Allergenic response to squid (Todarodes pacificus) tropomyosin Tod p1 structure modifications induced by high hydrostatic pressure. (February 2015)

• Record Type: Journal Article
• Authors: Jin, Yafang; Deng, Yun; Qian, Bingjun; Zhang, Yifeng; Liu, Zhenmin; Zhao, Yanyun
• Is Part Of: Food and chemical toxicology. Volume 76(2015)
• Page Start: 86
• Page End: 93
• Publication Date: 2015-02
• Subjects: ANS 8-Anilino-1-naphthalenesulfonic acid -- CD circular dichroism -- DTNB 5, 5′-dithiobis-(2-nitrobenzoic acid) -- DTT dithiothreitol -- EDTA ethylene diamine tetraacetic acid -- ELISA enzyme-linked immunosorbent assay -- HHP high hydrostatic pressure -- Ho surface hydrophobicity -- LC-Q-TOF-MS liquid chromatography quadrupole time-of-flight mass spectrometry -- PB phosphate buffer -- PSMF phenylmethanesulfonyl fluoride -- SDS-PAGE sodium dodecyl sulfate-polyacrylamide gel electrophoresis -- SGD simulated gastrointestinal digestion -- SH free sulfhydryl group -- TBST Tris-buffered saline and Tween 20 -- TMTp1 tropomyosin Tod p1 -- Tris tris(hydroxymethyl)aminomethane -- UV ultraviolet; High hydrostatic-pressure -- Tropomyosin Tod p1 -- Protein structure -- Allergenicity; Toxicology -- Periodicals; Food poisoning -- Periodicals; Food Poisoning -- Periodicals; Toxicology -- Periodicals; Toxicologie -- Périodiques; Intoxications alimentaires -- Périodiques; Food poisoning; Toxicology; Periodicals; Electronic journals; 615.9
• DOI: 10.1016/j.fct.2014.12.002
• Languages: English
• ISSNs: 0278-6915

Abstract

Graphical Abstract: Highlights: Allergy–structure relation of tropomyosin Todp1 under high pressure was studied. The contents of free sulfhydryl and α-helix decreased with increasing pressure. Surface hydrophobility increased at 200 and 400 MPa, but decreased at 600 MPa. High pressure enhanced in vitro gastrointestinal protein digestibility. 400 and 600 MPa caused more decrease in antigenicity of tropomyosin than 200 MPa. Abstract: The structural and allergenic modifications of tropomyosin Tod p1 (TMTp1) in fresh squids induced by high hydrostatic pressure (HHP) were investigated. The α-helix in TMTp1 decreased along with increasing pressure from 200 to 600 MPa, where almost 53% α-helix was converted into β-sheet and random coils at 600 MPa. The free sulfhydryl group dropped significantly as pressure went up, but the surface hydrophobicity increased at 200 and 400 MPa, while it slightly decreased at 600 MPa. Based on in vitro gastrointestinal digestion test, digestibility of TMTp1 was promoted by HHP treatment, in which 400 and 600 MPa were more effective in reducing the allergenicity than 200 MPa based on indirect ELISA. This study suggested that HHP can decrease allergenicity of TMTp1 by protein unfolding and secondary structure modification, thus providing potential for alleviating allergenicity of squid.