The Research Of Antioxidant Activity Of Chicken Bone Residue Hydrolyzed By Enzyme

This paper studied the optimal process and antioxidant activity of making chicken bone residue hydrolyzed by enzyme.This experiment uses the Nutrase and Papain to hydrolyze chicken bone residue,investigating the effect of different substrate concentration,enzyme concentration,reaction temperature and reaction time on the yield of oligopeptide of product.The Response surface optimization experiment was designer in order to get the higher TCA-NSI.The TCA-NSI influence of hydrolysis chicken bone residue by using different compound protease is also discussed in this paper.The clearance rate of hydroxyl free radicals,superoxide anion free radicals and DPPH free radicals,the chelation of Fe²⁺,and the reduction of Fe³⁺ are chosen to evaluate the antioxidant ability of chicken bone residue peptides.The main result of this paper is below:1.The results of single factor experiments indicates that TCA-NSI showed a trend of decline after rising first,with the increase of the substrate concentration and the reaction temperature.The TCA-NSI showed a trend of flatten after rising,with the increase of enzyme concentration and reaction time.2.The best process of Nutrase and Papain to hydrolyze chicken bone residue has been got respectively: The substrate concentration is 5%,and the enzyme concentration is200mg/g,the reaction temperature is 42 ?,the reaction time is 2h,under this condition the TCA-NSI is 56.16% ± 0.88;The substrate concentration is 11%,the enzyme concentration is 211 mg?g-1,the reaction temperature is 57 ?,and the reaction time is 3h,under this condition the TCA-NSI is 58.87%±0.51%.3.The result of antioxidant ability experiments shows: Compared with vitamin C,the peptides hydrolyze by Nutrase and Papain respectively have good ability to clear the free radicals at the concentration of 32 mg/m L,however,the peptide hydrolyzes by compound enzyme will have the nearly ability at the concentration of 8 mg/m L.Also,the peptides have rare ability of chelation of Fe²⁺ and reduction of Fe³⁺.