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Specific Disulfide Bond in α‐Lactalbumin Infiuences Heat‐ Induced Gelation of α‐Lactalbumin‐Ovalbumin‐Mixed Gels
Author(s) -
LEGOWO ANANG MOHAMAD,
IMADE TAMOTSU,
YASUDA YUKINORI,
OKAZAKI KATSUICHIRO,
HAYAKAWA SHIGERU
Publication year - 1996
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1996.tb14176.x
Subject(s) - ovalbumin , lactalbumin , chemistry , disulfide bond , chromatography , biochemistry , immunology , antigen , biology
The gel strength of ovalbumin mixed with α‐lactalbumin (α‐La) was determined after heating at 80°C for 15 min at pH 7.0 Gel strength of the mixture of 4%α‐La and 4% ovalbumin was two times that of 8% ovalbumin. Modified α‐La at Cys6‐Cys120 (3 SSα‐La) had low enhancement effects on ovalbumin gelation. Competitive ELISA using monoclonal antibody to α‐La showed decreased binding reactivities after heating α‐La with ovalbumin at specific concentrations. The decrease of total SH groups in the gel mixed with 3SS α‐La was much less than when mixed with α‐La. A disulfide bond of Cys6‐Cys120 in α‐La contributed to interactions between ovalbumin and α‐La in heat‐induced gels.