Antigenic Stability of Pecan [Carya illinoinensis (Wangenh.) K. Koch] Proteins: Effects of Thermal Treatments and in Vitro Digestion
Rabbit polyclonal antibody-based inhibition ELISA as well as immunoblotting analyses of proteins extracted from variously processed pecans (cv. Desirable) indicate that pecan proteins are antigenically stable. Pecan antigens were more sensitive to moist heat than dry heat processing treatments. SDS-...
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Published in | Journal of agricultural and food chemistry Vol. 54; no. 4; pp. 1449 - 1458 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
22.02.2006
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Subjects | |
Online Access | Get full text |
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Summary: | Rabbit polyclonal antibody-based inhibition ELISA as well as immunoblotting analyses of proteins extracted from variously processed pecans (cv. Desirable) indicate that pecan proteins are antigenically stable. Pecan antigens were more sensitive to moist heat than dry heat processing treatments. SDS-PAGE and immunoblotting analysis of the native and heat-denatured proteins that were previously subjected to in vitro simulated gastric fluid digestions indicate that stable antigenic peptides were produced. Both enzyme-to-substrate ratio and digestion time were influential in determining the stability of pecan polypeptides. The stable antigenic polypeptides may serve as useful markers in developing assays suitable for the detection of trace amounts of pecans in foods. Keywords: Pecans; proteins; inhibition ELISA; Western blotting; antigenic stability; digestibility |
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Bibliography: | ark:/67375/TPS-X8TKL8ZR-C istex:3E428998D779813DAE821B1792843F7F74ED8395 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-8561 1520-5118 |
DOI: | 10.1021/jf0520802 |