NDLI: Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (<i>Sinapis alba</i> L.) napin during industrial-scale myrosinase inactivation process

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Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (Sinapis alba L.) napin during industrial-scale myrosinase inactivation process

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Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (Sinapis alba L.) napin during industrial-scale myrosinase inactivation process

Content Provider	Royal Society of Chemistry (RSC)
Author	Cheng, Bifang McIntosh, Tara C. Marambe, Harsha K. Wanasundara, Janitha P.D.
Copyright Year	2015
Abstract	This study investigated the structural stability of yellow mustard (YM, Sinapis alba L.) napin and the changes of its Sin a 1 anti-epitope antibody-binding ability during myrosinase enzyme inactivation process. The food industry uses myrosinase-inactive non-pungent YM for uses beyond spice applications. Napin was isolated from seeds received from an industrial processor before (YM + M) and after (YM − M) myrosinase inactivation. Secondary and tertiary structural features and surface hydrophobicity parameters of napin were analyzed. The Sin a 1 content in YM seeds and the stability of Sin a 1-containing napin during simulated in vitro gastrointestinal (GI) digestion were determined by a non-competitive indirect enzyme-linked immunosorbent assay using the Sin a 1 anti-epitope antibody (AE-Ab) as the primary Ab. YM napin retained the dominant alpha-helical components of secondary and tertiary structure folds during this process. YM − M napin showed changes in hydrophobicity parameters of the molecules and binding ability of AE-Ab: 2.19 ± 0.48 g per 100 g of YM − M seeds vs. 1.49 ± 0.16 g per 100 g YM + M seeds. YM − M proteins were more susceptible for in vitro GI digestion and also showed a 30% reduction in AE-Ab binding ability upon digestion of napins. This suggests that the myrosinase inactivation process has induced the surface modification of napin, exposing Sin a 1 epitope, leading to an increase in AE-Ab binding. However, the epitope region of YM − M napin showed improved susceptibility for hydrolysis during GI digestion resulting in fewer available epitope regions, suggesting a possible reduction in napin immune reactivity.
Starting Page	2384
Ending Page	2395
Page Count	12
File Format	HTM / HTML PDF
ISSN	20426496
Volume Number	6
Issue Number	7
Journal	Food & Function
DOI	10.1039/c4fo00806e
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	YM Mustard seed White mustard Myrosinase Enzyme Hydrophobe ELISA Alpha helix Epitope Hydrolysis
Content Type	Text
Resource Type	Article
Subject	Medicine Food Science

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