Agricultural Research Service - Pacific West Area

Almond (Prunus dulcis) is not only widely used as a human food as a result of its flavor, nutrients, and health benefits, but it is also one of the most likely tree nuts to trigger allergies. Almond allergens, however, have not been studied as extensively as those of peanuts and other selected tree nuts. This review provides an update of the molecular properties of almond allergens to clarify some confusion about the identities of almond allergens and our perspective on characterizing putative almond allergens. At present, the following almond allergens have been designated by the World Health Organization/International Union of Immunological Societies Allergen Nomenclature Sub-Committee: Pru du 3 (a non-specific lipid transfer protein 1, nsLTP1), Pru du 4 (a profilin), Pru du 5 (60S acidic ribosomal protein 2), Pru du 6 (an 11S legumin known as prunin) and Pru du 8 (an antimicrobial protein with cC3C repeats). Besides, almond vicilin and almond γ-conglutin have been identified as food allergens, although further characterization of these allergens is still of interest. In addition, almond 2S albumin was reported as a food allergen as a result of the misidentification of Pru du 8. Two more almond proteins have been called allergens based on their sequence homology with known food allergens and their 'membership' in relevant protein families that contain allergens in many species. These include the pathogenesis related-10 protein (referred to as Pru du 1) and the thaumatin-like protein (referred to as Pru du 2). Almonds thus have five known food allergens and five more likely ones that need to be investigated further. Published 2020. This article is a U.S. Government work and is in the public domain in the USA.

Recent efforts have been made to develop hot-air-dried chips as a value-added product for persimmon fruit (Diospyros kaki). However, the long-term quality of this product and its dependence on processing conditions and packaging type have not yet been explored. Hence, in this work, chips were prepared from “Hachiya” persimmon fruit in 2 ways: 2 mm thickness fruit slices, hot-air-dried for 5 hours (Preparation 2–5), and 6 mm slices, dried for 10 hours (Preparation 6–10). The dried chips were then packaged into 2 bag types (plastic zip-top and metallized polyethylene terephthalate (Met-PET) with desiccant packets), stored under ambient conditions, and sampled for moisture-related, microbial, texture, and chemical quality traits throughout the 1-year storage study. It was found that–with the exception of a marked decrease in ascorbic acid (vitamin C)—all 4 Preparation/Packaging combinations yielded products that maintained acceptable color, microbial, nutritional, and textural quality throughout the entire study. Compared to Preparation 2–5 chips, Preparation 6–10 chips generally had lower contents of healthy nutrients—antioxidant compounds, ascorbic acid, and carotenoids. Evidence of invertase activity was found for Preparation 6–10 chips but not for Preparation 2–5 chips. For both preparations, the contents of ascorbic acid and carotenoids experienced time-dependent decreases. Plastic zip-top bags and Met-PET bags with desiccant packets performed equally well as packaging for most of the quality metrics tracked during this study. Overall, this work has demonstrated that hot-air-drying of persimmon slices is a promising approach to create a value-added product with at least one year of shelf-life.

Almond is one of the tree nuts listed by U.S. FDA as a food allergen source. A food allergen identified with patient sera has been debated to be the 2S albumin or the 7S vicilin. However, neither of these proteins has been defined as a food allergen. The purpose of this study was to clone, express, and purify almond vicilin and test whether it is a food allergen. Western blot experiment was performed with 18 individual sera from patients with double-blind, placebo-controlled clinical almond allergy. The results showed that 44% of the sera contained IgE antibodies that recognized the recombinant almond vicilin, indicating that it is an almond allergen. Identifying this and additional almond allergens will facilitate the understanding of the allergenicity of seed proteins in tree nuts and their cross-reactivity.

