Abstract
ABSTRACT Effects of high pressure processing on conformational changes of soybean β‐conglycinin was studied by means of sulfhydryl groups detection, spectrofluorimetry, ultraviolet difference spectra, circular dichroism and electrophoresis. Significantly more sulflhydryl groups as well as hydrophobic regions and amino acid residues, which had ultraviolet absorbance had been found after high pressure processing (≥300 MPa). The CD analysis indicated that some of the ordered structures ofα‐helix andβ‐structure were destroyed and converted to random coil after processing at 500 MPa for 10 min. Electrophoresis analysis revealed that β‐conglycinin could be denatured and might be dissociated into subunits after high pressure processing (≥300 MPa).PRACTICAL APPLICATIONSThe use of high pressure for food processing is now getting an increasing interest in the food industry because of the consumer's demand for convenience foods of the highest quality in terms of natural flavor and taste, and which are free from additives and preservatives. It is a possible alternative to temperature treatment. Soybean proteins play an important role in food consumption worldwide. The objectives of this study were to reveal the conformational changes of soybean β‐conglycinin after high pressure processing. The results will help the application of high pressure technology in soybean protein processing.
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