Shridhar K. Sathe

Food allergies are on the rise in Western countries. With the food allergen labeling requirements in the US and EU, there is an interest in learning how food processing affects food allergens. Numerous foods are processed in different ways at home, in institutional settings, and in industry. Depending on the processing method and the food, partial or complete removal of the offending allergen may be possible as illustrated by reduction of peanut allergen in vitro IgE immunoreactivity upon soaking and blanching treatments. When the allergen is discretely located in a food, one may physically separate and remove it from the food. For example, lye peeling has been reported to produce hypoallergenic peach nectar. Protein denaturation and/or hydrolysis during food processing can be used to produce hypoallergenic products. This paper provides a short overview of basic principles of food processing followed by examples of their effects on food allergen stability. Reviewed literature suggests assessment of processing effects on clinically relevant reactivity of food allergens is warranted.

ABSTRACT:  Eight almond ( Prunus dulcis L.) cultivars from 12 different California counties, collected during crop years 2004 to 2005 and 2005 to 2006, were extracted with petroleum ether. The extracts were subjected to GC‐MS analyses to determine fatty acid composition of soluble lipids. Results indicated palmitic (C16:0), oleic (C18:1), linoleic (C18:2), and α‐linolenic (C18:3) acid, respectively, accounted for 5.07% to 6.78%, 57.54% to 73.94%, 19.32% to 35.18%, and 0.04% to 0.10%; of the total lipids. Oleic and linoleic acid were inversely correlated ( r =–0.99, P = 0.05) and together accounted for 91.16% to 94.29% of the total soluble lipids. Statistically, fatty acid composition was significantly affected by cultivar and county.

Soybean glycinin (11S) and β-conglycinin (7S) were subjected to select chemical treatments at various concentrations and resulting changes in protein structures were investigated by circular dichroism (CD) and fluorescence spectrometry. Fluorescence quenching results indicated that urea ≥3 M caused significant unfolding of 11S, but not that of 7S. GuHCl was more effective than urea in denaturation of 11S. A two-step transition in 11S structure was observed with a possible existence of a folding intermediate at 2.5 M GuHCl. Sodium dodecyl sulfate (SDS) measurably altered secondary and tertiary structures of 11S and 7S below SDS critical micellar concentration (CMC), possibly due to formation of mixed peptide-SDS micelles. SDS treatment increased α-helical and unordered structures of both proteins at the expense of β-sheet structure. NaCl and CaCl₂ caused a significant decrease in fluorescence intensity without shifting emission λ_max. Exposure of 7S and 11S to NaSCN respectively at ≥0.3 and ≥0.6 M NaSCN caused a significant increase in fluorescence intensity measured at the corresponding λ_max of the protein. β-Mercaptoethanol (β-ME), N-ethylmaleimide (NEM), and phytic acid caused variable red shifts, 2.5–4 nm, in the emission λ_max.

Val bean (Lablab purpureus L.) proteins were fractionated using the Osborne protein fractionation scheme and biochemically characterized. The seed flour contained 302 g kg⁻¹ protein (micro‐Kjeldahl N × 6.25) on a dry weight basis. Albumin, globulin, prolamin, and glutelin accounted for 22.8%, 45.1%, 1.8% and 30.3%, respectively, of the total soluble seed proteins. Among the solvents tested, 0.1 mol L⁻¹ aqueous NaOH was the most effective protein solubilizer. Isoelectric focusing indicated the seed proteins to be predominantly acidic (pI range was ∼4–7). Val globulin is a glycoprotein composed of at least three polypeptides in the molecular mass range 51–64 kDa. Albumin fraction had the highest trypsin inhibitory activity, while the globulin fraction registered the highest hemagglutinating activity. Sulfur amino acids were the first limiting amino acids in the total seed proteins. The proportion of essential to total [E/T(%)] amino acids for the bean flour was 36.97%. Among the protein fractions, glutelin fraction had the highest E/T (42.86%) followed by albumin (41.57%), globulin (39.87%), and prolamin (39.15%). Native globulin, although resistant to pepsin, was effectively digested in vitro upon moist heat (100 °C, 30 min) denaturation. Copyright © 2007 Society of Chemical Industry

