在体胃肠道消化研究泥蟹（锯缘青蟹）主要过敏原原肌球蛋白和其他食物蛋白的稳定性。
Stability of major allergen tropomyosin and other food proteins of mud crab (Scylla serrata) by in vitro gastrointestinal digestion.
机构信息
College of Biological Engineering, The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei University, 43 Yindou Road, Xiamen, Fujian, China.
出版信息
Food Chem Toxicol. 2010 May;48(5):1196-201. doi: 10.1016/j.fct.2010.02.010. Epub 2010 Feb 13.
Stability in simulated gastric fluid is regarded as an important parameter for the estimation of food allergenicity. In this study, the digestive stability of allergenic protein tropomyosin (TM) and other food proteins from mud crab in simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) digestion assay system was investigated and compared by SDS-PAGE and Western blot. In SGF system, proteins such as actin and the original band of myosin heavy chain (MHC) were rapidly degraded within a short period of time, while TM was relatively resistant to pepsin digestion. In SIF system, MHC was easily decomposed, while TM and actin were similarly resistant to digestion. Further study by IgE-immunoblotting and inhibition ELISA using sera from crab-allergic patients indicated that allergenicity of TM was partially decreased, suggesting proteinase digestion is effective in reducing the allergenicity of crab TM.
在模拟胃液中的稳定性被认为是估计食物变应原性的一个重要参数。在这项研究中，通过 SDS-PAGE 和 Western blot 研究和比较了模拟胃液（SGF）和模拟肠液（SIF）消化液系统中来自泥蟹的致敏蛋白原肌球蛋白（TM）和其他食物蛋白的消化稳定性。在 SGF 系统中，肌动蛋白和肌球蛋白重链（MHC）的原始带等蛋白质在短时间内迅速降解，而 TM 对胃蛋白酶消化具有较强的抵抗力。在 SIF 系统中，MHC 很容易分解，而 TM 和肌动蛋白同样具有抗消化性。使用蟹过敏患者的血清进行 IgE-免疫印迹和抑制 ELISA 的进一步研究表明，TM 的致敏性部分降低，提示蛋白酶消化可有效降低蟹 TM 的致敏性。
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