Keywords

Cyclic Dipeptide (Histidine-Proline), Zein, Isolation And Purification, Structural Identification

Abstract

Cyclic dipeptide (His-Pro) (CHP) is an active cyclic dipeptide that has significant effects in lowering blood sugar and anti-oxidation. The experiment used methods such as DE-52 anion exchange chromatography, Sephadex G-25 gel chromatography, and semi-preparative high-performance liquid chromatography to conduct separation and purification research on the zein hydrolyzate after high-temperature and high-pressure cyclization to obtain CHP. Ultra-high performance liquid chromatography, Fourier transform infrared spectroscopy, hydrogen nuclear magnetic resonance spectroscopy, and carbon spectroscopy were used to identify the structure of the product, and its biological activity was preliminarily determined through in vitro hypoglycemic and antioxidant experiments. The results show that the purity of CHP prepared by the separation and purification method of this study is 97.36%. The measurement of Fourier transform infrared spectrum and nuclear magnetic resonance spectrum show that the structure of the peptide is consistent with the expected structure. The preliminary physiological activity identification results show that, After separation and purification, corn CHP has strong inhibitory ability to ¦Á-glucosidase and ¦Á-amylase activities, with half inhibitory concentrations (IC50) of 1.1 and 1.9 mg/mL respectively; and it has strong 1,1-diphenyl 2-Trinitrophenylhydrazine free radical scavenging activity (IC50 67 ¦Ìg/mL) and reducing power

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Original research done by Liu Hongcheng, Zhang Yanrong, Fan Hongxiu, Dong Xin

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