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Preparation of Angiotensin-Converting Enzyme Inhibitory Peptides by Hydrolysis of Cattle Bone

Author: CaiLiHua
Tutor: MaMeiHu
School: Huazhong Agricultural University
Course: Of Food Science
Keywords: Cattle bone meal Bovine bone collagen Angiotensin-converting enzyme ACE inhibitory peptides
CLC: TQ464.7
Type: Master's thesis
Year: 2010
Downloads: 85
Quote: 0
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Abstract


In this paper, bovine bone protein hydrolyzate prepared angiotensin-converting enzyme inhibitory peptides, carried out research in the following aspects: the nutritional value of the changes of the bone protein in cow bone softening process and laboratory preparation of cattle bone meal; through on bovine bone found alkaline protease, neutral protease, trypsin hydrolysis of cow bone better hydrolysis; hydrolysis conditions and kinetic parameters of the protein hydrolyzate of bovine bone, according to the dynamics test: alkaline protease protein in bone the optimum temperature was 55 ° C, pH 12, the Vmax of 0.10824 g / L · min Km for the 11.71892g / L; neutral protease acting on the optimum conditions of the bone protein temperature of 45 ° C and pH 7 At this point Vmax to 0.04724 g / L · min, Km and for 14.35711g / L; trypsin acting on the the bone protein optimum temperature of 55 ° C, a pH of 9, the Vmax was 0.05073g / L · min, Km 4.31516 g / L. Crude enzyme solution extracted from fresh pig lung angiotensin-converting enzyme (ACE), the specific activity 5.21u ACE enzyme solution obtained after purification; study found that different proteolytic hydrolysis by the degree of hydrolysis of ACE inhibition rate relationship degree of ACE inhibition rate relationship; selection of alkaline protease the tools enzyme as enzymatic of bone meal preparation ACE inhibitory peptide On this basis, through the optimization of the conditions of optimal enzymatic parameters of 50 ° C, pH 10, the substrate concentration 25%, E / S 0.4, hydrolysis time of 3h. The distribution of the molecular weight of the glucan gel chromatographic A3h, found that the mixed peptide is divided into three main components, wherein the component 111 a molecular weight of less than 1000 Da, and semi minimum inhibitory concentration of 0.561mg/ml, a higher inhibitory activity; The qualitative analysis of the 5000 Da of the hollow fiber membrane ultrafiltration, small molecule hybrid peptide obtained by amino acid analysis, etc.. Stability Experiment and ACE inhibitory activity of digestion by ACE inhibition kinetics studies, found that the mixed peptide is a competitive inhibitor of the true suppression type. Collection has been reported that the data analysis showed that the peptide of hydrophobic amino acids and aromatic amino acids have a greater impact on its activity of inhibiting ACE; macroporous resin enriched in hydrophobic amino acids to determine the operating conditions of a concentration of 50mg/ml bone peptide sample Jia, the highest inhibiting activity of 100% ethanol elution fraction obtained ACE half inhibitory concentration (IC50) was 0.45mg/ml component was 24.59%; enriched aromatic amino acid using the granular activated carbon, determined 30mg / ml concentration of the sample is preferably a component, using 100% ethanol and 5% acetic acid afforded the IC50 was 0.59mg/ml.

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CLC: > Industrial Technology > Chemical Industry > Pharmaceutical chemical industry > Drug production of biological products > Amino acids,peptides,proteins
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