Preparation And Chelating Properties Of Peptide-chelated Calcium From Chongren Cartridge Chicken

Chicken protein has a high economic value,but at present there are only a limited variety of industrially processed products for chicken protein,and the market is still dominated by rough processing,lacking high-value products.In this study,the peptides were prepared using modern enzymatic digestion technology and Ca Cl₂was used as the calcium source to prepare the calcium chelate for Chongren artridge Chicken peptides.The stability,calcium chelating power and binding mode were studied to provide a theoretical basis for the development of Chongren artridge Chicken products.The research content and results are as follows:The results showed that papain was the best hydrolytic enzyme,and the optimum enzymatic conditions were 53℃,p H 6.4,enzyme addition of 4131U/g,material-liquid ratio of 10.8:1 and enzymatic digestion time of 3.5 h.The calcium chelating power was 58.52 mg/g at this time.Further investigation of the protein functional properties of the peptide under these conditions showed that solubility was highest at p H>6,foaming was best at p H 7 under neutral conditions,and emulsification was best at p H 11.The results showed that the optimum chelating conditions were 1:1.7 peptide to calcium mass ratio,p H 8.0,38.8 min reaction time and 38.0°C,which resulted in a calcium chelating power of 76.95 mg/g.The stability of the chelate was further investigated and the results showed that the temperature stability of the peptide was better than that of the peptide.In vitro simulations showed that in the gastric,intestinal and gastric-intestinal simulations,the intestinal group had the best stability and the gastric group had the greatest influence on the stability.X-ray diffraction showed that this substance had a crystal structure that was not present in the peptide;scanning electron microscopy showed that the microstructure changed after chelation and protein aggregation was enhanced;Fourier infrared spectroscopy showed that the intensity and position of the spectral peaks changed after chelation.Fourier infrared spectroscopy showed that the intensity and position of the peaks changed after chelation,and the carboxyl and amino groups were the main binding sites of the chelate;the results of amino acid composition analysis showed that the acidic amino acids,mainly glutamic acid and aspartic acid,had the greatest influence on calcium chelation,and the proportion of essential amino acids increased after chelation.