4665028 Method for production of an immobilized enzyme preparation by means of a crosslinking agent

1987 ◽  
Vol 5 (2) ◽  
pp. 357
Keyword(s):  
Enzyme Preparation ◽  
Immobilized Enzyme ◽  
Crosslinking Agent

scholarly journals Preparation and immobilization Glucoamylase and Pectinase by CLEA method

2014 ◽  
Vol 17 (2) ◽  
pp. 45-51
Author(s):  
Giang Thi Linh Tran ◽  
Oanh Ngoc Huynh
Keyword(s):  
Aspergillus Niger ◽  
Enzyme Preparation ◽  
Immobilized Enzyme ◽  
Solution Culture ◽  
Crude Enzyme ◽  
Cross Linking ◽  
Solid Culture ◽  
Enzyme Solution ◽  
Crude Enzyme Solution ◽  
Semi Solid

CLEA method (cross-linking enzyme aggregates) combines enzyme preparation and immobilization from solution culture into the same step. In this study, we applied CLEA method to immobilize two enzymes, glucoamylase and pectinase, from crude enzyme solution obtained from semi-solid culture of Aspergillus niger. The results showed that: In the same immobilized conditions (glucoamylase: 7% glutaraldehyde, 5°C, 2 hours; pectinase: 10% glutaraldehyde, 5°C, 2 hours), the immobilized enzyme from crude enzyme solution, has the abilities to be reused and activation stability under the influences of pH and temperature higher than immobilized commercial enzyme respectively.

ChemInform Abstract: Asymmetric Hydrolysis of Epoxides Using an Immobilized Enzyme Preparation from Rhodococcus sp.

ChemInform ◽  
2010 ◽  
Vol 24 (41) ◽  
pp. no-no
Author(s):  
P. HECHTBERGER ◽  
G. WIRNSBERGER ◽  
M. MISCHITZ ◽  
N. KLEMPIER ◽  
K. FABER
Keyword(s):  
Enzyme Preparation ◽  
Immobilized Enzyme ◽  
Hydrolysis Of ◽  
Rhodococcus Sp

A study of biocatalysts based on glucose oxidase

2017 ◽  
Vol 202 ◽  
pp. 303-314 ◽  
Author(s):  
E. P. Golikova ◽  
N. V. Lakina ◽  
O. V. Grebennikova ◽  
V. G. Matveeva ◽  
E. M. Sulman
Keyword(s):  
Ftir Spectroscopy ◽  
Glucose Oxidase ◽  
Gluconic Acid ◽  
Oxidation Reaction ◽  
Immobilized Enzyme ◽  
Tight Binding ◽  
Crosslinking Agent ◽  
Covalent Immobilization ◽  
Modified Silica ◽  
Inorganic Support

During this work, we studied the possibility of glucose oxidase (GOx) covalent immobilization on a modified inorganic support. A series of GOx-based biocatalysts was synthesized by crosslinking the enzyme to a surface of modified silica or alumina. Polyelectrolyte layers were used as modifiers for the silica and alumina surfaces. These layers promote tight binding of the GOx to the support. The biocatalyst’s activity and stability were studied using an oxidation reaction of d-glucose to d-gluconic acid. It was found that GOx immobilized on the modified SiO2 using glutardialdehyde as a crosslinking agent was the most active and stable catalytic system, showing an 85% yield of gluconic acid. A study of the synthesized biocatalyst structure using FTIR spectroscopy showed that the enzyme was covalently crosslinked to the surface of an inorganic support modified with chitosan and glutardialdehyde. In the case of SiO2, the quantity of the immobilized enzyme was higher than in the case of Al2O3.

scholarly journals Parameters necessary to define an immobilized enzyme preparation

2020 ◽  
Vol 90 ◽  
pp. 66-80 ◽  
Author(s):  
Joseph Boudrant ◽  
John M. Woodley ◽  
Roberto Fernandez-Lafuente
Keyword(s):  
Enzyme Preparation ◽  
Immobilized Enzyme

Asymmetric hydrolysis of epoxides using an immobilized enzyme preparation from Rhodococcus sp.

1993 ◽  
Vol 4 (6) ◽  
pp. 1161-1164 ◽  
Author(s):  
Petra Hechtberger ◽  
Gernot Wirnsberger ◽  
Martin Mischitz ◽  
Norbert Klempier ◽  
Kurt Faber
Keyword(s):  
Enzyme Preparation ◽  
Immobilized Enzyme ◽  
Hydrolysis Of ◽  
Rhodococcus Sp

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.

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