Shridhar K Sathe

Florida State University, Tallahassee, Florida, United States

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Publications (136)487.78 Total impact

  • [Show abstract] [Hide abstract]
    ABSTRACT: The potential epitope of a recombinant food allergen protein, cashew Ana o 1, reactive to monoclonal antibody, mAb 2G4, has been mapped by solution-phase amide backbone H/D exchange (HDX) monitored by Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS). Purified mAb 2G4 was incubated with recombinant Ana o 1 (rAna o 1) to form antigen:monoclonal antibody (Ag:mAb) complexes. Complexed and uncomplexed (free) rAna o 1 were then subjected to HDX-MS analysis. Five regions protected from H/D exchange upon mAb binding are identified as potential conformational epitope-contributing segments. Copyright © 2015 John Wiley & Sons, Ltd.
    Journal of Mass Spectrometry 06/2015; 50(6). DOI:10.1002/jms.3589 · 2.71 Impact Factor
  • Aditya U. Joshi, Changqi Liu, Shridhar K. Sathe
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    ABSTRACT: Proximate composition of select commercially sold cereal, oilseed, dry bean, and tree nut seeds was determined. Full fat and defatted seed flours were evaluated for their color, bulk density, Water Holding Capacity (WHC), Oil Holding Capacity (OHC), and Least Gelation Concentration (LGC). On a dry weight basis (dwb), rice, wheat, pearl millet, black gram, chickpea, and soybean flours registered higher moisture content among the tested seeds. Seed protein content (dwb) ranged from 7.79 ± 0.72 g/100 g (rice) to 31.48 ± 0.76 g/100 g (soybean). On a dwb, rice (1.23 ± 0.07 g/100 g) and macadamia (67.63 ± 0.04 g/100 g) registered the lowest and the highest amount of lipid. Defatting typically improved flour lightness as indicated by an increase in the L∗ value as compared to the corresponding full fat flour. Upon defatting, bulk density of the tested flours decreased. Under the experimental conditions, WHC of full fat flours (range 0.66 ± 0.11–2.97 ± 0.02 g/g improved upon defatting (range 1.48 ± 0.00–3.53 ± 0.02 g/g). OHC of full fat flours (range 0.64 ± 0.14–1.44 ± 0.07 g/g) increased upon defatting (range 1.00 ± 0.12–3.40 ± 0.46 g/g). LGC of the tested flours ranged from 8 g/100 mL–18 g/100 mL.
    Lebensmittel-Wissenschaft und-Technologie 01/2015; 60(1):325–331. DOI:10.1016/j.lwt.2014.08.038 · 2.47 Impact Factor
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    ABSTRACT: The aims of the present work were to assess digestibility of almond protein in the upper gastrointestinal tract, evaluate the effects of food matrix on protein release and assess the persistence of immunoreactive polypeptides generated during simulated digestion. Prunin, the most abundant protein in almond flour, was sensitive to pepsin, with complete digestion after 20 min in the gastric phase. Addition of the surfactant phosphatidylcholine did not affect the rate and kinetic of digestion, as observed by SDS-PAGE analysis and HPLC, in the stomach and the small intestine of either natural or blanched almond flour. However, incorporation of almond flour into a food matrix, such as chocolate mousse and Victorian sponge cake, decreased the rate of almond protein degradation by pepsin and immunoreactivity of almond polypeptides detected by dot blots and sandwich ELISA retained better. Most of the almond protein identified by in-gel tryptic digestion and MALDI-TOF analysis corresponded to prunin, with pl values of 5-7. Further human sera studies are warranted to investigate the relationship between food matrix and almond allergy.
    Lebensmittel-Wissenschaft und-Technologie 11/2014; 59(1):439-447. DOI:10.1016/j.lwt.2014.05.005 · 2.47 Impact Factor
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    ABSTRACT: Amandin presence in 108 almond genotypes/hybrids and 80 almond marketing varieties grown in different locations was determined using murine monoclonal antibody 4C10-based sandwich ELISA. The results indicated that amandin was present in all the tested samples. The ELISA immunoreactivity variations were up to 8 fold among genotypes/hybrids and 2.5 fold among the almond marketing varieties. Amandin content variations were also confirmed using Western blot and dot blot. No correlation was observed between almond seed size and total soluble protein or amandin content.
