

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.

Mass transfer in heterogeneous system enzyme-substrate; Approximate analytical model for the case of liquid substrate-immobilized enzyme

1982 ◽  
Vol 47 (11) ◽  
pp. 3013-3018
Author(s):  
František Kaštánek ◽  
Jindřich Zahradník ◽  
Germanico Ocampo
Keyword(s):  
Mass Transfer ◽  
Heterogeneous System ◽  
Immobilized Enzyme ◽  
Enzymatic Reaction ◽  
Analytical Form ◽  
Approximate Model ◽  
Basic Type ◽  
Reaction Interface ◽  
Enzyme Substrate ◽  
Flow Intensity

Calculation procedure is suggested for flow intensity of substrate toward reaction interface of immobilized enzyme at simultaneous effect of enzymatic reaction and internal diffusion. The approximate model is presented in an analytical form for the basic type of Michaelis-Menten kinetics and for the case of inhibition in excess of substrate.

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