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-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.
Department of Nutrition, Food and Exercise Sciences, Florida State University, Tallahassee, Florida 32306, USA.
Mahesh
M
Venkatachalam
Suzanne S
SS
Teuber
W Rich
WR
Peterson
Kenneth H
KH
Roux
Shridhar K
SK
Sathe
D000941:Antigens / Q000032:analysis* / Q000378:metabolism; D031325:Carya / Q000737:chemistry / Q000276:immunology*; D004063:Digestion; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006358:Hot Temperature; D015151:Immunoblotting; D010434:Pepsin A / Q000378:metabolism; D010940:Plant Proteins / Q000276:immunology / Q000378:metabolism; D012639:Seeds / Q000737:chemistry / Q000276:immunology*; D012995:Solubility
D000941:Antigens; D010940:Plant Proteins; D010434:Pepsin A