Abstract
Transglutaminase (TGase) has high value to the field of food processing due to their protein cross-linking capacity. Compared with the widely used TGase from Streptococcus mobaraensis (MTG), Bacillus subtilis-derived TGase (BTG) exhibits higher thermal stability and broader range of pH, and is thus better suitable to food processing conditions. However, BTG's cross-linking preferences and characteristics are still unclear, restricting the application in food process. In this study, a modified in vitro RNA display was used to efficiently screen BTG's peptide substrates with a high library capacity. The results showed that BTG preferred to cross-link the Q sites around which were hydrophobic residues in the substrate sequences. LC-MS analysis validated that the top five screened peptides indeed showed high cross-linking rates by BTG. Moreover, the molecular dynamics simulation indicated that their binding affinity with BTG was mainly due to van der Waals interaction, which explained the cross-linking preference of BTG on the substrate. This study provided knowledge about BTG's cross-linking preference and characteristics, which will benefit the comprehensive understanding of BTG and promote its rational application in food industry.
Published Version
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