Effect of High Hydrostatic Pressure (HHP) Processing on Immunoreactivity and Spatial Structure of Peanut Major Allergen Ara h 1

被引：11

作者：

Pan, Di ^{[1
]}

Tang, Biling ^{[1
]}

Liu, Huipeng ^{[1
]}

Li, Zhenglong ^{[1
]}

Ma, Rongrong ^{[1
]}

Peng, Yajuan ^{[1
]}

Wu, Xuee ^{[1
]}

Che, Liming ^{[1
]}

He, Ning ^{[1
]}

Ling, Xueping ^{[1
]}

Wang, Yuanpeng ^{[1
]}

机构：

[1] Xiamen Univ, Dept Chem & Biochem Engn, Coll Chem & Chem Engn, Xiamen 361005, Peoples R China

来源：

FOOD AND BIOPROCESS TECHNOLOGY | 2020年 / 13卷 / 01期

关键词：

Ara h 1; High hydrostatic pressure (HHP); Structure; Immunoreactivity; Mulitimer; FUNCTIONAL-PROPERTIES; IGE-BINDING; POTENTIAL ALLERGENICITY; CONFORMATIONAL-CHANGES; PROTEIN-STRUCTURE; EPITOPES; ARA-H-1; ISOLATE;

D O I：

10.1007/s11947-019-02382-z

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Ara h 1 is recognized as a major peanut allergen. The effects of high hydrostatic pressure (HHP) on the immunoreactivity and structure of Ara h 1 were investigated in this study. The immunoreactivity of Ara h 1 was considerably reduced (P < 0.01) after HHP treatment (>= 400 MPa) with the increase of pressure holding time. The maximum reduction of 74.32% was achieved at 600 MPa for 1200 s. The particle size and molecular weight of Ara h 1 increased, and the secondary/tertiary structure changed markedly. The decrease of the immunoreactivity of Ara h 1 was mainly due to the changes in conformation (especially the tertiary structure) and the formation of new multimers, resulting in the inactivation of immunoreactive sites. Results indicate that HHP technology has the potential to be applied to the preparation of hypoallergenic peanut products.

引用

页码：132 / 144

页数：13

共 50 条

[1] Effect of High Hydrostatic Pressure (HHP) Processing on Immunoreactivity and Spatial Structure of Peanut Major Allergen Ara h 1
Di Pan
Biling Tang
Huipeng Liu
Zhenglong Li
Rongrong Ma
Yajuan Peng
Xuee Wu
Liming Che
Ning He
Xueping Ling
Yuanpeng Wang
[J]. Food and Bioprocess Technology, 2020, 13 : 132 - 144
[2] Crystal structure of the major peanut allergen Ara h 1
Cabanos, Cerrone
Urabe, Hiroyuki
Tandang-Silvas, Mary Rose
Utsumi, Shigeru
Mikami, Bunzo
Maruyama, Nobuyuki
[J]. MOLECULAR IMMUNOLOGY, 2011, 49 (1-2) : 115 - 123
[3] Structure of peanut major allergen Ara h 3
Zhang, Y.
Jin, T.
Howard, A.
Chen, Y.
[J]. JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, 2009, 123 (02) : S228 - S228
[4] Crystal structure of Ara h 3, a major allergen in peanut
Jin, Tengchuan
Guo, Feng
Chen, Yu-wei
Howard, Andrew
Zhang, Yu-Zhu
[J]. MOLECULAR IMMUNOLOGY, 2009, 46 (8-9) : 1796 - 1804
[5] Effect of digestion on the immunoreactivity and proinflammatory properties of recombinant peanut allergen Ara h 1
Tian, Yang
Rao, Huan
Fu, Wenhui
Tao, Sha
Xue, Wen-Tong
[J]. FOOD AND AGRICULTURAL IMMUNOLOGY, 2019, 30 (01) : 418 - 431
[6] The effect of digestion on the allergenicity of the major peanut allergen Ara h 1.
Kopper, RA
Maleki, S
Sampson, HA
Burks, AW
Bannon, GA
[J]. JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, 1999, 103 (01) : S67 - S67
[7] Structure and organization of the genomic clone of a major peanut allergen gene, Ara h 1
Viquez, OM
Konan, KN
Dodo, HW
[J]. MOLECULAR IMMUNOLOGY, 2003, 40 (09) : 565 - 571
[8] Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h 2 Roasted in a Matrix
Chang, Xuejiao
Zhou, Xiaoya
Tang, Yu
Zhang, Ying
Yuan, Juanli
Li, Xin
Yang, Anshu
Tong, Ping
Wu, Zhihua
Chen, Hongbing
[J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2022, 70 (02) : 626 - 633
[9] Effect of boiling on the structure and immunoreactivity of recombinant peanut protein Ara h 1
Tian, Yang
Rao, Huan
Tao, Sha
Xue, Wen-Tong
[J]. FOOD AND AGRICULTURAL IMMUNOLOGY, 2018, 29 (01) : 845 - 858
[10] Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases
Radosavljevic, Jelena
Dobrijevic, Dragana
Jadranin, Milka
Blanusa, Milan
Vukmirica, Jelena
Velickovic, Tanja Cirkovic
[J]. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 2010, 90 (10) : 1702 - 1708

← 1 2 3 4 5 →