Preparation and structural characterization of Zinc-binding antioxidant peptides from Corbicula fluminea hydrolysate
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    Abstract:

    Using clam meat as protein source, the hydrolysate was obtained by enzymehydrolysis with neutral protease. Antioxidant peptides were then separated and purified from the enzymatich-ydrolysate of Corbicula flumineaby using glucose gel G-50. Zinc-binding antioxidant peptides were prepared according to optimal process. Qualitative analysis of chelate products was carried out byninhydrin method and sodium sulfide method. Ultraviolet spectra, Fourier infrared and fluorescent light spectra, X-radiation diffraction and scanning electron microscopy were applied to predict the structure of the chelate products. The results showed that the product powder is a kind of polypeptide zinc chelate. The carboxyl, amino and amide bonds of the polypeptide all participate in the chelation reaction, and the structure of the peptide changed significantly after the reaction. The structure of the antioxidant peptide-zinc chelate from Corbicula fluminea can was deduced preliminarily by analysis data.

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刘晶晶,徐蕴桃,朱晨慧,等.河蚬抗氧化肽—锌螯合物的制备及结构表征[J].食品与机械英文版,2020,(10):28-31,48.

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  • Online: February 18,2023
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