Specific Disulfide Bond in α‐Lactalbumin Infiuences Heat‐ Induced Gelation of α‐Lactalbumin‐Ovalbumin‐Mixed Gels

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.