    Lebensmittel-Wissenschaft und-Technologie 08/2014; 60(1):535-543. DOI:10.1016/j.lwt.2014.08.042 · 2.47 Impact Factor
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    ABSTRACT: Influence of high pressure processing (HPP) at 450 and 600 MPa, 30 degrees C for various holding times (0, 30, 60,180, 300 and 600 s) on almond milk amandin was investigated. The immunoreactivity of pressure treated almond milk was compared with raw and thermally processed (TP) almond milk (72, 85 and 99 degrees C for 0 to 300 s) using a sandwich enzyme-linked immunosorbent assay (ELISA), Western blot and dot blot. Monoclonal antibodies (mAbs) targeting linear (4F10) and conformational (4C10) epitopes on amandin were used to assess amandin immunoreactivity. To determine the aggregation of almond proteins, almond milk protein solubility was quantified after 300s of HPP (up to 600 MPa, 30 degrees C) and TP (at 72,85 and 99 degrees C, 0.1 MPa). After HPP (for all holding times), amandin can no longer be detected by the anti-conformational mAb in ELISA while signal generated from the anti-linear epitopes mAb was reduced by half (P < 0.05). On the other hand, most TP samples did not show significant reductions in immunoreactivity (P > 0.05) unless processed at 85 and 99 degrees C for 300 s. Western blot and dot blot also confirmed the loss of immunoreactivity by both antibodies for HPP almond milk. The reduced band intensity of the 61 and 63 kDa polypeptides and concomitant appearance of high molecular weight polypeptides in Western blot indicated that the observed decrease in immunoreactivity was partly due to the aggregation of amandin. The tested HPP and TP treatments respectively caused a maximum of similar to 70% and similar to 75% reduction in protein solubility. The study demonstrated that the loss of protein solubility, rather than the epitope destruction, may be responsible for the observed decrease in amandin immunoreactivity. (C) 2014 Published by Elsevier Ltd.
    Food Research International 08/2014; 62:215-222. DOI:10.1016/j.foodres.2014.02.021 · 3.05 Impact Factor
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    ABSTRACT: Influence of high pressure processing (HPP) at 450 and 600 MPa, 30 °C for various holding times (0, 30, 60,180, 300 and 600 s) on almond milk amandin was investigated. The immunoreactivity of pressure treated almond milk was compared with raw and thermally processed (TP) almond milk (72, 85 and 99 °C for 0 to 300 s) using a sandwich enzyme-linked immunosorbent assay (ELISA), Western blot and dot blot. Monoclonal antibodies (mAbs) targeting linear (4F10) and conformational (4C10) epitopes on amandin were used to assess amandin immunoreactivity. To determine the aggregation of almond proteins, almond milk protein solubility was quantified after 300 s of HPP (up to 600 MPa, 30 °C) and TP (at 72, 85 and 99 °C, 0.1 MPa). After HPP (for all holding times), amandin can no longer be detected by the anti-conformational mAb in ELISA while signal generated from the anti-linear epitopes mAb was reduced by half (P < 0.05). On the other hand, most TP samples did not show significant reductions in immunoreactivity (P > 0.05) unless processed at 85 and 99 °C for 300 s. Western blot and dot blot also confirmed the loss of immunoreactivity by both antibodies for HPP almond milk. The reduced band intensity of the 61 and 63 kDa polypeptides and concomitant appearance of high molecular weight polypeptides in Western blot indicated that the observed decrease in immunoreactivity was partly due to the aggregation of amandin. The tested HPP and TP treatments respectively caused a maximum of ~ 70% and ~ 75% reduction in protein solubility. The study demonstrated that the loss of protein solubility, rather than the epitope destruction, may be responsible for the observed decrease in amandin immunoreactivity.
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    ABSTRACT: A sandwich ELISA using anti-almond soluble protein rabbit pAbs as capture and murine mAb 4C10 as the detection antibodies was developed. The assay is specific and sensitive (3-200 ng almond protein/mL) for almond detection. The standardized assay is accurate (<15% CV) and reproducible (intra- and inter-assay variability <15% CV). The assay did not register any cross-reactivity with the tested food matrices suggesting the assay to be almond amandin specific. The assay could detect the presence of declared almond in the tested matched commercial samples. Further, the assay reliably detected the presence of almonds in the laboratory prepared food samples spiked with almond flour. Key Words: Almond, ELISA, mAb 4C10, Detection, Assay.
