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Juan De Dios Alche - One of the best experts on this subject based on the ideXlab platform.

  • identification of Seed Storage Proteins as the major constituents of the extra virgin olive oil proteome
    Food Chemistry: X, 2020
    Co-Authors: Antonio Castro, Elena Limacabello, Juan De Dios Alche
    Abstract:

    Abstract Proteins are minor components of extra virgin olive oil (EVOO), but the nature of the olive oil proteome is still elusive. In this paper, we have uncovered the EVOO proteome for the first time. Seed Storage Proteins of globulin-type were identified as the most abundant Proteins in EVOO, which also contains an active 13-lipoxygenase and several potential allergenic Proteins, including the “panallergen” profilin. We validated our proteomic data by Western blotting and enzyme activity assays. Our data also demonstrated that the Seed is the main source of Proteins in EVOO, while the contribution of the pulp is uncertain and needs further verification. The impact of EVOO Proteins on its stability and quality, and on human health is discussed.

  • characterization of olive Seed Storage Proteins
    Acta Physiologiae Plantarum, 2007
    Co-Authors: Wei Wang, Juan De Dios Alche, Maria Isabel Rodriguezgarcia
    Abstract:

    At present little is known about olive Seed Storage Proteins (SSPs). A better understanding of olive SSPs will be important for future biotechnology efforts. In the present study, we first developed a protocol relied on chloroform for preparing protein samples free of lipids from lipid-rich olive Seeds. Then, we characterized olive SSPs by SDS-PAGE, N-terminal sequencing and immunoblot. Two smaller subunits (20 and 21.5 kD) of SSPs were purified to homogeneity and used for antibody production or N-terminal sequencing. N-terminal sequencing confirmed that major olive SSPs are 11S globulins. Moreover, the components and size distribution of SSPs are identical among several olive cultivars examined, suggesting that their synthesis is highly conserved in this species. Olive SSPs are soluble in aqueous alcohol, with limited solubility in water and dilute salt. Thus, despite their homology with globulins, olive SSPs are similar in solubility to prolamins and different from globulins in other dicot plants. Finally, the accumulation of olive SSPs during fruit maturation was examined. Our results revealed that the accumulation of SSPs is time-dependent and tissue-specific, and only 105 days after pollination (DAP), did individual components of SSPs synthesize substantially, and accumulate rapidly in large quantities over a short period of time. Our results suggest that a 36 kD protein is the precursor of olive SSPs, and 90–105 DAP seems to be a crucial transition period (from a precursor to mature subunits) for the accumulation of SSPs.

P M Colman - One of the best experts on this subject based on the ideXlab platform.

  • Structure of Phaseolin at 2·2 Å Resolution: Implications for a Common Vicilin/Legumin Structure and the Genetic Engineering of Seed Storage Proteins
    Journal of molecular biology, 1994
    Co-Authors: Michael C Lawrence, Tina Izard, M Beuchat, Robert J Blagrove, P M Colman
    Abstract:

    Abstract The refinement to 2·2 A resolution of the three-dimensional structure of the Seed Storage protein phaseolin from the French bean (Phaseolus vulgaris) via an alternative crystal form is described. The refined structure reveals details of the molecule hitherto unobserved and in particular we identify the structural role of conserved residues within the broader 7 S (vicilin) family of Seed Storage Proteins. On this basis we are able to postulate a canonical model for the structure of the 7 S Proteins. This model in turn provides a means for interpreting the structure of the 11 S (legumin) family of Seed Storage Proteins, for which no X-ray diffraction data are available. The 11 S Proteins are shown to bear a much closer relationship to the 7 S Proteins than was previously recognized. The canonical model of the 7 S protein structure also provides a basis for proposing engineered mutations of these Proteins with the goal of enhancing nutritional and functional properties.

  • structure of phaseolin at 2 2 a resolution implications for a common vicilin legumin structure and the genetic engineering of Seed Storage Proteins
    Journal of Molecular Biology, 1994
    Co-Authors: Michael C Lawrence, Tina Izard, M Beuchat, Robert J Blagrove, P M Colman
    Abstract:

    Abstract The refinement to 2·2 A resolution of the three-dimensional structure of the Seed Storage protein phaseolin from the French bean (Phaseolus vulgaris) via an alternative crystal form is described. The refined structure reveals details of the molecule hitherto unobserved and in particular we identify the structural role of conserved residues within the broader 7 S (vicilin) family of Seed Storage Proteins. On this basis we are able to postulate a canonical model for the structure of the 7 S Proteins. This model in turn provides a means for interpreting the structure of the 11 S (legumin) family of Seed Storage Proteins, for which no X-ray diffraction data are available. The 11 S Proteins are shown to bear a much closer relationship to the 7 S Proteins than was previously recognized. The canonical model of the 7 S protein structure also provides a basis for proposing engineered mutations of these Proteins with the goal of enhancing nutritional and functional properties.

