Transglutaminase-catalysed cross-linking eliminates Penaeus chinensis tropomyosin allergenicity by altering protein structure

被引:13
作者
Fu, Linglin [1 ,2 ]
Ni, Saiqiao [1 ]
Wang, Chong [1 ]
Wang, Yanbo [1 ,2 ]
机构
[1] Zhejiang Gongshang Univ, Sch Food Sci & Biotechnol, Food Safety Key Lab Zhejiang Prov, Hangzhou 310018, Zhejiang, Peoples R China
[2] Zhejiang Gongshang Univ, Zhejiang Engn Inst Food Qual & Safety, Hangzhou 310018, Zhejiang, Peoples R China
基金
中国国家自然科学基金;
关键词
Tropomyosin; allergenicity; structure; transglutaminase; MAJOR SHRIMP ALLERGEN; IGE-BINDING-CAPACITY; CONFORMATIONAL STRUCTURE; MYOFIBRILLAR PROTEIN; HEAT-TREATMENT; IDENTIFICATION; GLYCOSYLATION; LACTOGLOBULIN; ANTIGENICITY;
D O I
10.1080/09540105.2019.1580250
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Transglutaminase (TG) is a major food processing enzyme that induces protein cross-linking. Tropomyosin (TM) is a major shellfish allergen that is responsible for at least 80% of the shrimp allergic incidents. The aim of this research was to investigate the effect of TG on TM allergenicity and reveal the involvement of TM structure alternation. After treated with TG for different time, the allergenicity of TM was assessed by indirect ELISA with shrimp allergic patients' sera, and the structure of TM was characterized by circular dichroism (CD) spectroscopy, ultraviolet (UV) absorption spectroscopy and fluorescence spectroscopy. Results showed that the allergenicity slightly decreased at the early stage of reaction and dramatically decreased at the late stage, which is tightly correlated with the increment of beta-turn content and UV absorption. In conclusion, TG modification is an effective and promising food processing method to eliminate TM allergenicity with significant prospect of industrial application.
引用
收藏
页码:296 / 308
页数:13
相关论文
共 35 条
  • [1] [Anonymous], CHINESE FOOD ADDITIV
  • [2] Identification of continuous, allergenic regions of the major shrimp allergen Pen a 1 (tropomyosin)
    Ayuso, R
    Lehrer, SB
    Reese, G
    [J]. INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY, 2002, 127 (01) : 27 - 37
  • [3] Effect of heat treatment on the antigenicity of bovine -lactalbumin and -lactoglobulin in whey protein isolate
    Bu, Guanhao
    Luo, Yongkang
    Zheng, Zhe
    Zheng, Hai
    [J]. FOOD AND AGRICULTURAL IMMUNOLOGY, 2009, 20 (03) : 195 - 206
  • [4] Polyphenol oxidase/caffeic acid may reduce the allergenic properties of peanut allergens
    Chung, SY
    Kato, Y
    Champagne, ET
    [J]. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 2005, 85 (15) : 2631 - 2637
  • [5] Effects of Transglutaminase Catalysis on the Functional and Immunoglobulin Binding Properties of Peanut Flour Dispersions Containing Casein
    Clare, Debra A.
    Gharst, Greg
    Maleki, Sohelia J.
    Sanders, Timothy H.
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2008, 56 (22) : 10913 - 10921
  • [6] Nomenclature of the proteins of cows' milk - Sixth revision
    Farrell, HM
    Jimenez-Flores, R
    Bleck, GT
    Brown, EM
    Butler, JE
    Creamer, LK
    Hicks, CL
    Hollar, CM
    Ng-Kwai-Hang, KF
    Swaisgood, HE
    [J]. JOURNAL OF DAIRY SCIENCE, 2004, 87 (06) : 1641 - 1674
  • [7] Assessment of the sensitizing capacity and allergenicity of enzymatic cross-linked arginine kinase, the crab allergen
    Fei, Dan-Xia
    Liu, Qing-Mei
    Chen, Feng
    Yang, Yang
    Chen, Zhong-Wei
    Cao, Min-Jie
    Liu, Guang-Ming
    [J]. MOLECULAR NUTRITION & FOOD RESEARCH, 2016, 60 (07) : 1707 - 1718
  • [8] Identification of Allergenic Epitopes and Critical Amino Acids of Major Allergens in Chinese Shrimp (Penaeus chinensis) by Immunoinformatics Coupled with Competitive-Binding Strategy
    Fu, Linglin
    Wang, Jinbao
    Ni, Saiqiao
    Wang, Chong
    Wang, Yanbo
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2018, 66 (11) : 2944 - 2953
  • [9] [傅玲琳 Fu Linglin], 2017, [食品科学, Food Science], V38, P187
  • [10] Allergy and hypersensitivity - Nature versus nurture in allergy and hypersensitivity - Editorial overview
    Geha, RS
    [J]. CURRENT OPINION IN IMMUNOLOGY, 2003, 15 (06) : 603 - 608