Comparison of bovine serum albumin adsorption capacities of α-chitin isolated from an insect and β-chitin from cuttlebone

Murat Kaya*, Idris Sargin, Volkan Aylanc, Muhammed Nebi Tomruk, Seda Gevrek, Isil Karatoprak, Nazlican Colak, Yasar Gul Sak, Esra Bulut

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)146-156
Number of pages11
JournalJournal of Industrial and Engineering Chemistry
Volume38
DOIs
Publication statusPublished - 25 Jun 2016
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2016 The Korean Society of Industrial and Engineering Chemistry.

Keywords

  • Biopolymer
  • Blood protein
  • BSA
  • Characterization
  • Extraction

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