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Harold Corke - One of the best experts on this subject based on the ideXlab platform.
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hplc characterization of betalains from plants in the Amaranthaceae
Journal of Chromatographic Science, 2005Co-Authors: Yi-zhong Cai, Mei Sun, Harold CorkeAbstract:HPLC characterization of reversed-phase (RP) high-performance liquid chromatography (HPLC) has been widely used in separation and identification of plant pigments. An effective RP-HPLC-based method is established to systematically isolate, identify, and quantitate the betalain pigments in the plants of 37 species of eight genera in the Amaranthaceae. A total of 16 betacyanins and three betaxanthins are characterized mainly using the RP-HPLC method and also with the aid of mass spectroscopy. The identified betacyanins include eight amaranthine-types, six gomphrenintypes, and two betanin-types. They are also divided into six simple (nonacylated) betacyanins and 10 acylated betacyanins. Acylated betacyanins are identified as betanidin 5-O-bglucuronosylglucoside or betanidin 6-O-b-glucoside acylated with ferulic, p-coumaric, or 3-hydroxy-3-methylglutaric acids. Three betaxanthins were separated from Celosia species in the Amaranthaceae and identified to be immonium conjugates of betalamic acid with dopamine, 3-methoxytyramine, and (S)tryptophan; the latter two are found to be new betaxanthins from plants.
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hplc characterization of betalains from plants in the Amaranthaceae
Journal of Chromatographic Science, 2005Co-Authors: Yi-zhong Cai, Mei Sun, Harold CorkeAbstract:HPLC characterization of reversed-phase (RP) high-performance liquid chromatography (HPLC) has been widely used in separation and identification of plant pigments. An effective RP-HPLC-based method is established to systematically isolate, identify, and quantitate the betalain pigments in the plants of 37 species of eight genera in the Amaranthaceae. A total of 16 betacyanins and three betaxanthins are characterized mainly using the RP-HPLC method and also with the aid of mass spectroscopy. The identified betacyanins include eight amaranthine-types, six gomphrenin-types, and two betanin-types. They are also divided into six simple (nonacylated) betacyanins and 10 acylated betacyanins. Acylated betacyanins are identified as betanidin 5-O-beta-glucuronosylglucoside or betanidin 6-O-beta-glucoside acylated with ferulic, p-coumaric, or 3-hydroxy-3-methylglutaric acids. Three betaxanthins were separated from Celosia species in the Amaranthaceae and identified to be immonium conjugates of betalamic acid with dopamine, 3-methoxytyramine, and (S)-tryptophan; the latter two are found to be new betaxanthins from plants.
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characterization and application of betalain pigments from plants of the Amaranthaceae
Trends in Food Science and Technology, 2005Co-Authors: Harold CorkeAbstract:The colored vegetative tissues of plants in the family Amaranthaceae contain various betalain pigments and are often produced in high biomass, and therefore, attract interest as potential alternatives to the well-known betalains from beet roots. We attempted a comprehensive systematic study, including selection of betalain-producing genotypes and species, extraction, identification and quantification of betalains, determination and evaluation of physicochemical properties and antioxidant activity; and pigment utilization in certain food systems. The results demonstrated high potential for Amaranthus pigments for use as natural food colorants.
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Antioxidant activity of betalains from plants of the Amaranthaceae.
Journal of Agricultural and Food Chemistry, 2003Co-Authors: Yi-zhong Cai, Mei Sun, Harold CorkeAbstract:Antioxidant activity of betalain pigments (seven pure compounds and four combined fractions) from plants of the family Amaranthaceae was evaluated using the modified DPPH(*) (1,1-diphenyl-2-picrylhydrazyl) method. All tested betalains exhibited strong antioxidant activity. Their EC(50) values ranged from 3.4 to 8.4 microM. Gomphrenin type betacyanins (mean = 3.7 microM) and betaxanthins (mean = 4.2 microM) demonstrated the strongest antioxidant activity, 3-4-fold stronger than ascorbic acid (13.9 microM) and also stronger than rutin (6.1 microM) and catechin (7.2 microM). Antioxidant activity of the tested betalains decreased in the following order: simple gomphrenins > acylated gomphrenins > dopamine-betaxanthin > (S)-tryptophan-betaxanthin > 3-methoxytyramine-betaxanthin > betanin/isobetanin > celosianins > iresinins > amaranthine/isoamaranthine. This study also investigated and discussed the relationship between the chemical structure and the activity of the betalains. The free radical scavenging activity of the betalains usually increased with the numbers of hydroxyl/imino groups and, moreover, depended on the position of hydroxyl groups and glycosylation of aglycones in the betalain molecules.
