Abstract

Combined effects of pH-shifting and an autoclaving cycle (121 °C, 15 min) on red kidney bean lectin (RKBL) were investigated using intrinsic and extrinsic fluorescence, UV, FTIR, DSC, SEC, dot-blot analysis and in vitro digestibility. Spectroscopic studies suggested that the protein refolding was stable after 3 h incubation with the hydrophobic exposure after pH-shifting, and hydrophobicity was significantly increased with the formation of more looser structure, which would influence the structural stability of known epitopes. In details, the increase of β-turn and reduction of random coil was related with the lower denaturation enthalpy, while the protein aggregation was also observed in acidic treated samples after autoclaving. Lower antigenicity and good digestibility suggested the exposure of enzyme cutting sites, and confirmed the effectivity of pH-shifting prior to the autoclaving. Then the results would be beneficial to the development of hypoallergenic kidney bean foods.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.