Covalent attachment of lysozyme to cotton/cellulose materials: protein verses solid support activation |
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Authors: | J Vincent Edwards Nicolette T Prevost Brian Condon Alfred French |
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Institution: | (1) Southern Regional Research Center, USDA-ARS, 1100 Robert E. Lee Blvd., New Orleans, LA 70124, USA |
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Abstract: | Covalent attachment of enzymes to cellulosic materials like cotton is of interest where either release or loss of enzyme activity
over time needs to be avoided. The covalent attachment of an enzyme to a cellulosic substrate requires either activation of
a protein side chain or an organic functional group on the cellulosic substrate. Use of a water soluble carbodiimide to create
an amide linkage as the covalent attachment between the enzyme and substrate represents an aqueous-based alternative which
may be preferred for textile processes. Here we describe an amide bond-mediated lysozyme immobilization applied to cotton
where either the carboxylate side chains of the protein or pendant carboxylates in a citrate, cross-linked cotton support
are activated as the O-acyl-isourea intermediate, and the reactive amino nucleophiles are derived from amino-silanized cotton
and the protein’s amino side chains, respectively. A comparison is made of the two activation approaches to covalently link
lysozyme to two different cotton fabrics using the water soluble carbodiimide 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide-metho-p-toluene
sulfonate. A comparison of the resulting enzyme activities of lysozyme on two different cotton supports showed that linking
lysozyme to citrate crosslinked cotton gave higher activity than on aminosilanized cotton. The lysozyme-cellulose conjugate
formed on the citrate crosslinked nonwoven cotton fabric gave the highest yield and antimicrobial activity. |
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