Donald B Pratt - One of the best experts on this subject based on the ideXlab platform.
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the malagasy endemic dendroportulaca portulacaceae is referable to deeringia Amaranthaceae molecular and morphological evidence
Taxon, 2005Co-Authors: Wendy L. Applequist, Donald B PrattAbstract:Dendroportulaca mirabilis U. Eggli, a Malagasy liana described as an atypical member of Portulacaceae, was shown by ndhF sequence data to be placed within Amaranthaceae tribe Celosieae, strongly supported as sister to Deeringia polysperma. A re-evaluation of the morphology of Dendroportulaca, including field observations, also supported its placement within Celosieae and in particular its relationship to the existing Malagasy species of Deeringia. Dendroportulaca mirabilis is herein transferred to Deeringia.
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the malagasy endemic dendroportulaca portulacaceae is referable to deeringia Amaranthaceae molecular and morphological evidence
Taxon, 2005Co-Authors: Wendy L. Applequist, Donald B PrattAbstract:Dendroportulaca mirabilis U. Eggli, a Malagasy liana described as an atypical member of Portulacaceae, was shown by ndhF sequence data to be placed within Amaranthaceae tribe Celosieae, strongly supported as sister to Deeringia polysperma. A re-evaluation of the morphology of Dendroportulaca, including field observations, also supported its placement within Celosieae and in particular its relationship to the existing Malagasy species of Deeringia. Dendroportulaca mirabilis is herein transferred to Deeringia.
Mayte Villalba - One of the best experts on this subject based on the ideXlab platform.
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a relevant ige reactive 28 kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47 kda polygalaturonase
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28 kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2 Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28 kDa band together with an allergenic band of about 47 kDa in the pollen extract. Therefore, the 28 kDa was assigned as a natural degradation product of the 47 kDa integral polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47 kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m3 of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
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a relevant ige reactive 28kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47kda polygalaturonase proteins and proteomics
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28kDa band together with an allergenic band of about 47kDa in the pollen extract. Therefore, the 28kDa was assigned as a natural degradation product of the 47kDa integral polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m³ of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
Wendy L. Applequist - One of the best experts on this subject based on the ideXlab platform.
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the malagasy endemic dendroportulaca portulacaceae is referable to deeringia Amaranthaceae molecular and morphological evidence
Taxon, 2005Co-Authors: Wendy L. Applequist, Donald B PrattAbstract:Dendroportulaca mirabilis U. Eggli, a Malagasy liana described as an atypical member of Portulacaceae, was shown by ndhF sequence data to be placed within Amaranthaceae tribe Celosieae, strongly supported as sister to Deeringia polysperma. A re-evaluation of the morphology of Dendroportulaca, including field observations, also supported its placement within Celosieae and in particular its relationship to the existing Malagasy species of Deeringia. Dendroportulaca mirabilis is herein transferred to Deeringia.
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the malagasy endemic dendroportulaca portulacaceae is referable to deeringia Amaranthaceae molecular and morphological evidence
Taxon, 2005Co-Authors: Wendy L. Applequist, Donald B PrattAbstract:Dendroportulaca mirabilis U. Eggli, a Malagasy liana described as an atypical member of Portulacaceae, was shown by ndhF sequence data to be placed within Amaranthaceae tribe Celosieae, strongly supported as sister to Deeringia polysperma. A re-evaluation of the morphology of Dendroportulaca, including field observations, also supported its placement within Celosieae and in particular its relationship to the existing Malagasy species of Deeringia. Dendroportulaca mirabilis is herein transferred to Deeringia.
Carmen Oeosantos - One of the best experts on this subject based on the ideXlab platform.
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a relevant ige reactive 28 kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47 kda polygalaturonase
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28 kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2 Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28 kDa band together with an allergenic band of about 47 kDa in the pollen extract. Therefore, the 28 kDa was assigned as a natural degradation product of the 47 kDa integral polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47 kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m3 of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
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a relevant ige reactive 28kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47kda polygalaturonase proteins and proteomics
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28kDa band together with an allergenic band of about 47kDa in the pollen extract. Therefore, the 28kDa was assigned as a natural degradation product of the 47kDa integral polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m³ of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.