Amperometric Biosensor Based on Enzyme Immobilization with Post Process for Medical and Multiple Applications

2014 ◽  
Vol 47 (8) ◽  
pp. 1361-1374 ◽  
Author(s):  
Tomoko Gessei ◽  
Takahiro Arakawa ◽  
Hiroyuki Kudo ◽  
Hirokazu Saito ◽  
Kohji Mitsubayashi
Keyword(s):  
Enzyme Immobilization ◽  
Amperometric Biosensor ◽  
Post Process

Development of a new amperometric biosensor based on polyphenoloxidase and polyethersulphone membrane

2001 ◽  
Vol 73 (12) ◽  
pp. 1993-1999 ◽  
Author(s):  
P. V. Climent ◽  
M. L. M. Serralheiro ◽  
M. J. F. Rebelo
Keyword(s):  
Phenolic Compounds ◽  
Response Time ◽  
Enzyme Immobilization ◽  
Platinum Electrode ◽  
Enzymatic Catalysis ◽  
Amperometric Biosensor ◽  
Catecholase Activity

An amperometric biosensor based on the enzyme polyphenoloxidase (PPO), which makes the bioelectrocatalysis of phenolic compounds, was developed and optimized using cathecol as substrate. Polyethersulphone membranes were used for enzyme immobilization. Polyphenoloxidase oxidizes monophenols (cresolase activity) and diphenols (catecholase activity) into the corresponding o-quinones; the o-quinones formed in the enzymatic catalysis are then reduced back to cathecol at ­200 mV (vs. Ag, AgCl) at a platinum electrode. The polyphenoloxidase immobilized was from commercial origin or extracted from mushrooms. p-Cresol and phenol substrates were also tested. Reproducibility, response time, linearity, sensitivity, and stability of the biosensor were studied.

Development of a bienzymatic amperometric biosensor to determine uric acid in human serum, based on mesoporous silica (MCM-41) for enzyme immobilization

2014 ◽  
Vol 195 ◽  
pp. 58-62 ◽  
Author(s):  
Rodolfo Mundaca-Uribe ◽  
Francisca Bustos-Ramírez ◽  
Claudio Zaror-Zaror ◽  
Mario Aranda-Bustos ◽  
Jose Neira-Hinojosa ◽  
...  
Keyword(s):  
Uric Acid ◽  
Mesoporous Silica ◽  
Human Serum ◽  
Enzyme Immobilization ◽  
Amperometric Biosensor ◽  
Mcm 41

Bifunctional Langmuir-Blodgett film for enzyme immobilization and amperometric biosensor sensitization

1991 ◽  
Vol 202 (1) ◽  
pp. 145-150 ◽  
Author(s):  
Tetsu Tatsuma ◽  
Hirohiko Tsuzuki ◽  
Yusuke Okawa ◽  
Shoichiro Yoshida ◽  
Tadashi Watanabe
Keyword(s):  
Enzyme Immobilization ◽  
Amperometric Biosensor ◽  
Blodgett Film ◽  
Langmuir Blodgett ◽  
Langmuir Blodgett Film

Environmentally Friendly Preparation of Magnetic Composites Featuring Proteolytic Properties

INEOS OPEN ◽  
2020 ◽  
Author(s):  
N. A. Samoilova ◽  
Keyword(s):  
Enzyme Immobilization ◽  
Maleic Acid ◽  
Environmentally Friendly ◽  
Synthetic Polymer ◽  
Magnetic Composites ◽  
Interpolyelectrolyte Complex ◽  
Hydrolysis Rates ◽  
Poly Ethylene ◽  
Noncovalent Binding

The enzyme-containing magnetic composites are presented. The magnetic matrix for enzyme immobilization is obtained by sequential application of an amine-containing polysaccharide—chitosan and a synthetic polymer—poly(ethylene-alt-maleic acid) to the magnetite microparticles to form the interpolyelectrolyte complex shell. Then, the enzyme (trypsin) is immobilized by covalent or noncovalent binding. Thus, the suggested composites can be readily obtained in the environmentally friendly manner. The enzyme capacity of the resulting composites reaches 28.0–32.6 mg/g. The maximum hydrolysis rates of the H-Val-Leu-Lys-pNA substrate provided by these composites range within 0.60·10–7–0.77·10–7 M/min.

Instrumentation system for amperometric biosensor

2011 ◽  
Vol 1 (10) ◽  
pp. 49-51
Author(s):  
Chethan .G Chethan .G ◽  
◽  
Saurav Pratap Singh ◽  
Dr. Padmaja .K.V Dr. Padmaja .K.V ◽  
Dr. Prasanna kumar .S.C Dr. Prasanna kumar .S.C
Keyword(s):  
Amperometric Biosensor

Biocatalytic Ketone Reductions Using Biobeads

2020 ◽  
Author(s):  
Jia Shen Chew ◽  
Ken Chi Lik Lee ◽  
THI THANH NHA HO
Keyword(s):  
Enzyme Immobilization ◽  
High Throughput ◽  
High Throughput Screening ◽  
Chiral Hplc ◽  
Micro Scale

<p>Lee and coworkers offers a kind of new concept to enzyme immobilization and explores its suitability in the context of miniaturisation and high-throughput screening. Here, polystyrene-immobilized ketoreductases are compared with its non-immobilized counterparts in terms of conversion and stereoselectivity (both determined by chiral HPLC), and the study indicates that the BioBeads perform similarly (sometimes slightly more selective) which may be useful whenever defined micro-scale amounts of biocatalysts were required in high-throughput experiment settings.</p>

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