Deriden kollajen ve jelatinin saflaştırılması ve elde edilen protein materyallerinin karakterizasyonu
Küçük Resim Yok
Tarih
2010
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Bu çalışmada genç dana derilerinden pepsin enzimi kullanarak asetik asitte çözünür kollajen izole edilerek saflaştırılması yapılmıştır. Kollajen haricinde dana derilerinden alkali enzimatik yöntemle jelatin eldesi de gerçekleştirilmiştir. Saflaştırılan kollajen ve jelatin örneklerinde yapı karakterizasyonu için FTIR tayini yapılmış, kollajen örneğinde ilave olarak molekül ağırlığı tespiti için SDS PAGE analizi de gerçekleştirilmiştir. Elde edilen kollajen ve jelatin çözeltilerinden liyofilizatör ve sprey kurutucu ile toz formda, glutardialdehıt ile çapraz bağlanma suretiyle de film olarak kollajen bazlı materyaller elde edilmiştir. FTIR ve SDS PAGE sonuçları elde edilen kollajen çözeltisi içerisinde heliks yapının varlığını doğrulamıştır. Toz formdaki kollajen örneğinde morfolojik yapılarının belirlenmesi amacıyla Masa Üstü Taramalı Elektron Mikroskopu (Table Top SEM) kullanılmış ve poröz bir ağ yapısının olduğu ortaya konmuştur. Genç dana derilerinden izole edilen kollajen ve jelatin bazlı materyallerin gerekli toksikolojik analizlerinin yapılmasının ardından biyomedikal, kozmetik, eczacılık vb. birçok alanda kullanıma uygun olduğu sonucuna varılmıştır.
In the present study acetic acid soluble collagen was purified by isolation from young calfskins by using pepsin as enzyme. In addition, gelatin was also purified from the skins by using alkaline enzyme procedures. The structural characterization of collagen and gelatin samples was performed by FTIR and molecular weight of the purified collagen was also determined by SDS PAGE method. Coilagenic materials in powder form were prepared by freeze drying of collagen solution and sprey drying of gelatin solution. Coilagenic films were also prepared from the solutions after crosslinking by glutardialdehyde. FTIR and SDS PAGE analyses verified the helix structure of obtained collagen. Table Top Scanning electron microscopical (Table Top SEM) studies performed on powder collagen samples for assessing the morphology exhibited a fibrilar network with a porous structure. The coilagenic materials obtained from young calf skins were considered to be proper for use in biomedical, cosmetic, pharmaceutical applications etc. after carrying out neccesary toxicological tests.
In the present study acetic acid soluble collagen was purified by isolation from young calfskins by using pepsin as enzyme. In addition, gelatin was also purified from the skins by using alkaline enzyme procedures. The structural characterization of collagen and gelatin samples was performed by FTIR and molecular weight of the purified collagen was also determined by SDS PAGE method. Coilagenic materials in powder form were prepared by freeze drying of collagen solution and sprey drying of gelatin solution. Coilagenic films were also prepared from the solutions after crosslinking by glutardialdehyde. FTIR and SDS PAGE analyses verified the helix structure of obtained collagen. Table Top Scanning electron microscopical (Table Top SEM) studies performed on powder collagen samples for assessing the morphology exhibited a fibrilar network with a porous structure. The coilagenic materials obtained from young calf skins were considered to be proper for use in biomedical, cosmetic, pharmaceutical applications etc. after carrying out neccesary toxicological tests.
Açıklama
Anahtar Kelimeler
Malzeme Bilimleri, Tekstil
Kaynak
DERİ BİLİM
WoS Q Değeri
Scopus Q Değeri
Cilt
4
Sayı
2
