Abstract:The in situ cross-linking reaction of β-lactoglobulin (β-LG) induced by microbial transglutaminase (MTGase) was investigated using size-exclusion chromatography (SEC) combined with multi-angle laser light scattering (MALLS). The results indicated that, in the presence of 20 mM dithiothreitol (DTT), the MTGase treatment up to about 11 h gradually resulted in the formation of biopolymers or oligomers with higher molecular weight (MW), and the transformation of dimeric form of β-LG to its monomeric form. This transformation was also observed in the absence of DTT. These data suggested that MTGase treatment could be utilized as a potential technique to modulate the thermal stability of many globular proteins.
