Preparation And Enteral Nutrition Effects Glutamine Of Peptide Extracted From Glutenin

Extraction process of glutenin from Wheat gluten was optimized by means of the orthogonal experiment design in this paper. Monitored by yields of Gln, the alkali proteinase was selected from three commercial proteinases and used for enzymolysis to produce the Active Glutamine Peptides Made From glutenin By two times of Enzymatic Hydrolysis; the gel chromatography method was used for the separation and purification, the GPC was used to investigate the distribution of molecular weights, HPLC-MS was used to preliminarily analyze the product structure, and the Small Intestine of Rats was selected to test activity in animal in vivo. The experimental results were as follows:1.The extraction technology of glutenin from wheat gluten and physic-chemical properties were investigated. The results indicated that the optimal conditions for separating glutenin from the wheat gluten were as follows: pH12, material/solvent ratio 1:20 and extraction time 1h.The sequence of importance for the product yields was gluten and extraction time, gluten / solvent ratio and pH, and the yield of 25.5% can be obtained under such conditions. DSC analysis showed that the peak denaturation temperature was 67.41℃.2.The paper confirms enzyme for Gln active peptide hydrolization, trypsinase, alkaline proteinase, and optimization enzymolysis condition in the duration. Gln active peptide was prepared through two times enzymolysis technology. trypsinase was selected for enzymolysis by the method of response surface to produce Gln active peptides.The requirement of trypsinase is that concentration of substrate is 2.79%, enzyme concentration is 73mg, pH8.0, temperature is 47.6℃, and reaction time is 2 hours. The requirement of alkaline proteinase is that concentration of substrate is 3%, enzyme concentration is 3%, pH8.0, temperature is 68℃, and reaction time is 1.5 hours. The concentration of effective Gln is 213.5mg/g after enzymolysis solution3.Glutamine Peptides were separated and purified by the method of gel chromatography, and the distributions of molecular weights of different components were analyzed by GPC.component IV were analyzed by HPLC-MS and the results indicated that the single component separated from gel column was the mixture of peptides of different molecular weights, and its molecular weights were mainly distributed in the range of 1000-800D.4.Administration of methotrexate to rats caused severe enterocolitis with 42.9% and 16.7% mortalities with in 72 hours in the first group(Blank Group) and the second group respectively(control group). But the sucrase and aminopeptidase activities,DNA and RNA contents of small intestine in rats of low-dose group and high dose group were significantly higher than those of group 1 and group 2. These results showed that glutaminebioactive peptide enhanced digestion processes...