Abstract
Bovine serum albumin is the key protein in blood. Chitin is a widely used biocompatible polymer in bioengineering and it is mainly found as two allomorphs (α, β). In this study the interactions of α-chitin (from the insect Omophlus sp.) and β-chitin (from the cuttlebone of Sepia sp.) with BSA were studied. Chitin isolates were examined by SEM, XRD, BET, TGA and FTIR. β-Chitin exhibited a far higher affinity for BSA than α-chitin, indicating α-chitin can be used in applications where surface–protein interactions should be limited, and β-chitin can be used in chitin-based materials on which protein adsorption is desired.
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