    Journal of Agricultural and Food Chemistry 10/2013; 61(45). DOI:10.1021/jf402851k · 3.11 Impact Factor
  • Leanna N Willison, Shridhar K Sathe, Kenneth H Roux
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    ABSTRACT: Allergic reactions to tree nuts are a growing global concern as the number of affected individuals continues to rise. Unlike some food allergies, tree nuts can cause severe reactions that persist throughout life. The tree nuts discussed in this review include those most commonly responsible for allergic reactions: cashew, almond, hazelnut, walnut, pecan, Brazil nut, pistachio, and chestnut. The native allergenic proteins derived from tree nuts are frequently difficult to isolate and purify and may not be adequately represented in aqueous nut protein extracts. Consequently, defined recombinant allergens have become useful reagents in a variety of immunoassays aimed at the diagnosis of tree nut allergy, assessing cross-reactivity between various nuts and other seeds, mapping of IgE binding epitopes, and analyzing the effects of the food matrix, food processing, and gastric digestion on allergenicity. This review describes the approaches that can be used for the production of recombinant tree nut allergens and addresses key issues associated with their production and downstream applications.
    Methods 07/2013; 66(1). DOI:10.1016/j.ymeth.2013.07.033 · 3.22 Impact Factor
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    ABSTRACT: The potential epitopes of a recombinant food allergen protein, cashew Ana o 2, reactive to polyclonal antibodies, were mapped by solution-phase amide backbone H/D exchange (HDX) coupled with Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS). Ana o 2 polyclonal antibodies were purified in the serum from a goat immunized with cashew nut extract. Antibodies were incubated with recombinant Ana o 2 (rAna o 2) to form antigen:polyclonal antibody (Ag:pAb) complexes. Complexed and uncomplexed (free) rAna o 2 were then subjected to HDX-MS analysis. Four regions protected from H/D exchange upon pAb binding are identified as potential epitopes and mapped onto a homologous model.
    Journal of the American Society for Mass Spectrometry 05/2013; DOI:10.1007/s13361-013-0644-7 · 3.19 Impact Factor
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    ABSTRACT: The purpose of this study was to determine if there were differences between adolescents and parents in their perceptions of parental indulgence, stress (economic and life), and life satisfaction. In addition, using the conceptual frameworks of family ecosystems and developmental theory, the relationships between the three types of parental indulgence (soft structure, overnurturance, and giving too much), economic stress, life stress, and life satisfaction were examined for parents and adolescent children. Findings indicated that adolescents perceived higher levels of stress and soft structure as compared to their parents, whereas parents perceived higher levels of economic stress. Additionally, each type of parental indulgence affected parent and adolescent life stress and life satisfaction differently. Implications for research and practice are discussed.
    Journal of Family Social Work 05/2013; 16(3):205-224. DOI:10.1080/10522158.2013.786776
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    ABSTRACT: Tree nuts are a widely consumed food. Although enjoyed safely by most individuals, allergic reactions to tree nuts, including almond, are not uncommon. Almond prunin (Pru du 6), an 11S globulin (legumin), is an abundant nut seed protein and a major allergen. Conformational epitope mapping studies of prunin have been performed with a murine monoclonal antibody (mAb) 4C10. This mAb reacts with non-reduced but not reduced prunin in immunoblotting assays, indicating the recognition of a conformational epitope. 4C10 competes with patient IgE, as assessed by ELISA, indicating clinical significance of the epitope. To characterize the 4C10 epitope, hydrogen/deuterium exchange (HDX) monitored by 14.5T Fourier transform ion cyclotron resonance mass spectrometry (MS) was performed on the native prunin-4C10 complex and on uncomplexed native prunin. Several epitope candidate peptides that differ in deuterium uptake between the complexed and uncomplexed forms were identified. The epitope was further mapped by analyzing chimeric molecules incorporating segments of the homologous soybean allergen, Gly m 6, in immunoassays. These data indicate that the 4C10 epitope overlaps with a subset of patient IgE binding epitopes on almond prunin and further supports HDX-MS as a valid technique for mapping conformational epitopes.
