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Electrochemical evaluation of lactate dehydrogenase immobilized in polyacrylamide gels
Author(s) -
Chen A. K.,
Liu C. C.
Publication year - 1977
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260191205
Subject(s) - ferricyanide , lactate dehydrogenase , ferrocyanide , chemistry , nicotinamide adenine dinucleotide , nad+ kinase , polyacrylamide , electrochemistry , dehydrogenase , aqueous solution , chromatography , immobilized enzyme , platinum , inorganic chemistry , nuclear chemistry , biochemistry , enzyme , electrode , catalysis , organic chemistry , polymer chemistry
Lactate dehydrogenase (EC 1.1.1.27) has been immobilized in polyacrylamide gels over a platinum grid matrix. The immobilized enzyme is used to oxidize L ‐lactate in the presence of nicotinamide adenine dinucleotide (NAD + ) and femcyanide. The NADH produced is then chemically oxidized back to NAD + by ferricyanide. The coupled reduction of ferricyanide ions to ferrocyanide ions results in a measurable electrochemical potential. This measurable zero‐current potential is found to be Nernstian in nature and directly proportional to the logarithm values of L ‐Iactate concentration over the range of 2 × 10 −5 to 5 × 10 −2 M . The results indicate that immobilized lactate dehydrogenase can be incorporated into a system to detect L ‐Lactate acid in aqueous solutions.
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