共查询到17条相似文献,搜索用时 203 毫秒
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晒干处理对花生过敏原蛋白潜在致敏性的影响 总被引:1,自引:0,他引:1
花生是八大食物过敏原之一,花生过敏通常是终身的。晒干是花生加工的重要环节,本研究通过对新鲜花 生进行去壳晒干和带壳晒干2 种不同的晒干处理,探索不同晒干方式对花生过敏原蛋白潜在致敏性的影响。采用凯 氏定氮法、二喹啉甲酸法和聚丙烯酰胺凝胶电泳法测定花生及蛋白提取液中的蛋白浓度和过敏原蛋白的组成,用圆 二色谱、紫外扫描光谱检测花生蛋白的结构变化,用血清免疫球蛋白E(immunoglobulin E,IgE)结合能力表征花 生蛋白潜在致敏性的变化。结果显示,晒干处理后,花生蛋白与血清IgE的结合能力显著增强(P<0.05),去壳晒 干的花生蛋白质二级结构比带壳晒干的花生更有序,三级结构更加紧凑,带壳晒干的花生蛋白可能因为其结构较为 松散,故与IgE结合能力更强。 相似文献
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食物过敏已成为世界关注的重大公共卫生和食品安全问题。文章综述近年来国内外有关加工处理(热加工和非热加工)对食物过敏蛋白致敏性的影响:加工方式、处理强度等均会影响过敏蛋白的分子特性,从而导致其或增敏、或脱敏、或不变;加工虽不能完全消除过敏原的致敏潜力,但可通过加工方式和加工参数的选择使其致敏潜力最小化。通过选择合适的食品加工方式控制食物过敏原,在不改变食物营养价值的条件下,获得脱敏性食物,满足食物易敏人群的正常饮食需求,为消费者提供安全食品,是现代食品工业的重要任务之一。 相似文献
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花生是我国一种重要的粮食作物,但是同时花生蛋白也是重要的食物过敏原。目前国内关于花生蛋白改性后致敏活性与蛋白分子量分布、水解程度的研究报道相对较少。采用胰蛋白酶和木瓜蛋白酶对花生蛋白粉进行限制性水解,通过超滤手段逐级分离蛋白水解物,酶联免疫结果显示:随着水解时间的增加,致敏蛋白含量逐渐增加,未水解的蛋白提取物致敏蛋白含量为71.19 mg/g蛋白,水解4 h后,致敏蛋白含量可达356.74 mg/g;超滤后,致敏蛋白含量显著降低,最低仅为1.91 mg/g,与4 h后的水解液相比较致敏蛋白含量降低了180倍。综上,酶解结合超滤技术是降低花生致敏蛋白的有效方法,可以用于开发低过敏的花生功能食品。 相似文献
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植物多酚与花生致敏蛋白相互作用及脱敏机理研究进展 总被引:1,自引:0,他引:1
花生过敏是最主要的食物过敏类型之一,花生致敏蛋白是主要致敏物质。当前解决花生过敏的方法如热加工法、基因工程方法和酶处理法等存在效率低,安全风险高、易破坏营养成分等缺点。植物多酚是一种天然植物活性物质,具有广泛的生理功能,如抗氧化、降糖、抗炎等,利用植物多酚与花生致敏蛋白相互作用是解决花生过敏的一项新途径,已有文献报道植物多酚具有抗过敏作用。本文主要阐述植物多酚与花生致敏蛋白的相互作用及植物多酚降低花生蛋白致敏性的潜在机理,并对该研究方向进行展望,以期为利用植物多酚解决花生过敏提供新思路。 相似文献
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Beneficial Influence of Short‐Term Germination on Decreasing Allergenicity of Peanut Proteins 下载免费PDF全文
Yingchao Li Xiulan Sun Zhezhe Ma Yan Cui Chao Du Xiuhua Xia He Qian 《Journal of food science》2016,81(1):T255-T261
Most allergenic storage proteins in peanuts are degraded during seed germination. By altering this natural physiological process, it might be possible to reduce peanut protein allergenicity. However, little is known about the change in allergenic proteins and their corresponding immunocreactivity, and the effects of major environmental conditions on their allergenicity during germination. In this study, the influence of different germination conditions (temperature and light) on the degradation of Ara h1 and allergenicity changes of peanut seeds was evaluated by ELISA and Western blotting. The results showed that the 40‐ and 65‐kDa proteins in peanut seeds degraded rapidly during the time course, beginning at 60 (at 25 °C) and 108 h (at 20 °C), and the corresponding immunocreactivity of Ara h1 decreased approximately one‐third after 5 to 7 d of germination. Compared with the cotyledons, the embryonic axes had a higher proportion of Ara h1, which was then degraded relatively faster during germination, resulting in a significant reduction in its allergenicity. Although a higher temperature improved the seed germination rate, it affected sprout quality (as did light); therefore, 25 °C and dark surroundings were suitable conditions under which peanut sprouts were processed; neither factor significantly affected the allergenicity of Ara h1. These results provided a theoretical basis for studies using biological methods to reduce peanut allergenicity. 相似文献
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Qin Geng Ying Zhang Min Song Xiaoya Zhou Yu Tang Zhihua Wu Hongbing Chen 《Comprehensive Reviews in Food Science and Food Safety》2023,22(2):1058-1081
