Isolation and characterization of collagen of hybrid tilapia skin (black tilapia (Oreochromis mossambicus) × red tilapia (Oreochromis nilotica))

• Main Authors: Chun-Kai Fang, 方俊凱
• Other Authors: Rong-Huei Chen
• Format: Others
• Language: zh-TW
• Published: 2006
• Online Access: http://ndltd.ncl.edu.tw/handle/48537822513657475053

碩士 === 國立臺灣海洋大學 === 食品科學系 === 94 === The aim of this study was to establish the isolation conditions to characterize the physical and properties of collagen from the skin waste material of hybrid tilapia (black tilapia (Oreochromis mossambicus) cross red tilapia (Oreochromis nilotica)) by solvent extraction. The physical-chemical properties include amino acid analysis, circular dichroism (CD) , sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), denaturation temperture (Td) to characterize, and thermal denaturation temperature of hybrid tilapia skin collagen. The results showed that hybrid tilapia collagen have no cystine, it indicated that telopeptide was removd. Proline and hydroxyproline contents in hybrid tilapia collagen is 20%. Hydroxyproline and hydroxylysine were oxidized hydroxylation a medium with compare to other fish species. SDS-PAGE include the molecular weight of the band were at 100 kDa, 150 kDa and 250 kDa. composed of α1, α2 momomer , β dimmer, and γ trimer. No bands of molecular weight less than 50 Kda showed the telopeptide right have been removed because it has two α1 and one α2 band only. CD is use to collagen triplehelix ratio measurement is 80.4%, The Td (denature temperature) in hybrid tilapia is 33.2 ℃ with no ion influence. The range of Melting temperature(Tm) is 10-11℃. At FTIR (Fourier transform infrared) show The positions of amide bands A Merged around amide bands B Have stable comformation for all the blends and only slightly different for other collagen. By the stability, the purification samples lower than the unpurification ones.