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Catalysis of linoleate oxidation by copper‐proteins
Author(s) -
Tappel A. L.
Publication year - 1955
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02634456
Subject(s) - copper , chemistry , hemocyanin , catalysis , conjugated diene , allylic rearrangement , copper protein , peroxide , conjugated system , bovine serum albumin , albumin , organic chemistry , biochemistry , polymer , monomer , antigen , biology , genetics
Summary Copper‐proteins formed by the binding of copper ions to conalbumin, serum albumin, or caseinate are more effective catalysts for linoleate oxidation than is copper alone. The main product is conjugated diene linoleate hydroperoxide. Hemocyanin shows similar catalytic activity. The increase in linoleate oxidation catalysis of copper‐proteins compared to ionic copper is ascribed to increased ease of formation and increased stability of the intermediate complex of linoleate peroxide‐copper‐protein.