Study Of The Dynamic High Pressure Microfluidization On Modification And Mechanism Of Ovalbumin

Ovalbumin, the main components of egg, is a quality protein. However, because of some imperfect functional properties, cause the application of ovalbumin is limited in the food processing industry, it should be improved further to develop and utilize. The dynamic ultra high pressure micro-fluidization technology is a set of transportation, mixed, superfine, grinding, pressure and other units operation in one physical modification. The technology can change the structures of ovalbumin, then lead to the changes of its functional properties. So in this paper, the changes of functional properties and structure of ovalbumin treated by micro-fluidization is studied and the mechanism of modification is discussed. This paper offered a new method with the protein modification, meanwhile, provided a theoretical basis for improving the functional properties of protein research and development in the application of micro-fluidization. The experimental results were as follows:1. Micro-fluidization technology greatly improved the solubility, retention ability, foaming capability, gel property of ovalbumin, the emulsibility and emulsibility stability properties of 4% and 6% ovalbumin protein increases after treatment, while 8% ovalbumin protein decreases. The rheological property of ovalbumin decreases and the flow pattern of different concentration protein are different.2. The apparent structure and crystal structure of ovalbumin by micro-fluidization will be destroyed. The protein polymer was broken up; molecular weight is no changes; the -SH content of ovalbumin increased with the pressure increasing; surface hydrophobicity increased and the maximum absorption wavelength blue shift slightly; fluorescence intensity decreased at 160MPa; the surface amino acid of absorbing UV decreased; the peak temperature decreased, the thermal stability of ovalbumin became worse at 160MPa and under other pressures, the peak temperature enhanced in varying degrees and the thermal stability increased.3. The analysis results of the FT-IR and CD spectrum indicated the secondary structure of ovalbumin is changed by micro-fluidization treatment. The amide I bands blue shift. The absorption of amide I and amide II bands increased. The content of α-helix and random coil increased, where asβ-sheet content decreased. It can beconjectured that the unfolded structure of ovalbumin was changed bymicro-fludization.4. The mechanism of the modification of micro-fluidization on ovalbumin isdiscussed by combining the relation between structure and functional properties ofovalbumin.