Analysis Of Selenium-Containing Protein Composition Of Selenium-Enriched Rice By Size Exclusion Chromatography-Inductively Coupled Plasma Mass Spectrometry
method for analyzing the composition of selenium-containing proteins in selenium-enriched rice was established using size exclusion chromatography-inductively coupled plasma mass spectrometry (SEC-HPLC-ICP-MS). Through water extraction, salt extraction, alkali extraction and alcohol extraction, and using acetone to precipitate the protein, the recovery rates of selenium are 9.6%, 16.8%, 48.2% and 14.9% respectively. The amount of selenium bound to the purified protein is from large to small. The order is alkali prolamin>globulin>gliadin>albumin. The protein liquid was detected by SEC-HPLC-ICP-MS, and through comparative analysis of the protein chromatographic peak (¦Ë=280nm) and the ICP-MS selenium peak (78Se), the molecular weight of the selenoproteins in the four types of proteins was determined using the molecular weight standard curve. The results show that albumin and gliadin are not the main proteins of selenium in selenium-rich rice. Selenium mainly exists in alkali-soluble prolamins and globulin >7kDa, among which the main component of alkali-soluble selenoproteins, F1, has a molecular weight of 199.8kDa.
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Original research was done by Fang Yong, Yang Wenjian, Ma Ning, Tang Xiaozhi, Chen Xi, Hu Qiuhui
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