    Molecular Immunology 03/2013; DOI:10.1016/j.molimm.2013.02.004 · 3.00 Impact Factor
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    ABSTRACT: Effects of different solvents, ionic strength, and pH on Inca peanut seed protein solubility were assessed by quantitatively analyzing solubilized proteins using Lowry and Bradford methods. Soluble proteins were fractionated using Osborne procedure and the polypeptide composition of solubilized proteins was determined by one dimensional 25 % monomer acrylamide linear gradient SDS-PAGE. Osborne protein fractions were analyzed by the 2D gel electrophoresis. Total seed proteins were efficiently solubilized by 2 M NaCl among the tested solvents. The soluble seed proteins registered a minimum solubility at pH ~4.0. Osborne protein fractions, albumins, globulins, prolamins, and glutelins accounted for 43.7, 27.3, 3.0, and 31.9 %, respectively, of the total aqueous soluble proteins. Soluble seed flour proteins are mainly composed of polypeptides in the MW range of 6-70 kDa of which the predominant polypeptides were in the 20-40 kDa range. Prolamin fraction was mainly composed of four polypeptides (MW < 15 kDa). Glycoprotein staining indicated 32-35 and <14 kDa peptides to be positive.
    Plant Foods for Human Nutrition 08/2012; 67(3):247-55. DOI:10.1007/s11130-012-0301-5 · 2.42 Impact Factor
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    ABSTRACT: A survey of adolescents aged 15 to 16 years was used to examine the relationship between their perceptions of indulgent parenting and adolescent weight status to overall satisfaction with life, as associated with adolescent perceptions of body image, health and stress. In addition, perceptions of parental indulgence were examined in terms of their association with adolescent eating behaviours and health. The results revealed a paradox related to indulgent parenting, with both positive and negative outcomes for adolescents. Structural equation analyses showed that parental indulgence was not only related to lower stress and higher life satisfaction, but also to unhealthy eating behaviours. Path analysis indicated that both positive and negative eating outcomes for adolescents were related to parental indulgence. This research has many implications for both parent and adolescent health education, focusing on parenting styles, stress and healthy lifestyles.
    Stress and Health 08/2012; 28(3):211-21. DOI:10.1002/smi.1426 · 1.34 Impact Factor
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    ABSTRACT: The epitopes of a homohexameric food allergen protein, cashew Ana o 2, identified by two monoclonal antibodies, 2B5 and 1F5, were mapped by solution-phase amide backbone H/D exchange (HDX) coupled with Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) and the results were compared to previous mapping by immunological and mutational analyses. Antibody 2B5 defines a conformational epitope, and 1F5 defines a linear epitope. Intact murine IgG antibodies were incubated with recombinant Ana o 2 (rAna o 2) to form antigen-monoclonal antibody (Ag-mAb) complexes. mAb-complexed and uncomplexed (free) rAna o 2 were then subjected to HDX. HDX instrumentation and automation were optimized to achieve high sequence coverage by protease XIII digestion. The regions protected from H/D exchange upon antibody binding overlap and thus confirm the previously identified epitope-bearing segments: the first extension of HDX monitored by mass spectrometry to a full-length antigen-antibody complex in solution.
    Analytical Chemistry 08/2011; 83(18):7129-36. DOI:10.1021/ac201501z · 5.83 Impact Factor
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    ABSTRACT: Among tree nut allergens, pecan allergens remain to be identified and characterized. The objective was to demonstrate the IgE-binding ability of pecan 11S legumin and characterize its sequential IgE-binding epitopes. The 11S legumin gene was amplified from a pecan cDNA library and expressed as a fusion protein in Escherichia coli. The native 11S legumin in pecan extract was identified by mass spectrometry/mass spectrometry (MS/MS). Sequential epitopes were determined by probing the overlapping peptides with three serum pools prepared from different patients' sera. A three-dimensional model was generated using almond legumin as a template and compared with known sequential epitopes on other allergenic tree nut homologues. Of 28 patients tested by dot blot, 16 (57%) bound to 11S legumin, designated Car i 4. MS/MS sequencing of native 11S legumin identified 33 kDa acidic and 20-22 kDa basic subunits. Both pecan and walnut seed protein extracts inhibited IgE binding to recombinant Car i 4, suggesting cross-reactivity with Jug r 4. Sequential epitope mapping results of Car i 4 revealed weak, moderate, and strong reactivity of serum pools against 10, 5, and 4 peptides, respectively. Seven peptides were recognized by all three serum pools, of which two were strongly reactive. The strongly reactive peptides were located in three discrete regions of the Car i 4 acidic subunit sequence (residues 118-132, 208-219, and 238-249). Homology modeling of Car i 4 revealed significant overlapping regions shared in common with other tree nut legumins.
