2000•Journal of Nutritional Science and VitaminologyOpen access

Efficient Extraction and Some Properties of Storage Proteins (Prolamin and Glutelin) in Ancient Rice Cultivars.

Junko Udaka, Tetsuro Koga, Hideaki Tsuji, Masumi Kimoto, Kenji Takumi

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Abstract

Two typical storage proteins (prolamin and glutelin) in a total of 14 samples of ancient rice cultivars were examined for their accumulation in the endosperms during days after flowering (DAF), extraction efficiency with various solvents, and variations in polypeptide components or amino acid compositions. There was little difference in accumulation profiles between this and previous observations, in which glutelin appeared on 5-7 DAF and prolamin on 7-9 DAF. As for the extraction of prolamin and glutelin, it was most effectively attained by sequential usage of 55% propanol and 21% SDS. As a result of SDS-PAGE, prolamin and glutelin proved to be composed mainly of a single polypeptide with a molecular weight (MW) of 15 kDa and two subunits with MWs of 21 kDa (alpha) and 32 kDa (beta), respectively. A comparison between the ancient and modern rice cultivars revealed the same physicochemical properties in either case of prolamin or glutelin. Additionally, a good relationship was observed on the total protein and glutelin (but not prolamin) contents in the ancient rice cultivar.

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Two typical storage proteins (prolamin and glutelin) in a total of 14 samples of ancient rice cultivars were examined for their accumulation in the endosperms during days after flowering (DAF), extraction efficiency with various solvents, and variations in polypeptide components or amino acid compositions. There was little difference in accumulation profiles between this and previous observations, in which glutelin appeared on 5-7 DAF and prolamin on 7-9 DAF. As for the extraction of prolamin and glutelin, it was most effectively attained by sequential usage of 55% propanol and 21% SDS. As a result of SDS-PAGE, prolamin and glutelin proved to be composed mainly of a single polypeptide with a molecular weight (MW) of 15 kDa and two subunits with MWs of 21 kDa (alpha) and 32 kDa (beta), respectively. A comparison between the ancient and modern rice cultivars revealed the same physicochemical properties in either case of prolamin or glutelin. Additionally, a good relationship was observed on the total protein and glutelin (but not prolamin) contents in the ancient rice cultivar.

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Available abstract

Two typical storage proteins (prolamin and glutelin) in a total of 14 samples of ancient rice cultivars were examined for their accumulation in the endosperms during days after flowering (DAF), extraction efficiency with various solvents, and variations in polypeptide components or amino acid compositions. There was little difference in accumulation profiles between this and previous observations, in which glutelin appeared on 5-7 DAF and prolamin on 7-9 DAF. As for the extraction of prolamin and glutelin, it was most effectively attained by sequential usage of 55% propanol and 21% SDS. As a result of SDS-PAGE, prolamin and glutelin proved to be composed mainly of a single polypeptide with a molecular weight (MW) of 15 kDa and two subunits with MWs of 21 kDa (alpha) and 32 kDa (beta), respectively. A comparison between the ancient and modern rice cultivars revealed the same physicochemical properties in either case of prolamin or glutelin. Additionally, a good relationship was observed on the total protein and glutelin (but not prolamin) contents in the ancient rice cultivar.

Key concepts: Glutelin, Prolamin, Storage protein, Cultivar, Extraction (chemistry), Food science, Chemistry, Globulin

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Efficient Extraction and Some Properties of Storage Proteins (Prolamin and Glutelin) in Ancient Rice Cultivars. — Research Paper | ScholarLens