Structural Stability and Surface Activity of Sunflower 2S Albumins and Nonspecific Lipid Transfer Protein

Berecz, Bernadett; Mills, E. N. Clare; Tamás, László; Láng, F.; Shewry, Peter R.; Mackie, Alan

doi:10.1021/jf100554d

Cited by 31 publications

(24 citation statements)

References 37 publications

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“…Although it still remains unclear what makes an allergen an allergen, properties preserving its structure, such as stability to low pH, bile salts, and proteolytic degradation, is a fundamental feature of a protein to survive the transport through the GI tract and reach the gut‐associated lymphoid tissue. Several 2S albumins have been shown to be highly resistant to GI digestion retaining their compact structure .…”

Section: Discussionmentioning

confidence: 99%

Cor a 14, the allergenic 2S albumin from hazelnut, is highly thermostable and resistant to gastrointestinal digestion

Pfeifer

Bublin

Dubiela

et al. 2015

Molecular Nutrition Food Res

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ScopeAllergens from nuts frequently induce severe allergic reactions in sensitive individuals. The aim of this study was to elucidate the physicochemical characteristics of natural Cor a 14, the 2S albumin from hazelnut.Methods and resultsCor a 14 was purified from raw hazelnuts using a combination of precipitation and chromatographic techniques. The protein was analyzed using gel electrophoresis, MS, and far‐UV circular dichroism (CD) analyses. The immunoglobulin E (IgE) binding of native, heat‐treated, and in vitro digested Cor a 14 was studied. We identified two different Cor a 14 isoforms and showed microclipping at the C‐terminus. CD spectra at room temperature showed the typical characteristics of 2S albumins, and temperatures of more than 80°C were required to start unfolding of Cor a 14 demonstrating its high stability to heat treatment. In vitro digestion experiments revealed that Cor a 14 is resistant to proteolytic degradation. Native and heat‐treated protein was recognized by sera from hazelnut allergic patients. However, denaturation of the allergen led to significantly reduced IgE binding.ConclusionWe identified two different isoforms of Cor a 14 displaying high stability under heating and gastric and duodenal conditions. Data from IgE‐binding experiments revealed the existence of both, linear and conformational epitopes.

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Section: Discussionmentioning

confidence: 99%

Cor a 14, the allergenic 2S albumin from hazelnut, is highly thermostable and resistant to gastrointestinal digestion

Pfeifer

Bublin

Dubiela

et al. 2015

Molecular Nutrition Food Res

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“…They possess four or five α-helices, which are stabilized by four conserved disulfide bridges formed by an eight-Cys motif (8CM) with the general form C-Xn-C-Xn-CC-Xn-CXC-Xn-C-Xn-C. The disulfide bridges promote the folding of the LTP into a very compact structure, which is extremely stable to heat and denaturation agents (Lindorff-Larsen and Winther 2001 ; Berecz et al 2010 ; Edstam et al 2014 ). The LTPs are in general synthesized with an N-terminal signal peptide that localizes the protein to the apoplastic space.…”

Section: Features and Classification Of Ltpsmentioning

confidence: 99%

Lipid transfer proteins: classification, nomenclature, structure, and function

Salminen

Blomqvist

Edqvist

2016

Planta

198

202

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The non-specific lipid transfer proteins (LTPs) constitute a large protein family found in all land plants. They are small proteins characterized by a tunnel-like hydrophobic cavity, which makes them suitable for binding and transporting various lipids. The LTPs are abundantly expressed in most tissues. In general, they are synthesized with an N-terminal signal peptide that localizes the protein to spaces exterior to the plasma membrane. The in vivo functions of LTPs are still disputed, although evidence has accumulated for a role in the synthesis of lipid barrier polymers, such as cuticular waxes, suberin, and sporopollenin. There are also reports suggesting that LTPs are involved in signaling during pathogen attacks. LTPs are considered as key proteins for the plant’s survival and colonization of land. In this review, we aim to present an overview of the current status of LTP research and also to discuss potential future applications of these proteins. We update the knowledge on 3D structures and lipid binding and review the most recent data from functional investigations, such as from knockout or overexpressing experiments. We also propose and argument for a novel system for the classification and naming of the LTPs.

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“…sunflower (12-15 kDa)(Berecz et al, 2010), and buckwheat (8-16 kDa)(Radovic, Maksimovic, Brkljacic, Varkonji- Gasic, & Savic, 1999). The polypeptide of 24 kDa was reported in other albumins of seeds as Inca peanut (Plukenetia volubilis L.) and Jatropha curcas(León-Villanueva et al, 2018;Li et al, 2018).The electrophoretic patterns of the globulin fraction showed eight bands(9, 12, 15, 16, 22, 26, 34, and 64 kDa) under non-reducing-denaturing conditions.…”

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confidence: 84%

“…The physicochemical and functional properties of proteins (solubility, water holding, oil binding, gelling, emulsifying, foaming, and rheological behaviors) determine their aptness for use in food systems (Wani, Sogi, Shivhare, & Gill, 2015). Previously, the functional properties of albumins (water-soluble proteins) and globulins (salt-soluble proteins) from seeds such as soybean (Barac, Pesic, Stanojevic, Kostic, & Bivolarevic, 2015), amaranth (Silva-Sánchez, González-Castañeda, De León-Rodríguez, & Barba-de-la-Rosa, 2004), sunflower (Berecz et al, 2010), and kidney bean (Wani et al, 2015) have been studied for use in the food industry.…”

Section: Introductionmentioning

confidence: 99%

Biochemical and functional characterization of albumins and globulins of Brosimum alicastrum seeds

González‐González

Peraza-Campos

Ceballos‐Magaña

et al. 2020

J Food Process Preserv

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Anthropological research indicates that Brosimum alicastrum seed, also known as Ramón tree or mojo was one of the staple foods of pre‐Columbian people. Because of world population growth demand alternative source of food, there is an increasing use of B. alicastrum, especially in American continent. In order to contribute to its rational use, this research presents, biochemical and functional characterization of mojo albumins and globulins. Our results demonstrated that these storage proteins are the most abundant protein fractions. Albumins presented good solubility at pH values of 4–9; the best emulsifying activity index (EAI) was found at pH 7 (322.93 m2/g). Globulins showed a high solubility at pH 2 and at a pH range of 5–9; the maximum EAI values (339.30–309.88 m2/g) were found at pH 4–5. Practical applications Brosimum alicastrum seeds have been used a food source since the pre‐Colombian period, however, there is no information about their proteins (albumins, globulins, prolamins, and glutelins). We have found that mojo seeds can be employed as an alternative source of gluten‐free food and can also be used in the development of novel and/or conventional food products because of biochemical and functional properties of their albumins and globulins, main storage proteins.

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Structural Stability and Surface Activity of Sunflower 2S Albumins and Nonspecific Lipid Transfer Protein

Cited by 31 publications

References 37 publications

Cor a 14, the allergenic 2S albumin from hazelnut, is highly thermostable and resistant to gastrointestinal digestion

Cor a 14, the allergenic 2S albumin from hazelnut, is highly thermostable and resistant to gastrointestinal digestion

Lipid transfer proteins: classification, nomenclature, structure, and function

Biochemical and functional characterization of albumins and globulins of Brosimum alicastrum seeds

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