Verification of the biocontent in biobased or "green" products identifies genuine products, exposes counterfeit copies, supports or refutes content claims, and ensures consumer confidence. When the biocontent includes protein, elemental nitrogen analysis is insufficient for verification since non-protein, but nitrogen-rich, content also may be present. However, the proteins can be extracted, separated by electrophoretic methods, and detected by UV absorption, protein stain, or immunoblotting. We utilized capillary zone electrophoresis (CZE) to separate proteins in a gliadin fraction that had been dissolved in aqueous ethanol (70%) and polyacrylamide gel electrophoresis (PAGE) to separate proteins in a gliadin-plus-glutenin fraction that had been dissolved in water containing both sodium dodecyl sulfate (SDS) and a reducing agent, dithiothreitol (DTT). We sought to verify the presence of these wheat grain proteins in wheat bread, a wheat flake cereal, wheat beer, and an enclosure for an antique automobile ignition coil reputed to contain wheat gluten. Proteins extracted from commercial wheat, corn, and soy flours served as standards, and proteins from heat-altered wheat served as process condition references. This approach successfully identified wheat proteins in these products especially if the process temperature did not exceed 120 degrees C. Above this temperature attenuation was nearly complete for proteins analyzed by CZE, but wheat-like patterns could still be recognized by one- and two-dimensional PAGE. Immunoblots reacted with grain-specific antibodies confirmed the identities of the cereal component especially when the protein pattern was greatly altered by thermal modification, specific protein adsorption, or protein digestion. In addition to verifying that wheat proteins are present, the complementary use of these methods can reveal whether whole wheat gluten or merely an alcohol-soluble fraction had been used in the specific product and indicate the level of thermal damage.

The PV-1 protein is endogenously expressed from a single mRNA in the mouse pancreatic MS-1 endothelial cell line as a 60-kDa N-glycosylated and 50-kDa non-glycosylated protein that form DTT sensitive oligomers. In the absence of cell permeabilization, PV-1 labels transcellular openings of variable size, many that penetrate through the cytosol with circular openings on the free and attached surface of the plasma membrane. Intracellular PV-1 is localized in perinuclear aggregates that can extend as a fibrous network through the cytosol and often surround the nuclear compartment. In some cells, PV-1 is organized as a large unipolar spindle-like structure that is often associated with severe deformation of the nucleus. The VEGF-R2 inhibitor SU5614 increased the PV-1 protein in a dose-dependent manner and inhibited MS-1 cell growth, without inducing apoptosis. This report provides compelling evidence for a functional role of PV-1 in the formation of large transendothelial channels and modulation of nuclear shape. Moreover, these data suggest the PV-1 protein is negatively regulated by VEGF.

This collaborative study was conducted to determine the total monomeric anthocyanin concentration by the pH differential method, which is a rapid and simple spectrophotometric method based on the anthocyanin structural transformation that occurs with a change in pH (colored at pH 1.0 and colorless at pH 4.5). Eleven collaborators representing commercial laboratories, academic institutions, and government laboratories participated. Seven Youden pair materials representing fruit juices, beverages, natural colorants, and wines were tested. The repeatability relative standard deviation (RSDr) varied from 1.06 to 4.16%. The reproducibility relative standard deviation (RSDR) ranged from 2.69 to 10.12%. The HorRat values were < or = 1.33 for all materials. The Study Director recommends that the method be adopted Official First Action.

ABSTRACT Field experiments may be useful for researchers and managers concerned with aquatic plants. Since experimental design and statistical analysis are closely related, this paper discusses statistical and practical considerations for conducting and evaluating field experiments with aquatic plants. Special emphasis is given to the analysis of variance, assumptions required for its use, and concepts related to it (e.g., statistical power, means comparison procedures, treatment structure, pseudoreplication, etc.). The paper concludes with a brief introduction to papers in the literature which illustrate the use of field experiments for studying aquatic plants.

Journal Article What's on the Farm? Get access Martin H. Rogoff Martin H. Rogoff US Department of Agriculture, Agricultural Research Service, Pacific West Area Western Regional, Research Center, Albany, CA 94710 Search for other works by this author on: Oxford Academic Google Scholar BioScience, Volume 39, Issue 6, June 1989, Pages 356–357, https://doi.org/10.2307/1311061 Published: 01 June 1989