Antonio Castro - One of the best experts on this subject based on the ideXlab platform.

Suzanne S Teuber - One of the best experts on this subject based on the ideXlab platform.

  • extensive in vitro cross reactivity to Seed Storage Proteins is present among walnut juglans cultivars and species
    Clinical & Experimental Allergy, 2004
    Co-Authors: Sarah S Comstock, G Mcgranahan, W R Peterson, Suzanne S Teuber
    Abstract:

    Summary Background Tree nuts, including English walnuts (Juglans regia), are sources of food allergens often associated with life-threatening allergic reactions. It is unknown if Seed Storage Proteins from other Juglans species have IgE epitopes similar to those of the important English walnut allergens, Jug r 1 (2S albumin) and Jug r 2 (vicilin-like). Objective To screen for potential germplasm sources of hypoallergenic Seed Storage Proteins of relevance in walnut food allergy. We sought to identify English walnut cultivars (cvs) or other Juglans species that showed decreased IgE binding to major Seed Storage Proteins or an inability to cross-react with Jug r 1 or Jug r 2. Methods We determined if IgE in sera of patients who have had life-threatening systemic reactions to English walnut bound protein extracts from all tested walnut cvs (57 cvs total) or species (six) by Western immunoblot. Further, we used immunoblot inhibition to determine the in vitro cross-reactivity of Jug r 1 and Jug r 2, native and recombinant, with several walnut species. Results All walnut cvs and species contain allergenic Proteins. Furthermore, as shown by in vitro immunoblot inhibition, the major walnut allergens in the species tested cross-reacted with those in J. regia cv. Chandler and J. nigra cv. Thomas extracts. Conclusions Based on our findings, it is unlikely that a composite hypoallergenic walnut could be bred from available germplasm. In addition, patients with severe allergy to English walnut are likely to be clinically allergic to all commercial English walnut cvs and other closely related Juglans species.

Michael C Lawrence - One of the best experts on this subject based on the ideXlab platform.

  • Structure of Phaseolin at 2·2 Å Resolution: Implications for a Common Vicilin/Legumin Structure and the Genetic Engineering of Seed Storage Proteins
    Journal of molecular biology, 1994
    Co-Authors: Michael C Lawrence, Tina Izard, M Beuchat, Robert J Blagrove, P M Colman
    Abstract:

    Abstract The refinement to 2·2 A resolution of the three-dimensional structure of the Seed Storage protein phaseolin from the French bean (Phaseolus vulgaris) via an alternative crystal form is described. The refined structure reveals details of the molecule hitherto unobserved and in particular we identify the structural role of conserved residues within the broader 7 S (vicilin) family of Seed Storage Proteins. On this basis we are able to postulate a canonical model for the structure of the 7 S Proteins. This model in turn provides a means for interpreting the structure of the 11 S (legumin) family of Seed Storage Proteins, for which no X-ray diffraction data are available. The 11 S Proteins are shown to bear a much closer relationship to the 7 S Proteins than was previously recognized. The canonical model of the 7 S protein structure also provides a basis for proposing engineered mutations of these Proteins with the goal of enhancing nutritional and functional properties.

  • structure of phaseolin at 2 2 a resolution implications for a common vicilin legumin structure and the genetic engineering of Seed Storage Proteins
    Journal of Molecular Biology, 1994
    Co-Authors: Michael C Lawrence, Tina Izard, M Beuchat, Robert J Blagrove, P M Colman
    Abstract:

    Abstract The refinement to 2·2 A resolution of the three-dimensional structure of the Seed Storage protein phaseolin from the French bean (Phaseolus vulgaris) via an alternative crystal form is described. The refined structure reveals details of the molecule hitherto unobserved and in particular we identify the structural role of conserved residues within the broader 7 S (vicilin) family of Seed Storage Proteins. On this basis we are able to postulate a canonical model for the structure of the 7 S Proteins. This model in turn provides a means for interpreting the structure of the 11 S (legumin) family of Seed Storage Proteins, for which no X-ray diffraction data are available. The 11 S Proteins are shown to bear a much closer relationship to the 7 S Proteins than was previously recognized. The canonical model of the 7 S protein structure also provides a basis for proposing engineered mutations of these Proteins with the goal of enhancing nutritional and functional properties.