Purification and partial characterization of a novel hemagglutinating glycoprotein from the cultured mycelia of Hericium erinaceus
文献类型： 外文期刊
作者： Cui, Feng-Jie 1 ; Li, Yun-Hong 1 ; Zan, Xin-Yi 1 ; Yang, Yan 2 ; Sun, Wen-Jing 1 ; Qian, Jing-Ya 1 ; Zhou, Qian 3 ; Yu, S 1 ;
作者机构： 1.Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China
2.Shanghai Acad Agr Sci, Natl Engn Res Ctr Edible Fungi, Shanghai 201403, Peoples R China
3.Jiangxi Prov Engn & Technol Ctr Food Addit Biopro, Dexing 334221, Peoples R China
关键词： Hericium erinaceus, Cultured mycelia;Glycoprotein;Hemagglutinating activity;Structural novelty
期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：3.757； 五年影响因子：3.665 ）
ISSN： 1359-5113
年卷期： 2014 年 49 卷 8 期
页码：
收录情况： SCI
摘要： HEG-5, a novel glycoprotein with hemagglutinating activity, was firstly isolated and purified from the cultured mycelia of Hericium erinaceus CZ-2. SDS-PAGE, Native-PAGE and MALDI-TOF-MS proved that HEG-5 was a single band with the molecular weight of approximately 14.4 kDa. HEG-5 had the protein: polysaccharide ratio of approximately 10:1 (%/%) and contained ID-glucose, L-rhamnose, D-galactose and D-mannose with a molar ratio of 1.00:1.09:2.45:7.14 in polysaccharide fraction. HEG-5 was an acidic glycoprotein with a PI value of 6.3 and the higher content of acidic amino acids (Asp, 12.42 +/- 0.25% and Glu, 12.24 +/- 0.26%) in protein fraction. FT-IR and NMR spectra revealed that HEG-5 contained the protein and carbohydrate portions with (1 -> 4)-linked beta-galactose residues and beta-linked glucose residues. Circular dichroism (CD) demonstrated that HEG-5 was a beta-sheet predominant glycoprotein. Hemagglutination assay proved it was a thermo-unstable glycoprotein. The HEG-5 structural novelty was finally presented by protein sequencing and modeling by using MALDI-TOF-MS, NCBI blast search and online SWISS-MODEL Workspace service. (C) 2014 Elsevier Ltd. All rights reserved.
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