Abstract
ABSTRACT The thermodynamic parameters of heat denaturation of (β-lactoglobulin solutions (2.5 ≤ pH ≤ 8) are determined by differential scanning calorimetry and the rheological properties of heat induced gels are studied in compression with an Instron Universal Testing machine. The emulsifying activity index is determined by a turbidimetric method and by calculation from the globule size distribution measured by laserdiffraction. The thermal stability of the protein, evaluated from the denaturation temperature, is maximum at the isoelectric pH in citric acid/NaOH buffer and at pH 3.5 in distilled water. The incipient gelation temperatures is compared to the denaturation temperatures TS, determined from the onset of increase of the heat flow which are slightly lower than the gelation temperatures, except at pH 4.8 and at pH 8 where they are higher or equal, respectively. The emulsifying activity index is relatively low at pHs ≤ 4.8 and it increases with higher pHs. The results are discussed in terms of free...
Sign-in/Register to access full text options 
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 callDisclaimer: 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.
