Kaya, MuratSargın, İdrisAylanç, VolkanTomruk, Muhammed NebiGevrek, SedaKaratoprak, IşılÇolak, NazlıcanSak, Yaşar GülBulut, Esra13.07.20192019-07-2913.07.20192019-07-2920161226-086X1876-794Xhttps://doi.org/10.1016/j.jiec.2016.04.015https://hdl.handle.net/20.500.12451/5969Bovine 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 (alpha, beta). In this study the interactions of alpha-chitin (from the insect Omophlus sp.) and beta-chitin (from the cuttlebone of Sepia sp.) with BSA were studied. Chitin isolates were examined by SEM, XRD, BET, TGA and FFIR. beta-Chitin exhibited a far higher affinity for BSA than alpha-chitin, indicating alpha-chitin can be used in applications where surface-protein interactions should be limited, and beta-chitin can be used in chitin-based materials on which protein adsorption is desired.eninfo:eu-repo/semantics/closedAccessBiopolymerExtractionBlood ProteinCharacterizationBSAArticle3814615610.1016/j.jiec.2016.04.015Q1WOS:000378451600017N/A