Premium
Oxidatively induced chemical changes and interactions of mixed myosin, β‐lactoglobulin and soy 7S globulin
Author(s) -
Liu Gang,
Xiong Youling L
Publication year - 2000
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/1097-0010(20000901)80:11<1601::aid-jsfa685>3.0.co;2-o
Subject(s) - myosin , chemistry , globulin , biochemistry , food science , biology , immunology
The effects of oxidation on the chemical characteristics of myosin, β‐lactoglobulin and soy 7S globulin were investigated in a free radical‐generating system (FeCl 3 /H 2 O 2 /ascorbate). Oxidised myosin exhibited a marked increase (>10‐fold) in carbonyls, a small increase in amines and conversion of some free sulphhydryls to disulphide bonds. Oxidised β‐lactoglobulin and 7S globulin also showed a major increase in the carbonyl content (five‐ and threefold respectively), but other chemical changes were relatively minor. In the oxidised myosin/β‐lactoglobulin composites, some cross‐linked aggregates were formed. Aggregation was also evidenced in the myosin/7S globulin composites exposed to the oxidising agents. The results indicated that oxidation enhanced interactions of the non‐muscle proteins with myosin apparently through the modification of amino acid side chains. These physicochemical changes may influence the functionality of processed muscle foods. © 2000 Society of Chemical Industry