Cover illustration Introduction of hydrophilic polypeptides to soybean proglycinin A1aB1b and A2B1a C-termini resulted in intrinsic solubility profiles, a small change in thermal stability and surface hydrophobicity, and improvement of both emulsifying abilities and emulsion stabilities of the proteins.The improvement of the emulsion properties was based on the length and hydropathy profile of the polypeptides that were introduced to the C-termini of the proteins. Among all the introduced peptides, the α extension region was the best polypeptide for the improvement of the emulsion stability of the proteins at low ionic strength (I=0.08). Here is the crystal structure of proglycinin A1aB1b where the dashed lines represent the disordered regions and all the introduced peptides were attached to a dashed line in pink color (C-terminus). For further details please see Prak et al. pp. 433-422.
[Table of Contents]