虾类过敏原及消减方法研究进展

虾及其制品味道鲜美,营养丰富,但却具有较高的致敏性。本文综述国内外有关虾类主要过敏原——原肌球蛋白的结构、表位预测与定位、变态反应原性检测及脱敏方法等方面的研究进展,为进一步研究虾类过敏原及其消减技术提供一定的参考。     

免疫印迹法对四种海虾主要过敏原的鉴定

以凡纳滨对虾、中国明对虾、刀额新对虾以及虾蛄4 种海虾为研究对象,对这4 种海虾过敏原蛋白组分进行研究。首先利用聚丙烯酰胺凝胶电泳对4 种海虾过敏原组分进行分析,然后经免疫印迹鉴定其主要过敏原。结果显示：凡纳滨对虾的主要过敏原为99、33、19、14kD 的蛋白质组分;中国明对虾的主要过敏原为39、33、28kD 的蛋白质组分;刀额新对虾的主要过敏原为33kD 和24kD 的蛋白质组分;虾蛄的主要过敏原为56kD 和48kD的蛋白组分。     

Tropomyosin Contains IgE‐Binding Epitopes Sensitive to Periodate but Not to Enzymatic Deglycosylation

Glycosylation has been reported to affect the epitopes of food allergens, however, there are few reports on its role in crab allergen. In the present study, the effect of glycosylation on the IgE‐binding activity of tropomyosin (TM), a major allergen in Scylla paramamosain, was investigated. The results showed that TM was a glycoprotein with a 0.2% carbohydrate moiety and contained O‐glycan. Moreover, enzymatic deglycosylation of TM by glycosidase had no effect on the IgE‐binding activity of TM. In contrast, treatment with periodate resulted in a significant reduction in its IgE‐binding activity.     

Comparative study of in vitro digestibility of major allergen,tropomyosin and other proteins between Grass prawn (Penaeus monodon) and Pacific white shrimp (Litopenaeus vannamei)

BACKGROUND: Stability in simulated gastric fluid is supposed to be an important parameter for the estimation of food allergenicity. In the present study, the digestive stability of allergenic protein tropomyosin (TM) and other food proteins from Grass prawn and Pacific white shrimp in simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) digestion assay system was investigated and comparatively studied by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE), western blotting, and inhibition enzyme‐linked immunosorbent assay (ELISA). RESULTS: In the SGF system, proteins such as actin and myosin heavy chain (MHC) were rapidly degraded within a short period of time, while TM was relatively resistant to pepsin digestion. In the SIF system, MHC was also easily decomposed, while TM and actin were resistant to digestion. Western blotting using a specific polyclonal antibody against TM indicated that the degradation pattern of shrimp TM by SGF and SIF was almost unaffected by the presence of other myofibrillar proteins. Further study by IgE immunoblotting and inhibition ELISA using sera from crustacean‐allergic patients indicated that IgE binding of TM was decreased. CONCLUSION: Proteinase digestion is effective in reducing IgE binding of shrimp TM. It is also of interest to notice that Pacific white shrimp TM had higher digestion stability than Grass prawn TM. However, Pacific white shrimp TM revealed enhanced IgE binding over that of TM from Grass prawn and thus it is possibly more allergenic. Copyright © 2010 Society of Chemical Industry     

蛋白溶出与变性结合消减虾仁致敏性

以南美白对虾虾仁为原料,采用高压下蛋白溶出与变性相结合的方法消减虾仁致敏性。在室温下采用不 同压力（0.1～900.0 MPa）处理虾仁,确定适合虾仁蛋白溶出和变性的压力条件,并以虾仁蛋白致敏性的消减效果 为指标确定虾仁的处理条件。结果显示,在200.0 MPa下保压处理30 min,有利于虾仁蛋白的溶出;当压力大于等 于500.0 MPa时,可引起虾仁蛋白的变性;当压力在600.0 MPa时,虾仁蛋白的致敏性最小。将虾仁在200.0 MPa下 处理30 min后,再用600.0 MPa处理30 min,虾仁的致敏性消减率大于80%。因此,高压处理可消减虾仁的致敏性, 采用适合蛋白溶出与变性相结合的压力处理,能够提高虾仁致敏性消减效果。