Abstract:

Ultraviolet (UV) spectroscopy, fluorescence spectroscopy and SDS-PAGE were used to measure changes in
the physio-chemical properties and structure of chicken sarcoplasmic proteins after ultrasonic treatment. Results indicated
that ultrasonic power and treatment time exhibited great effects on the emulsifying properties, forming properties, surface
hydrophobicity and intrinsic fluorescence properties of chicken sarcoplasmic proteins. As ultrasonic power and treatment
time increased, the emulsifying capacity of chicken sarcoplasmic proteins decreased, and emulsion stability and foam
stability increased initially and then decreased. However, an opposite effect of ultrasonic treatment time was observed the
emulsifying properties and forming properties of chicken sarcoplasmic proteins. Moreover, the surface hydrophobicity
and intrinsic fluorescence intensity became enhanced after ultrasonic treatment, but the UV spectra and molecular weight
presented no obvious changes. These observations illustrate that ultrasonic exposure can not lead to fragmentation of peptide
bonds in chicken sarcoplasmic proteins.

Key words: ultrasonic, sarcoplasmic proteins, ultraviolet, fluorescence, emulsifying properties, forming properties