Identification of gluten-like proteins in selected pod bearing leguminous tree seeds
The protein composition, molecular weight distribution, and rheological properties of honey locust, mesquite, Kentucky coffee tree, and carob seed germs were compared against wheat gluten. Polymeric and Osborne fractionation protocols were used to assess biochemical properties. Dynamic oscillatory s...
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| Veröffentlicht in: | PloS one 2021-04, Vol.16 (4), p.e0249427 |
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| creator | Taghvaei, Mostafa Smith, Brennan Yazar, Gamze Bean, Scott Tilley, Michael Ioerger, Brian |
| description | The protein composition, molecular weight distribution, and rheological properties of honey locust, mesquite, Kentucky coffee tree, and carob seed germs were compared against wheat gluten. Polymeric and Osborne fractionation protocols were used to assess biochemical properties. Dynamic oscillatory shear tests were performed to evaluate protein functionality. All samples had similar ratios of protein fractions as well as high molecular weight disulfide linked proteins except for the Kentucky coffee tree germ proteins, which were found to have lower molecular weight proteins with little disulfide polymerization. Samples were rich in acidic and polar amino acids (glutamic acid and arginine,). Rheological analyses showed that vital wheat gluten had the most stable network, while Kentucky coffee seed proteins had the weakest. High molecular weight disulfide linked glutenous proteins are a common, but not universal feature of pod bearing leguminous trees. |
| doi_str_mv | 10.1371/journal.pone.0249427 |
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Polymeric and Osborne fractionation protocols were used to assess biochemical properties. Dynamic oscillatory shear tests were performed to evaluate protein functionality. All samples had similar ratios of protein fractions as well as high molecular weight disulfide linked proteins except for the Kentucky coffee tree germ proteins, which were found to have lower molecular weight proteins with little disulfide polymerization. Samples were rich in acidic and polar amino acids (glutamic acid and arginine,). Rheological analyses showed that vital wheat gluten had the most stable network, while Kentucky coffee seed proteins had the weakest. High molecular weight disulfide linked glutenous proteins are a common, but not universal feature of pod bearing leguminous trees.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0249427</identifier><identifier>PMID: 33819280</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Agricultural research ; Agriculture ; Animal health ; Beans ; Biology and Life Sciences ; Carob ; Chromatography ; Coffee ; Data analysis ; Dough ; Editing ; Extraction procedures ; Fabaceae - chemistry ; Fabaceae - metabolism ; Flour ; Food ; Fractionation ; Genetic aspects ; Gluten ; Glutens - analysis ; Glutens - chemistry ; Glutens - metabolism ; Grain ; Honey ; Identification and classification ; Legumes ; Legumins - metabolism ; Medical research ; Medicine and Health Sciences ; Mesquite ; Methodology ; Mimosaceae ; Molecular Weight ; Molecular weight distribution ; Nutrient content ; Physical Sciences ; Plant Proteins - metabolism ; Protein composition ; Protein sources ; Proteins ; Research and Analysis Methods ; Research facilities ; Rheological properties ; Rheology ; Seeds ; Seeds - chemistry ; Seeds - metabolism ; Size exclusion chromatography ; Tree seeds ; Trees ; Triticum - chemistry ; Triticum - metabolism ; Viscoelasticity ; Visualization</subject><ispartof>PloS one, 2021-04, Vol.16 (4), p.e0249427</ispartof><rights>COPYRIGHT 2021 Public Library of Science</rights><rights>This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. 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Polymeric and Osborne fractionation protocols were used to assess biochemical properties. Dynamic oscillatory shear tests were performed to evaluate protein functionality. All samples had similar ratios of protein fractions as well as high molecular weight disulfide linked proteins except for the Kentucky coffee tree germ proteins, which were found to have lower molecular weight proteins with little disulfide polymerization. Samples were rich in acidic and polar amino acids (glutamic acid and arginine,). Rheological analyses showed that vital wheat gluten had the most stable network, while Kentucky coffee seed proteins had the weakest. 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Polymeric and Osborne fractionation protocols were used to assess biochemical properties. Dynamic oscillatory shear tests were performed to evaluate protein functionality. All samples had similar ratios of protein fractions as well as high molecular weight disulfide linked proteins except for the Kentucky coffee tree germ proteins, which were found to have lower molecular weight proteins with little disulfide polymerization. Samples were rich in acidic and polar amino acids (glutamic acid and arginine,). Rheological analyses showed that vital wheat gluten had the most stable network, while Kentucky coffee seed proteins had the weakest. 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| subjects | Agricultural research Agriculture Animal health Beans Biology and Life Sciences Carob Chromatography Coffee Data analysis Dough Editing Extraction procedures Fabaceae - chemistry Fabaceae - metabolism Flour Food Fractionation Genetic aspects Gluten Glutens - analysis Glutens - chemistry Glutens - metabolism Grain Honey Identification and classification Legumes Legumins - metabolism Medical research Medicine and Health Sciences Mesquite Methodology Mimosaceae Molecular Weight Molecular weight distribution Nutrient content Physical Sciences Plant Proteins - metabolism Protein composition Protein sources Proteins Research and Analysis Methods Research facilities Rheological properties Rheology Seeds Seeds - chemistry Seeds - metabolism Size exclusion chromatography Tree seeds Trees Triticum - chemistry Triticum - metabolism Viscoelasticity Visualization |
| title | Identification of gluten-like proteins in selected pod bearing leguminous tree seeds |
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