Study on purification and physicochemical characterization of Agrocybe aegrita lectin

碩士 === 國立屏東科技大學 === 食品科學系所 === 96 === Lectin is widely existed in the nature, it is a group of proteins or glycoproteins of nonimmune original, which can bind the monosaccharide or polysaccharide specifically, reversibly and noncatalytically, and it can agglutinate the erythrocytes, normal or transf...

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Bibliographic Details
Main Authors: Chia-Hung Hsu, 徐嘉鴻
Other Authors: Ming-Chang Wu
Format: Others
Language:zh-TW
Published: 2008
Online Access:http://ndltd.ncl.edu.tw/handle/91127291794863234985
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Summary:碩士 === 國立屏東科技大學 === 食品科學系所 === 96 === Lectin is widely existed in the nature, it is a group of proteins or glycoproteins of nonimmune original, which can bind the monosaccharide or polysaccharide specifically, reversibly and noncatalytically, and it can agglutinate the erythrocytes, normal or transformed cells. Many reports showed that the lectin has some function, such as anti-tumor, immune regulation, probe testing etc…, and mushrooms containing a rich source of lectins were proved by the scholars. In this study, the Agrocybe aegerita was extracted with 5% NaCl solution, fractionated at 50~80% ammonium sulfate after heating, then further separated with DEAE-Sepharose and Sephacryl S-100 chromatography, the pure lectin could be gotten. Analysis by gel filtration and SDS-PAGE, the molecular weight of Agrocybe aegerita lectin was 32 kDa, and the MW of subunit was 16 kDa. The specific sugar of Agrocybe aegerita lectin is lactose. This lectin can maintain its 50% activity under 60℃for 30 minutes, the activity of the lectin could not be affected in the alkaline condition or by the bivalent cation. The lectin was examined the agglutinin activity with different source of erythrocytes which were treated or non treated with enzymes, the result show that papain treatment can increase agglutinin titer most, the Agrocybe aegerita lectin is not glycoprotein by periodic acid- ammoniacal silver dyeing.