Food allergies are a global food safety problem. Peanut allergies are common due, in part, to their popular utilization in the food industry. Peanut allergy is typically an immunoglobulin E-mediated reaction, and peanuts contain 17 allergens belonging to different families in peanut. In this review, we first introduce the mechanisms and management of peanut allergy, followed by the basic structures of associated allergens. Subsequently, we summarize methods of epitope localization for peanut allergens. These methods can be instrumental in speeding up the discovery of allergenicity-dependent structures. Many attempts have been made to decrease the allergenicity of peanuts. The structures of hypoallergens, which are manufactured during processing, were analyzed to strengthen the desensitization process and allergen immunotherapy. The identification of conformational epitopes is the bottleneck in both peanut and food allergies. Further, the identification and modification of such epitopes will lead to improved strategies for managing and preventing peanut allergy. Combining traditional wet chemistry research with structure simulation studies will help in the epitopes’ localization. 相似文献
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为探究经发酵后的花生营养价值及其蛋白进入体内后致敏性的变化,更好地将微生物发酵应用于花生制品加工生产中。本实验以花生浆(RPP)为研究对象,依次采用高压蒸汽(121 ℃,20 min)、纳豆芽孢杆菌发酵12~60 h处理后,对其冻干产物进行理化性质检测,同时采用聚丙烯酰胺凝胶电泳(SDS-PAGE)和酶联免疫吸附测定(ELISA)检测其蛋白成分在模拟胃肠消化过程中致敏性的变化。结果表明,RPP经高压蒸汽处理后,其蛋白分子量、致敏性、可溶性蛋白含量降低,水解度和多肽含量增加;经纳豆芽孢杆菌进一步发酵后,随着发酵时间的延长,其蛋白分子量、致敏性降低,水解度增加,多肽和可溶性蛋白含量先增加后降低,且其水解度、多肽和可溶性蛋白含量的增加率最高分别为106.9%(发酵60 h)、339.6%(发酵48 h)、42.8%(发酵36 h)。在模拟消化过程中,花生致敏性的降低主要发生在胃液消化阶段,胃肠液连续作用对花生致敏性的影响比其单一作用效果更明显。结合理化指标及致敏性等因素可知,经纳豆芽孢杆菌发酵36 h的花生浆为最好的发酵花生产品,具有营养价值较高、理化性质较好、致敏性较低等特点。 相似文献
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Rodrigo Jiménez-Saiz Sara Benedé Elena Molina 《Critical reviews in food science and nutrition》2015,55(13):1902-1917
Heat treatment has been used since ancient times for food processing, first to ensure the safety of food and its storage, but also to transform its characteristics (in its raw form) and obtain new textures, flavors, or novel foods. However, the transformation experienced by food components when heated, or processed, can dramatically affect the allergenicity of food, either reducing or increasing it. To date, most of the articles published dealing with the changes in the potential allergenicity of food are focused on heat treatment and the Maillard reaction. However, it is also important to give prominence to other group of new technologies developed nowadays, such as high-pressure processing, microwaves and food irradiation. These techniques are not likely to replace traditional processing methods, but they are becoming attractive for the food industry due to different reasons, and it is expected in the near future to have different products on the market processed with these new technologies at an affordable cost. Moreover, other biochemical modifications, particularly enzymatic cross-linking of proteins, have attracted wide-spread attention and will be considered as well in this review, because of its great opportunities to induce protein modification and thus affect food allergenicity. Together with the effect of processing of food allergens, this review will place special attention on gastroduodenal digestion of processed allergens, which directly affects their allergenicity. 相似文献