Study On Production Of Collagen From Chick Sternal Cartilage

The cartilage collagen was employed to analyze the effects on the degree of hydrolysis and yield of collagen by acid swell and enzymatic extraction. The processing conditions were optimized and the product quality and structure of collagen during purification were also researched. The detailed contents and the main results were as follow:Response surface methodology(RSM) was employed to analyze the effects of the enzyme dosage,hydrolysis tempeature and hydrolysis time on degree of hydrolysis. Optimization of the processing was also performed. The results showed that The results showed that predicted regression models of degree of hydrolysis were found to be in good agreement with experimental values. The processing conditions had significant effects on degree of hydrolysis. The optimum conditions were:enzyme dosage of0.57%, hydrolysis tempeature of36.18℃, hydrolysis time of7.14h. At this optimum point, degree of hydrolysis were1.19%.Cartilage was treatment by combined method of acid swelling and pepsin hydrolysis in order to increase the extraction rate of cartilage collagen.On the base of single factor experiment,the optimum parameters of extraction for collagen from cartilage were determined by response surface methodology.Consequently,the optimized processing parameters were determined,including acidity of0.84mol·L-1,time of4.8h,temperature of28.06℃and ratio of liquid to solid of5.43mL·g-1.At the optimum conditions, the yield of collagen reached to60.78%.The results show that acid swelling a helpful treatment to improve the extraction rate of cartilage collagen.The product quality and structure of collagen were detected by multi-determination method.The results showed that the product during purification were rich in glycine,proline,hydroxyproline acid but low in methionine, tyrosine, histidine and cystine. This feature was consistent with the typical collagen amino acid composition. The typical UV spectrum of collagen solutions from200to330nm. The characteristic absorption at220nm is mainly due to the presence of hydroxyproline and a weaker maximum at280nm due to aromatic amino acid in collagen molecules.The results and amino acid analysis were in accordance with that from the UV absorption spectrum.In product the content of collagen were higher,and the contents of fat and polysaccharides were low. The mass fraction of collagen in product reaches55%.