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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
  • *Bu çalışma için yazışmadan sorumlu yazar

Araştırma sonucu: Dergiye katkıMakalebilirkişi

43 Atıf (Scopus)

Özet

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.

Orijinal dilİngilizce
Sayfa (başlangıç-bitiş)146-156
Sayfa sayısı11
DergiJournal of Industrial and Engineering Chemistry
Hacim38
DOI'lar
Yayın durumuYayınlandı - 25 Haz 2016
Harici olarak yayınlandıEvet

Bibliyografik not

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

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