Electron-transfer communication between a redox polymer matrix and an immobilized enzyme: activity of nitrate reductase in a viologen-acrylamide copolymer

1990 ◽  
Vol 112 (17) ◽  
pp. 6438-6439 ◽  
Author(s):  
Itamar Willner ◽  
Azalia Riklin ◽  
Noa Lapidot
Keyword(s):  
Electron Transfer ◽  
Enzyme Activity ◽  
Nitrate Reductase ◽  
Polymer Matrix ◽  
Immobilized Enzyme ◽  
Redox Polymer

Immobilization of enzymes masks their active site

1984 ◽  
Vol 4 (3) ◽  
pp. 181-187 ◽  
Author(s):  
Minoru Kumakura ◽  
Isao Kaetsu
Keyword(s):  
Enzyme Activity ◽  
Polymer Matrix ◽  
Active Site ◽  
Immobilized Enzyme ◽  
Monomer Concentration ◽  
Radiation Polymerization ◽  
Immobilization Of Enzymes ◽  
Repeated Batch

We studied the effect of immobilizing cellulase to carboxycellulose sodium by radiation polymerization on the masking of the active site of the enzyme. Masking of the enzyme during the preparation of immobilized enzyme was assayed at tow temperature. The activity of immobilized enzyme was retained during repeated batch reactions, indicating that the enzyme was firmly trapped in the polymer matrix. Various compounds (designated monomers) were used to dissolve the carboxymethylcellulose; enzyme activity was affected by the nature of the monomer, by the monomer concentration, and by the solubility of the substrate in monomer.

Effect of the hydrophilicity of the polymer matrix on immobilized α-chymotrypsin

1984 ◽  
Vol 49 (6) ◽  
pp. 1552-1556
Author(s):  
Minoru Kumakura ◽  
Isso Kaetsu
Keyword(s):  
Thermal Stability ◽  
Enzyme Activity ◽  
Pore Size ◽  
Polymer Matrix ◽  
Low Temperatures ◽  
Radiation Polymerization ◽  
Thermal Stability Of

α-Chymotrypsin was immobilized by radiation polymerization at low temperatures and the effect of the hydrophilicity of the polymer matrix on the enzyme activity and thermal stability was studied. The activity and thermal stability of immobilized chymotrypsin increased with the increasing hydrophilicity of the polymer matrix or monomer. The thermal stability was affected by the form and pore size of the polymer matrix; chymotrypsin immobilized on a soft-gel polymer matrix exhibited an enhanced thermal stability.

scholarly journals Effects of morphology and pore size of mesoporous silicas on the efficiency of an immobilized enzyme

RSC Advances ◽  
2021 ◽  
Vol 11 (17) ◽  
pp. 10010-10017
Author(s):  
Ping-Chung Kuo ◽  
Zhi-Xun Lin ◽  
Tzi-Yi Wu ◽  
Chun-Han Hsu ◽  
Hong-Ping Lin ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Mesoporous Silica ◽  
Pore Size ◽  
Immobilized Enzyme ◽  
Mesoporous Silicas ◽  
High Loading ◽  
Loading Capacity ◽  
Silica Films

Mesoporous silica films were used as supports with high loading capacity and enzyme activity.

Acid phosphatase, alkaline phosphatase, and nitrate reductase activity of selected ectomycorrhizal fungi

1989 ◽  
Vol 67 (3) ◽  
pp. 750-753 ◽  
Author(s):  
Iwan Ho
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Nitrate Reductase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Phosphatase Alkaline

Seventeen isolates, encompassing five genera and eight species of ectomycorrhizal fungi, were compared for acid phosphatase, alkaline phosphatase, and nitrate reductase activity. Isolates within species differed in enzyme activity and isozyme patterns by host specificity and site (as exemplified by the genus Suillus). Host and site may have affected phosphatase enzyme activity. Generally, the Douglas-fir associates, which dominate in mesic sites, have higher acid phosphatase activity than pine associates, which mostly occupy xeric sites; however, pine associates from mesic sites also have higher acid phosphatase activity (e.g., S. tomentosus). In four isolates of Amanita muscaria, the effect of site was also apparent. Two of them, which have significantly higher acid phosphatase activity than the others, were isolated from mesic sites. The isozyme pattern of the genus Suillus appeared to be separated by host groups. Other isolates with only one species also differed more or less by host groups. They shared at least one band within host groups, except for the two isolates of Paxillus involutus from different hosts. The P. involutus S-403 isolated from an orchard showed much higher nitrate reductase activity than all other isolates. No apparent differences in nitrate reductase activity were found between the other isolates.

Electron transfer between a quinohemoprotein alcohol dehydrogenase and an electrode via a redox polymer network

1996 ◽  
Vol 18 (7) ◽  
pp. 489-494 ◽  
Author(s):  
E.C.A. Stigter ◽  
G.A.H. de Jong ◽  
J.A. Jongejan ◽  
J.A. Duine ◽  
J.P. van der Lugt ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Alcohol Dehydrogenase ◽  
Polymer Network ◽  
Redox Polymer

Unravelling electron transfer processes at photosystem 2 embedded in an Os-complex modified redox polymer

2018 ◽  
Vol 290 ◽  
pp. 451-456 ◽  
Author(s):  
Fangyuan Zhao ◽  
Volker Hartmann ◽  
Adrian Ruff ◽  
Marc M. Nowaczyk ◽  
Matthias Rögner ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Photosystem 2 ◽  
Redox Polymer ◽  
Transfer Processes ◽  
Electron Transfer Processes
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