Study On Sika Deer Velvet Fat-soluble Components, Collagen And Collagen Peptides

Sika Deer Velvet has a unique biological activity and chemical composition, it enjoys a special status in the field of medicine and health care products, due to the backward mode of the traditional methods, The content of active ingredients plum velvet processing antler is very low,can not make this traditional the rare medicinal herbs are fully utilized. So we make Sika Deer Velvet grouped according to their solubility characteristics for the comprehensive development. In this study, we use supercritical CO2extraction to get fat-soluble components of Sika Deer Velvet and analysis the insoluble components in collagen and collagen peptide composition of Sika Deer Velvet to determine the The best hydrolysis conditions of the functional and biological activity of. The study results are as follows:1.Used supercritical CO2fluid (SFE) and gas chromatography-mass spectrometry (GC-MS) to identify extract18kinds of fat-soluble ingredients of the composition and content of the Sika Deer Velvet fat-soluble ingredients. By orthogonal test the optimum conditions for CO2-the SFE extraction of fat-soluble ingredients of the plum flower antler as follows:the amount of extraction time3h, the entrainer (70%) lml/g, temperature of50℃, pressure of30MPa. The fatty acid composition accounted for the main part of the18kinds of extracts, and fatty acids is the mainly composition..2.Insoluble components of the Sika Deer Velvet that not soluble in any component of the neutral solvent, Firstly used quantitative hydroxyproline method to quantify the collagen content,after testing calculations,we got the plum antler collagen content of4.5795%. And then select the papain enzymatic extraction of insoluble component preparation plum velvet collagen, demineralized insoluble components by single-factor test before the extraction, to determine the best decalcification conditions as follows:4%of the hydrochloric acid concentration, solid to liquid1:15, the pickling time48h, at this time decalcification was96.42%. Removal of contaminating proteins, samples after decalcification by single factor test to determine the best conditions of impurity proteins as follows:4%of the concentration of NaCl, the volume ratio of1:10, the impurity time12h. After treatment, the insoluble components extraction rate by a single factor and orthogonal experiments, the collagen index to determine the optimum conditions of plum velvet collagen as follows:2%of the optimum amount of enzyme, pH value6.0, the volume ratio of1:20, the hydrolysis time was66h. Click here conditions extracted plum velvet collagen extraction rate of54.59%. Sika Deer Velvet collagen will be to continue to use the Sika Deer Velvet papain hydrolysis of collagen peptides, the degree of hydrolysis of collagen peptides by single factor and orthogonal experiments Sika Deer Velvet collagen peptides, optimal conditions were:for the index to determine the optimal enzyme dosage of6000U/g, temperature50℃, PH value6.0, Sika Deer Velvet hydrolysis time was5h. under these conditions the hydrolysis of collagen peptide hydrolysis degree of15.49%. The samples were prepared using the molecular weight determination by SDS-PAGE, the results show that the molecular weight of plum velvet collagen belong to macromolecules, and molecular weight distribution of the size of a narrow range between100kD-200kD, to maintain a complete triple helix structure. The plum antler collagen polypeptide molecular weight concentrated in the following6.5kD and it has been hydrolyzed easy digestion and absorption of small molecules. The results showed that the composition and the content of amino acid of the plum velvet collagen is close to collagen peptides, as a kind of typical collagen amino acid,the samples were prepared.After testing the ability like antioxidant,clearing hydroxyl radical and DPPH of Sika Deer Velvet collagen and collagen peptides.We got the results that the ability of collagen peptides are stronger than the collagen. Keratinocyte cell study found that growth and reproductive capacity of cultured cells on collagen was significantly better than in cultured on collagen polypeptide, indicating that the hydrolysis of collagen and collagen peptide hydrolysis raise the temperature of collagen denaturation reason, the loss of collagen peptides The natural structure of collagen has lose biologically active. Collagen peptides of collagen hydrolysates, lower molecular weight, easy for the body to fully absorb the use and contains all the amino acids of collagen, so the functional collagen peptide is superior to the collagen.