    Journal of Agricultural and Food Chemistry 06/2011; 59(17):9542-52. DOI:10.1021/jf2017447 · 3.11 Impact Factor
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    ABSTRACT: IgE-reactive proteins have been identified in almond; however, few have been cloned and tested for specific patient IgE reactivity. Here, we clone and express prunin 1 and prunin 2, isoforms of the major almond protein prunin, an 11S globulin, and assay each for IgE reactivity. Prunin isoforms were PCR-amplified from an almond cDNA library, sequenced, cloned and expressed in Escherichia coli. Reactivity to the recombinant (r) allergens, Pru du 6.01 and Pru du 6.02, was screened by dot blot and immunoblot assays using sera from almond-allergic patients and murine monoclonal antibodies (mAbs). Sequential IgE-binding epitopes were identified by solid-phase overlapping peptide analysis. Epitope stability was assessed by assaying denatured recombinant proteins by immunoblot. IgE reactivity to rPru du 6.01 and rPru du 6.02 was found in 9 of 18 (50%) and 5 of 18 patients (28%), respectively. Four patients (22%) demonstrated reactivity to both isoforms. Murine anti-almond IgG mAbs also showed greater reactivity to rPru du 6.01 than to rPru du 6.02. Both stable and labile epitopes were detected. Six IgE-binding sequential epitope-bearing peptide segments on Pru du 6.01 and 8 on Pru du 6.02 were detected using pooled almond-allergic sera. rPru du 6.01 is more widely recognized than rPru du 6.02 in our patient population. The identification of multiple sequential epitopes and the observation that treatment with denaturing agents had little effect on IgE-binding intensity in some patients suggests an important role for sequential epitopes on prunins.
    International Archives of Allergy and Immunology 06/2011; 156(3):267-81. DOI:10.1159/000323887 · 2.43 Impact Factor
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    ABSTRACT: Although pecans are associated with IgE-mediated food allergies, the allergens responsible remain to be identified and characterized. The 2S albumin gene was amplified from the pecan cDNA library. Dot-blots were used to screen the recombinant protein with pecan allergic patients' serum. The affinity purified native protein was analyzed by Edman sequencing and mass spectrometry/mass spectrometry (MS/MS) analysis. Cross-reactivity with walnut was determined by inhibition enzyme-linked immunosorbent assay (ELISA). Sequential epitopes were determined by probing the overlapping peptides with three different patients' serum pool. The 3-dimensional homology model was generated, and the locations of the pecan epitopes were compared with those of known sequential epitopes on other allergenic tree nut homologues. Of 28 patients tested by dot-blot, 22 (79%) bound to 2S albumin, designated as Car i 1. Edman sequencing and the MS/MS sequencing of native 2S albumin confirmed the identity of recombinant (r) Car i 1. Both pecan and walnut protein extracts inhibited the IgE-binding to rCar i 1. Sequential epitope mapping indicated weak, moderate, and strong reactivity against 12, 7, and 5 peptides, respectively. Of the 11 peptides recognized by all serum pools, 5 peptides were strongly reactive and located in 3 discrete regions of the Car i 1 (amino acids 43-57, 67-78, and 106-120). Three-dimensional modeling revealed IgE-reactive epitopes to be solvent accessible and share significant homology with other tree nuts providing a possible basis for previously observed cross-reactivity.
    Journal of Agricultural and Food Chemistry 03/2011; 59(8):4130-9. DOI:10.1021/jf104319d · 3.11 Impact Factor
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    ABSTRACT: Native, undenatured amandin and anacardein secondary structures were estimated to be, respectively, 56.4 and 49% β-sheet, 14 and 23.7% α-helix, and 29.6 and 27.4% random coil. Circular dichroic (CD) and fluorescence spectroscopy were used to assess structural changes in amandin and anacardein subjected to denaturing treatments that included heat (100 °C, 5 min), guanidium HCl (GuHCl), urea, sodium dodecyl sulfate (SDS), and reducing agent, 2% v/v β-mercaptoethanol (βME) + heat. Mouse monoclonal antibodies (mAbs) 4C10 and 4F10 directed against amandin and 1F5 and 4C3 directed against anacardein were used to assess the influence of denaturing treatments on the immunoreactivity of amandin and anacardein. Among the denaturing treatments investigated, SDS and β-ME caused a significant reduction in the immunoreactivity of amandin and anacardein when probed with mAb 4C10 and 4C3, respectively.