Three marketing varieties of almonds; Carmel, Mission, and Nonpareil; were analyzed for proximate composition and protein nutritive quality. Moisture, lipids, protein, ash, sugars, and tannins ranges were 3.05–4.33%, 43.37–47.50%, 20.68–23.30%, 3.74–4.56%, 5.35–7.45%, and 0.12–0.18%, respectively. No detectable hemagglutinating and trypsin inhibitory activities were present in Carmel, Mission, and Nonpareil almonds. Amino acid analyses indicated the sulfur amino acids (methionine + cysteine), lysine, and threonine to be the first, second, and third limiting amino acids in almonds when compared to the recommended amino acid pattern for children 2–5-year old. However, compared to the recommended amino acid pattern for adults, sulfur amino acids were the only limiting amino acids in almonds tested. True Protein Digestibility (% TPD) values for Carmel, Mission, and Nonpareil were 88.55 ± 1.26, 92.25 ± 1.05, and 82.62 ± 1.47, respectively. Protein Digestibility Corrected Amino Acid Scoring (PDCAAS) values suggested almond proteins to be of poor nutritional quality.

For various reasons, a considerable majority of the global population must rely on plant proteins obtained from cereals, legumes (including oilseeds), fruits, vegetables, and nuts to satisfy dietary protein needs and requirements. Edible seeds are a significant source of proteins in livestock production and in the manufacture of pet foods. In addition, edible seeds are important sources of carbohydrates (including dietary fiber), minerals, and certain vitamins in human and animal food supply. For various reasons, edible seeds are underutilized as human food. To fully exploit this renewable natural resource to its full potential, focused research efforts are warranted. With increased number of seed proteins being identified as food allergens, renewed interest in seed proteins is evident. In this article, a brief overview of seed proteins with special reference to their allergenicity is provided. An attempt is made to identify areas needing further research.

Whole unprocessed almonds, cashew nuts and walnuts were each subjected to γ‐irradiation (1, 5, 10 and 25 kGy) followed by heat processing including autoclaving (121 °C, 15 psi for 15 and 30 min), dry roasting (138 and 160 °C for 30 min each, 168 and 177 °C for 12 min each), blanching (100 °C for 5 and 10 min), oil roasting (191 °C, 1 min) and microwave heating (500 W for 1 and 3 min). Rabbit polyclonal antibodies were raised against each major protein isolated from defatted, but not subjected to γ‐irradiation and/or any thermal processing, almond, cashew nut and walnut flours. Immunoreactivity of almond, cashew nut and walnut proteins soluble in borate saline buffer, normalised to 1 mg protein ml⁻¹ for all samples, was determined by inhibition enzyme‐linked immunosorbent assay (ELISA) and Western blotting. ELISAs and Western blotting experiments indicated that almond, cashew nut and walnut proteins exposed to γ‐irradiation alone or followed by various thermal treatments remained antigenically stable. Copyright © 2004 Society of Chemical Industry

A water soluble storage albumin from Inca peanut (IPA) accounted for ∼25% (w/w) of defatted seed flour weight, representing 31% of the total seed protein. IPA is a 3S storage protein composed of two glycosylated polypeptides, with estimated molecular weights (MW) of 32800 and 34800 Da, respectively. IPA has an estimated sugar content of 4.8% ± 0.92% (n = 6). IPA is a basic protein (pI of ∼9.4) and contains all of the essential amino acids in adequate amounts when compared to the FAO/WHO recommended pattern for a human adult. The tryptophan content of IPA is unusually high (44 mg/g of protein), whereas the phenylalanine content is low (9 mg/g of protein). IPA is a highly digestible protein in vitro. Keywords: Inca peanut; albumin; storage protein; in vitro protein digestibility; glycoprotein