چكيده انگليسي :
79 Extraction and purification of collagen from Aurelia sp jellyfish in the Persian Gulf coast in Bushehr Elham Hajiani e hajiani@ce iut ac ir Date of Submisson 13 January 2016 Department of Chemical Engineering Isfahan University of Technology Isfahan 84156 83111 Iran Defree M Sc Language Farsi Supervisors Kayghobad Shams K shams@cc iut ac ir Abstract Proteins are one of the types of biological macromolecules that were made of thesmaller subunit called amino acids Proteins are very diverse and are the basis of life livingorganisms These biological molecules have the role of construction and other importantfunctions such as hormonal storage protection and safety inside of living creatures Collagen is a protein in connective tissue that its fibers would determine the shape of thetissue and maintain it Collagen is widely used in medical and non medical includinggelatin construction cosmetics heart surgery and pharmaceutical industry Increase inworld population and the need for protein cause special attention to marine food sources The other hand jellyfish is full of collagen Therefore extraction of collagen from jellyfishhas attracted a lot of attention of researchers In general separation of dissolved andundissolved materials from diluted solutions is a difficult task This problem becomesmore serious for substances such as proteins and enzymes That is due to the fact that thesematerials are sensitive to changes in operating conditions such as temperature Method ofacid and pepsin digestion commonly is used in extraction of collagen Since the objectiveof this study is to extract collagen from jellyfish with high efficiency a combination ofthree methods of acid pepsin and salting out for extraction and purification of collagenfrom Aurelia sp species jellyfish was used According to pervious research the extractionefficiency increases with increasing the percentage of pepsin So in this thesis pepsin 0 3 was used in the method pepsin The yield of the ASC was 14 dry weight and that ofthe PSC was 6 dry weight The amount of jellyfish protein and purified collagens wasmeasured by using a spectrophotometer The protein of the jellyfish the acid solublecollagens ASC and pepsin solubilized collagens PSC were 19 65 692 8 and 723 4 respectively In order to evaluation of collagen type and the purification and the lack ofchange the nature of the collagen electrophoresis was used In electrophoresis patterns theacidic and pepsin collagen was observed 1 3 chain that was similar the acidic and pepsincollagen from jellyfish C nozakii Atomic absorption spectrometry was used to determinethe chemical elements The results showed that the amount of Pb was less than detectionlimit Cd exceeded limit and the amount of Fe Zn and Cu was less than the limit More ofCd may be due to entering industrial wastewater to the Bushehr Persian Gulf To check thedenaturation temperature the viscometer was used The results showed that the
