Structure and antioxidant activity of β-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions

2013 ◽  
Vol 138 (1) ◽  
pp. 590-599 ◽  
Author(s):  
Dragana Stanic-Vucinic ◽  
Ivana Prodic ◽  
Danijela Apostolovic ◽  
Milan Nikolic ◽  
Tanja Cirkovic Velickovic
Keyword(s):  
Antioxidant Activity ◽  
Maillard Reaction ◽  
High Intensity ◽  
Model Systems ◽  
High Intensity Ultrasound ◽  
Neutral Conditions ◽  
Β Lactoglobulin

scholarly journals Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin

Molecules ◽  
2020 ◽  
Vol 25 (16) ◽  
pp. 3637
Author(s):  
Xinhui Zhou ◽  
Cuina Wang ◽  
Xiaomeng Sun ◽  
Zixuan Zhao ◽  
Mingruo Guo
Keyword(s):  
Thermal Stability ◽  
Structural Properties ◽  
High Intensity ◽  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Goat Milk ◽  
High Intensity Ultrasound ◽  
Hydrophobicity Index ◽  
Β Lactoglobulin

This study aimed to compare the effects of high intensity ultrasound (HIU) applied at various amplitudes (20~40%) and for different durations (1~10 min) on the physiochemical and structural properties of goat milk β-lactoglobulin. No significant change was observed in the protein electrophoretic patterns by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Deconvolution and second derivative of the Fourier transform infrared spectra (FTIR) showed that the percentage of β-sheet of goat milk β-lactoglobulin was significantly decreased while those of α-helix and random coils increased after HIU treatment The surface hydrophobicity index and intrinsic fluorescence intensity of samples was enhanced and increased with increasing HIU amplitude or time. Differential scanning calorimetry (DSC) results exhibited that HIU treatments improved the thermal stability of goat milk β-lactoglobulin. Transmission electron microscopy (TEM) of samples showed that the goat milk β-lactoglobulin microstructure had changed and it contained larger aggregates when compared with the untreated goat milk β-lactoglobulin sample. Data suggested that HIU treatments resulted in secondary and tertiary structural changes of goat milk β-lactoglobulin and improved its thermal stability.

Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound

2012 ◽  
Vol 56 (12) ◽  
pp. 1894-1905 ◽  
Author(s):  
Dragana Stanic-Vucinic ◽  
Marija Stojadinovic ◽  
Marina Atanaskovic-Markovic ◽  
Jana Ognjenovic ◽  
Hans Grönlund ◽  
...  
Keyword(s):  
High Intensity ◽  
Structural Changes ◽  
High Intensity Ultrasound ◽  
Β Lactoglobulin
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