    Journal of Agricultural and Food Chemistry 01/2011; 59(1):386-93. DOI:10.1021/jf1030899 · 3.11 Impact Factor
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    ABSTRACT: Brazil nut storage proteins, 2S albumin, 7S vicilin, and an 11S legumin, were purified using column chromatography. Analytical ultracentrifugation of the purified albumin, vicilin, and legumin proteins, respectively, registered sedimentation coefficients of 1.8, 7.1, and 11.8 S. Under reducing conditions, the major polypeptide bands in 2S albumin were observed at 6.4, 10-11, and 15.2 kDa. The 7S globulin was composed of one 12.6 kDa, two approximately 38-42 kDa, and two approximately 54-57 kDa polypeptides, whereas the 11S globulin contained two major classes of polypeptides: approximately 30-32 and approximately 20-21 kDa. The 7S globulin stained positive when reacted with Schiff reagent, indicating that it is a glycoprotein. The estimated molecular mass and Stokes radius for 2S albumin and 7S and 11S globulins were 19.2 kDa and 20.1 A, 114.8 kDa and 41.1 A, and 289.4 kDa and 56.6 A, respectively. Circular dichroism spectroscopic analysis indicated the secondary structure of the three proteins to be mainly beta-sheets and turns. Emission fluorescence spectra of the native proteins registered a lambda(max) at 337, 345, and 328 nm for 2S albumin and 7S and 11S globulins, respectively. When probed with anti-Brazil nut seed protein rabbit polyclonal antibodies, 7S globulin exhibited higher immunoreactivity than 2S albumin and 11S globulin.
    Journal of Agricultural and Food Chemistry 05/2010; 58(9):5714-23. DOI:10.1021/jf9036326 · 3.11 Impact Factor
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    ABSTRACT: Amandin, the primary storage protein in almonds, contains key polypeptides recognized by almond-allergic patients. A variety of food matrices representing diverse categories of foods were analyzed to assess the effect of food matrix on amandin recognition and recovery using rabbit polyclonal antibody based immunoassays. Food matrices from dairy, nuts, and vegetables typically resulted in over-estimation of amandin. Some foods representing legumes and cereals resulted in over-estimation while others in under-estimation of amandin. The amandin recovery range was 116–198 μg/100μg (dairy) 110–292 μg/100μg (tree nuts), 43–304 μg/100μg (legumes), 106–183 μg/100μg (most cereals- with the exception of barley, whole-wheat flour, wild rice and raisin bran whole mix). Amandin recovery from spices was typically low (2–85 μg/100μg) with a few exceptions where higher recoveries were observed (121–334 μg/100μg). Salt (black and white), tea, confectionery (sugar, cocoa, dark chocolate), and fruits (1–83 μg/100μg) generally resulted in lower recoveries. Tested food matrices did not adversely affect amandin immunorecognition in Western blots. The pH and the extraction buffer type affected amandin recovery. The results suggest that food matrix effects as well as extraction conditions need to be carefully evaluated when developing immunoassays for amandin detection and quantification.
    Lebensmittel-Wissenschaft und-Technologie 05/2010; 43(4-43):675-683. DOI:10.1016/j.lwt.2009.11.012 · 2.47 Impact Factor

Publication Stats

4k Citations
487.78 Total Impact Points

Institutions

  • 1994–2015
    • Florida State University
      • • Department of Nutrition, Food & Exercise Sciences
      • • College of Human Sciences
      • • Department of Biological Science
      Tallahassee, Florida, United States
  • 2007
    • Virginia Polytechnic Institute and State University
      • Department of Food Science and Technology
      Blacksburg, Virginia, United States
  • 1980–2007
    • Utah State University
      • Department of Nutrition, Dietetics and Food Sciences
      Logan, Ohio, United States
  • 2006
    • Central Food Technological Research Institute
      • Department of Biochemistry and Nutrition (CFTRI)
      Mahisūr, Karnātaka, India
  • 1999–2006
    • University of California, Davis
      • • Division of Rheumatology/Allergy/Clinical Immunology
      • • Department of Internal Medicine
      Davis, California, United States
  • 1997–2006
    • Purdue University
      West Lafayette, Indiana, United States
  • 1982–2006
    • The University of Arizona
      Tucson, Arizona, United States
  • 1983
    • University of Illinois, Urbana-Champaign
      Urbana, Illinois, United States