Structure−Physicochemical Function Relationships of Soybean Glycinin at Subunit Levels Assessed by Using Mutant Lines

Maruyama, Nobuyuki; Prak, Krisna; Motoyama, Shiori; Choi, Seon-Kang; Yagasaki, Kazuhiro; Ishimoto, Masao; Utsumi, Shigeru

doi:10.1021/jf048786y

Cited by 50 publications

(54 citation statements)

References 33 publications

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“…Each subunit is composed of an acidic and a basic polypeptide linked by a disulphide bond (Staswick et al, 1981). The five subunits form three groups according to the combination of acid and basic peptides (Maruyama et al, 2004). Subunits Gy1 and Gy5 are considered main epitopes for this protein (Schiller et al, 2014).…”

Section: Identified Allergensmentioning

confidence: 99%

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Products¹

2014

EFS2

117

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Following a request from the Food Safety Authority of Ireland, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA Panel) was asked to deliver a scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. In view of the request, the NDA Panel decided to update its previous opinions relative to food ingredients or substances with known allergenic potential listed in Annex IIIa of 2003/89/EC, as amended. These include cereals containing gluten, milk and dairy products, eggs, nuts, peanuts, soy, fish, crustaceans, molluscs, celery, lupin, sesame, mustard and sulphites. The opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. It includes information on the prevalence of food allergy in unselected populations, proteins identified as food allergens, cross-reactivities, the effects of food processing on the allergenicity of foods and ingredients, methods for the detection of allergens and allergenic foods, doses observed to trigger adverse reactions in sensitive individuals and risk assessment methodologies that have been used to derive individual and population thresholds for selected allergenic foods. The present opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. For each food ingredient or substance listed in Annex IIIa, it includes information on the prevalence of food allergy in unselected populations, on proteins identified as food allergens, on cross-reactivities, on the effects of food processing on the allergenicity of foods and ingredients, on methods for the detection of allergens and allergenic foods, and on doses observed to trigger adverse reactions in sensitive individuals.Immune-mediated adverse reactions to foods manifest with clinical signs and symptoms of variable severity and duration, which may affect different organs and systems. Anaphylactic reactions to food are IgE mediated and may occur at any age. Non-IgE-mediated food allergy includes a wide range of diseases, including protein-induced enterocolitis and eosinophilic oesophagitis.A careful family and clinical history are the basis for diagnosis of food allergy. Food diaries, skin prick tests (SPTs), allergen-specific IgE measurements, food elimination diets and food challenges are part of the standard protocol for the diagnosis of food allergy. A positive SPT indicates sensitisation to the tested food, but it is not diagnostic of food allergy. Allergen-specific serum IgE antibodies similarly denote sensitisation to a particular food, but they are not diagnostic without a clinical history or food challenge. The use of atopy patch tests for the diagnosis of food allergy is controversial. Other available tests have no current role in the diagnosis of food allergy. Diag...

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Section: Identified Allergensmentioning

confidence: 99%

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Products¹

2014

EFS2

117

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“…The five subunits (A 1a B 2 , A 1b B 1b , A 2 B 1a , A 3 B 4 and A 5 A 4 B 3 ) have been isolated, purified (Staswick et al, 1981;Maruyama et al, 2004) and characterized using amino-terminal amino acid sequence (Moreira, Hermodson, Larkins, & Nielsen, 1979;Staswick et al, 1981). Many works about the polypeptides have been carried out for amino acid sequence analysis (Staswick, Hermodson, & Nielsen, 1984), emulsifying properties of acidic polypeptides (Liu, Lee, & Damodaran, 1999), functional properties of polypeptides with different MW obtained by special methods (Dias et al, 2003), as well as their physicochemical and adhesion properties (Mo, Zhong, Wang, & Sun, 2006).…”

Section: Introductionmentioning

confidence: 99%

Physicochemical and functional properties of acidic and basic polypeptides of soy glycinin

Yuan

Yang

Tang

et al. 2009

Food Research International

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“…2a-d). However, very low solubility was reported for glycinin at acidic pH and high ionic strength conditions (μ= 0.5) [3,11], which was also reported for cruciferin composed of heteromeric subunits [9,[11][12][13]. The effect of neutral salts, such as NaCl, on ion-protein interactions for 11S globulins (e.g., glycinin) is concentration dependent.…”

Section: Solubilitymentioning

confidence: 98%

“…Therefore, structural, functional, and physico-chemical data obtained from WT cruciferin cannot be related to individual subunit types. Studies on glycinin, the 11S globulin of Glycine max, showed that the subunits A1bB2, A2B1a, A5A4B3, A3B4, and A1aB1b possess distinct structural and physico-chemical properties [3][4][5][6], which are responsive to manipulation through protein engineering [7][8][9][10]. The current understanding of cruciferin subunit structure and function is very limited.…”

Section: Introductionmentioning

confidence: 99%

Solubility, Heat-Induced Gelation and Pepsin Susceptibility of Cruciferin Protein as Affected by Subunit Composition

et al. 2014

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This study examined the solubility, heat-induced gel formation ability, and pepsin susceptibility of cruciferin with mixed (wild type, WT) or identical subunits (CRUA, CRUB, or CRUC). All cruciferin species exhibited minimal solubility at pH 4.0 and slight solubility between pH 7.5 and 8, which was not influenced by the presence of NaCl. Increasing temperature to 90°C did not affect the solubility of CRUC, but affected the solubility of other cruciferins between pH 4.0 and 8.0. Changes of secondary structure of cruciferins in a range of pH suggested structural alterations of the hexameric assembly might occur at pH 2.0. Near neutral pH was suitable to form heat-induced gels of WT, CRUA, and CRUB species. Although pH 2.0 was suitable for CRUC to form a strong gel, the same pH inhibited CRUB gel formation. High salt content (0.5 M NaCl) at neutral pH did not change the gel formation ability of WT, CRUA, or CRUB, but affected the gel characteristics. All cruciferins were hydrolyzed by pepsin, but the CRUC was degraded at a slower rate than the others. Trimer surface characteristics and the orientation and interaction of the HVR-I region of the hexameric assembly could be main structural factors for these property differences. Although the CRUC subunit showed properties that deviated from other species, the influence of CRUA and CRUB subunits seemed more prominent in the mixed subunit hexamer of WT.

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Structure−Physicochemical Function Relationships of Soybean Glycinin at Subunit Levels Assessed by Using Mutant Lines

Cited by 50 publications

References 33 publications

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Physicochemical and functional properties of acidic and basic polypeptides of soy glycinin

Solubility, Heat-Induced Gelation and Pepsin Susceptibility of Cruciferin Protein as Affected by Subunit Composition

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