Immobilized enzyme catalysis with reaction-generated pH change

1974 ◽  
Vol 16 (10) ◽  
pp. 1345-1357 ◽  
Author(s):  
J. E. Bailey ◽  
Mary T. C. Chow
Keyword(s):  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
Ph Change

scholarly journals Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite

Catalysts ◽  
2018 ◽  
Vol 8 (7) ◽  
pp. 287 ◽  
Author(s):  
Paula Bracco ◽  
Guzman Torrelo ◽  
Sander Noordam ◽  
Glenn de Jong ◽  
Ulf Hanefeld
Keyword(s):  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
Immobilized Enzymes ◽  
Prunus Amygdalus ◽  
Hydroxynitrile Lyase ◽  
High Enzyme ◽  
Background Reaction

The hydroxynitrile lyase from Prunus amygdalus was immobilized on Celite R-633. The immobilized enzyme could successfully be utilized in buffer saturated MTBE and excellent conversions of benzaldehyde to R-mandelonitrile were observed. No leaching occurred. To achieve high enantioselectivities, the suppression of the undesired background reaction was essential. This could be achieved by high enzyme loadings and the tight packing of the immobilized enzymes. When the immobilized enzyme is loosely packed, both the enzyme catalysis and the background reaction accelerates and only a modest enantioselectivity is observed. The enzyme was recycled for up to ten times, with some loss of activity and also enantioselectivity after 5 cycles, independent of packing.

Orderly cascade of immobilized-enzyme catalysis and photocatalysis for continuous-microflow production of 2-phenylbenzothiazole

2021 ◽  
Author(s):  
Qiang Chen ◽  
Yujun Wang ◽  
Guangsheng Luo
Keyword(s):  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
First Time

Green, economic, efficient, and sustainable synthesis of 2-phenylbenzothiazole (2-PBZ)—an important versatile scaffold—remains challenging. Here, for the first time, we propose to cascade immobilized enzyme catalysis and photocatalysis in a continuous-microflow...

Specific immobilization of d-amino acid oxidase on hematin-functionalized support mimicking multi-enzyme catalysis

2015 ◽  
Vol 17 (8) ◽  
pp. 4465-4472 ◽  
Author(s):  
Jian Sun ◽  
Kun Du ◽  
Xiaoqiang Song ◽  
Qian Gao ◽  
Hao Wu ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Specifically immobilized enzyme and hematin sequentially catalyze the conversion of d-alanine and the decomposition of the generated hydrogen peroxide.

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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