Enzymatic grafting of lactoferrin onto silk fibroins for antibacterial functionalization

Abstract

Enzymatic oxidation of tyrosine side-chains in proteins could produce reactive o-quinones that might subsequently react with the primary amino groups of functional compounds, which provided a worthwhile reference for functionalization of fibrion materials. In the present work the potential for using tyrosinase to graft the bovine lactoferrin onto Bombyx mori silk fibroin was examined. Lactoferrin could adsorb onto silk fibers and covalently bind to the previous enzymatically oxidized fibroin surface. The enzyme-generated quinones in silk fibers also might cause self-crosslinking of fibroin peptides, which led to beneficial changes of silk properties. For the fabric treated with tyrosinase and lactoferrin slight improvements of dyeability and strength were obtained in comparison to the control. The combinedly treated fabric showed encouraging resistance to S. aureus and E. coli, the antibacterial activities reached to 87.0 % and 76.4 %, respectively. The durability of the antibacterial silk was noticeably higher than that of the sample treated with lactoferrin alone.