Extraction And Properties Of Tilapia Bone Collagen Protein
Keywords
Tilapia Bone,Collagen,Physicochemical Propertytilapia Bone,Collagen,Physicochemical Property
Abstract
In order to make full use of the collagen protein in fish bones from fish fillet processing waste, single factor and orthogonal experimental methods were used to study the optimal process for extracting tilapia bone collagen protein by pepsin under acidic medium conditions. The refined collagen protein was SDS-PAGE electrophoresis, ultraviolet and Fourier transform infrared scanning, circular dichroism detection, amino acid analysis, thermal denaturation temperature measurement and other methods are used to analyze the physical and chemical properties of collagen proteins. The results show that: the pH of the lactic acid solution is 2.6, the temperature is 30¡ãC, the material-to-liquid ratio is 1:30 (g/mL), the amount of enzyme added is 200 U/g, and the extraction time is 24 h. The extraction rate of crude collagen protein under this process condition reaches 70.28%. , the yield is 12.76%; tilapia bone collagen protein contains 2 ¦Á chains and 1 ¦Â chain, which is a typical type I collagen protein; the main amino acids of tilapia bone collagen protein are glycine, proline, and hydroxyproline Acid, glutamic acid and alanine; the thermal denaturation temperature of tilapia bone collagen protein is 34.5 ¡æ. Studies have shown that using pepsin to extract fish bone collagen protein has higher extraction rate and purity. Fish bone,containing plenty of collagen,is the main offal from fish fillet processing. The collagen from Tilapia bone after removing impurities was extracted by pepsin digestion in acid medium condition. The effects of extraction medium,temperature,material to liquid ratio,pepsin addition ,extraction duration on yield of collagen were investigated. The optimum conditions using lactic acid as medium to extract collagen were pH 2.6,material to liquid ratio(w/v) 1:30,30 ¡æ,200 U/g pepsin addition,extraction time 24 h,and the yield of extracted collagen reached 70.28%(12.76% when compared with the initial weight of Tilapia bone). Then, the extracted crude collagen was further purified and its physicochemical property was determined by the methods of SDS-PAGE,UV and FT-IR scanning,DSC,CD and amino acid analysis. The results indicated that the extracted Tilapia bone collagen belongs to typical collagen¢ñwith two ¦Á and one ¦Â chains. Furthermore, the Tilapia bone collagen contains high percentages of Gly,Pro,Hyp, Glu and Ala and its denaturation temperature was 34.5 ¡æ. In conclusion, the extracted Tilapia bone collagen by pepsin digestion has a higher yield and purity
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Original research was done by Ye Tao, Lin Lin, Zhang Xiaoxia, Jiang Shaotong, Lu Jianfeng
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