EXPRESSION AND FUNCTIONAL-ANALYSIS OF M-R 58000 PEPTIDES DERIVED FROMTHE REPETITIVE DOMAIN OF HIGH-MOLECULAR-WEIGHT GLUTENIN SUBUNIT-1DX5

A highly repetitive M-r 58000 peptide based on residues 102 to 643 of subunit IDx5 and forms containing one to four cysteine residues were e xpressed in E. coli and purified to homogeneity. Incorporation into do ugh using a 2g Mixograph showed that most peptides resulted in reduced strength, which was possibly due to dilution or chain termination of glutenin polymers. However, a form containing four cysteines (two each close to the N-terminus and C-terminus) resulted in increased strengt h, indicating that the repetitive domains of the HMW subunits are suff icient to contribute to dough strength when incorporated into glutenin polymers. (C) 1998 Academic Press Limited