Heterologous Expression and Dough Mixing Studies of Wild-Type and Mutant C Hordeins

Wild type and mutant (cysteine-containing) forms of C hordein were expressed inEscherichia coli. Incorporation of a mutant form with N- and C-terminal cysteine residues into dough using a 2 g Mixograph showed similar positive effects on dough strength to the incorporation of HMW subunit 1Bx7. Co-inc...

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Bibliographic Details
Published in:Journal of cereal science 1998-01, Vol.27 (1), p.15-22
Main Authors: Tamás, L., Békés, F., Greenfield, J., Tatham, A.S., Gras, P.W., Shewry, P.R., Appels, R.
Format: Article
Language:English
Subjects:
amino acid sequences
Biological and medical sciences
Cereal and baking product industries
chemical structure
cysteine
dough
Escherichia coli
Food industries
Fundamental and applied biological sciences. Psychology
gene expression
genetically modified organisms
hordein
molecular sequence data
mutants
nucleotide sequences
recombinant proteins
rheological properties
strength
wheat flour
wheat gluten
wheat, Mixograph, C hordeins, HMW subunit, rheology, disulphide bonds
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Summary:Wild type and mutant (cysteine-containing) forms of C hordein were expressed inEscherichia coli. Incorporation of a mutant form with N- and C-terminal cysteine residues into dough using a 2 g Mixograph showed similar positive effects on dough strength to the incorporation of HMW subunit 1Bx7. Co-incorporation showed that the effects of the two proteins were additive. In contrast, the incorporation of wild type C hordein or mutants with single cysteines at the N- or C-terminus resulted in decreased dough strength, with the two mutant forms inhibiting the positive effect of 1Bx7. Analysis of total protein extracts from the doughs indicate that the differences resulted from alterations in the proportions of gluten monomers, small gluten polymers and large gluten polymers.
ISSN:0733-5210
1095-9963
DOI:10.1006/jcrs.1997.0147