Search

• The structure of PPI became more disordered after multiple F-T cycles. • F-T cycles could effectively improve the emulsification property of PPI. • The changes of PPI structure and functional properties depended on F-T cycles times. This study investigated changes of the structure and emulsifying properties of peanut protein isolate (PPI) during multiple freeze-thaw (F-T) cycles. According to the Fourier transform infrared spectrum, the F-T treatment to PPI reduced the content of protein ordered structure significantly. The result of fluorescence spectrum revealed that the polarity of PPI surroundings first increased and then decreased. Similarly, the free sulfhydryl content and surface hydrophobicity of PPI increased firstly and decreased. However, the carbonyl content and particle size of PPI increased continuously after F-T treatment. The emulsification performance of PPI after F-T treatment was significantly improved. The emulsion prepared by PPI after 3 F-T cycles had the smallest mean particle size, the highest absolute value of zeta-potential and the most uniform microstructure distribution, showed the best performance of emulsifying ability. Therefore, it can be known that F-T cycles treatment could effectively change protein structure and improve protein emulsifying properties. [ABSTRACT FROM AUTHOR]

The conjugates of black bean protein isolate (BBPI) and glucose (G) were prepared via the wet heating Maillard reaction with ultrasound pretreatment. The physicochemical properties of UBBPI-G conjugates prepared by ultrasound pretreatment Maillard reaction had been compared with classical Maillard reaction (BBPI-G). The reaction rate between BBPI and glucose was speeded up by ultrasound pretreatment. A degree of glycation (DG) of 20.49 was achieved by 2 h treatment for UBBPI-G, whereas 5 h was required using the classical heating. SDS-PAGE patterns revealed that the BBPI-G conjugates with higher molecular weight were formed after glycosylation. The results of secondary structure analysis suggested that the α-helix and β-sheet content of UBBPI-G were lower than that of BBPI-G. In addition, UBBPI-G conjugates had exhibited bathochromic shift compared with BBPI by fluorescence spectroscopy analysis. Finally, UBBPI-G achieved higher level of surface hydrophobicity, solubility, emulsification property and antioxidant activity than BBPI and BBPI-G (classical Maillard reaction). [ABSTRACT FROM AUTHOR]