Title
The investigation of protein flexibility of various soybean cultivars in relation to physicochemical and conformational properties
Year
2020
Journal
Food Hydrocolloids
Abstract
The conformation and physicochemical attributes of proteins play important roles in determining their flexibility. This study investigates the structural flexibility of twelve different soybean proteins. Results suggest that
amino acids not only affects protein flexibility but its spatial structure as well. In addition, β-conglycinin protein
contained more flexible subunits than glycinin. The HN-87, HN-48, HH-44 and HH-53 proteins were more
flexible with lower α-helix content. Other key factors that influence higher structural flexibility include higher
surface hydrophobicity and fewer disulfide bonds. Furthermore, more flexible proteins ensured the unfolding of
the polypeptide chain backbone and endowed them with excellent emulsifying characteristics. In all, flexible
proteins showed stronger surface activity than rigid ones. These findings thus provide clear evidence on the
structural flexibility-functional properties interactions of different soybean proteins.
Instrument
J-815
Keywords
Circular dichroism, Protein folding, Secondary structure, Food science, Biochemistry