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Isolation and partial characterisation of two low molecular weight durum wheat ( Triticum durum ) glutenins
Author(s) -
Kobrehel Kàroly,
Alary Rémi
Publication year - 1989
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740480406
Subject(s) - glutenin , cultivar , amino acid , chemistry , food science , biology , botany , biochemistry , gene , protein subunit
Two low molecular weight durum wheat ( Triticum durum Desf) glutenins, DSG‐1 and DSG‐2 (durum‐wheat sulphur‐rich glutenin fractions) were isolated from two cultivars, Mondur of good technological quality and Kidur of poor technological quality. The glutenin fraction, composed mostly of DSG protein, was extracted using a low concentration of NA‐tetradecanoate and then fractionted by by using molecular sieve chromatography (Bio‐Gel P 30). The amino acid compositions and the N‐terminal sequences of the pure DSG proteins were determined, and their hydrophobic characteristics, calculated on the basis of these data, showed that DSG‐2 is more hydrophobic than DSG‐1. The amino acid compositions of DSG‐1 and DSG‐2 were different. The N‐terminal amino acids of DSG‐1 and DSG‐2 were also different but were identical for each of the two cultivars. In the case of DSG‐1, in addition to the main chain a minor chain was found in which the first three amino acids of the main chain were missing. The minor chain represented about 30% int he DSG‐1 of mondur and almost 50% in Kidur.