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AuthorLi, Ying
AuthorYu, Jianmei
AuthorGoktepe, Ipek
AuthorAhmedna, Mohamed
Available date2017-03-05T10:40:16Z
Publication Date2016-04-01
Publication NameFood Chemistry
Identifierhttp://dx.doi.org/10.1016/j.foodchem.2015.10.089
CitationLi, Y., Yu, J., Goktepe, I. and Ahmedna, M. (2016)” The potential of papain and alcalase enzymes and process optimizations to reduce allergenic gliadins in wheat flour” Food Chemistry, vol.196, pp. 1338–1345.
ISSN0308-8146
URIhttp://www.sciencedirect.com/science/article/pii/S0308814615300893
URIhttp://hdl.handle.net/10576/5345
AbstractThe objectives of this study were to select effective enzymes that catalyze the hydrolysis of allergenic proteins, gliadins, in wheat flour and to optimize the enzymatic treatment conditions. Six proteases were tested. Hydrolyzed samples were tested for residual gliadin concentrations and in vitro allergenicity. The hydrolysis conditions of wheat protein by the effective enzymes were optimized by central composite design. Results showed that alcalase from Bacillus licheniformis, and papain from latex of papaya fruit had greater ability to reduce gliadin content of wheat flour than flavourzyme, pepsin, trypsin or α-chymotrypsin. The sequential-treatment of wheat flour by alcalase–papain was more effective in reducing gliadin content than single enzyme treatment. Under the optimal conditions of sequential enzymatic treatment, gliadin was almost completely removed, resulting in the flour extract showing lowest IgE-binding. Therefore, this could be a promising biotechnology for preparing low allergenic wheat products.
SponsorGrant 2011-67017-3003 from the National Institute of Food and Agriculture (NIFA), USDA.
Languageen
PublisherElsevier Ltd
SubjectWheat allergen reduction
Enzymatic treatment
Digestive protease
Non-digestive protease
Gliadin content
IgE-binding
TitleThe potential of papain and alcalase enzymes and process optimizations to reduce allergenic gliadins in wheat flour
TypeArticle
Pagination1338–1345
Volume Number196
dc.accessType Abstract Only


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