Expression and functional analysis of Mr 58000 peptides derived from the repetitive domain of high molecular weight glutenin subunit 1Dx5

F. Buonocore; L. Bertini; C. Ronchi; F. Békés; C. Caporale; D. Lafiandra; P. Gras; A. S. Tatham; J. A. Greenfield; N. G. Halford; P. R. Shewry

doi:10.1006/jcrs.1998.0177

Expression and functional analysis of M_r 58000 peptides derived from the repetitive domain of high molecular weight glutenin subunit 1Dx5

F. Buonocore, L. Bertini, C. Ronchi, F. Békés, C. Caporale, D. Lafiandra, P. Gras, A. S. Tatham, J. A. Greenfield, N. G. Halford, P. R. Shewry^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

29 Citations (Scopus)

Abstract

A highly repetitive M_r 58000 peptide based on residues 102 to 643 of subunit 1Dx5 and forms containing one to four cysteine residues were expressed in E. coli and purified to homogeneity. Incorporation into dough using a 2 g 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 strength, indicating that the repetitive domains of the HMW subunits are sufficient to contribute to dough strength when incorporated into glutenin polymers.

Original language	English
Pages (from-to)	209-215
Number of pages	7
Journal	Journal of Cereal Science
Volume	27
Issue number	3
DOIs	https://doi.org/10.1006/jcrs.1998.0177
Publication status	Published - May 1998
Externally published	Yes

Keywords

Glutenin
Mixograph
Protein engineering
Wheat

Access to Document

10.1006/jcrs.1998.0177

Cite this

Buonocore, F., Bertini, L., Ronchi, C., Békés, F., Caporale, C., Lafiandra, D., Gras, P., Tatham, A. S., Greenfield, J. A., Halford, N. G., & Shewry, P. R. (1998). Expression and functional analysis of M_r 58000 peptides derived from the repetitive domain of high molecular weight glutenin subunit 1Dx5. Journal of Cereal Science, 27(3), 209-215. https://doi.org/10.1006/jcrs.1998.0177

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abstract = "A highly repetitive Mr 58000 peptide based on residues 102 to 643 of subunit 1Dx5 and forms containing one to four cysteine residues were expressed in E. coli and purified to homogeneity. Incorporation into dough using a 2 g 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 strength, indicating that the repetitive domains of the HMW subunits are sufficient to contribute to dough strength when incorporated into glutenin polymers.",

keywords = "Glutenin, Mixograph, Protein engineering, Wheat",

author = "F. Buonocore and L. Bertini and C. Ronchi and F. B{\'e}k{\'e}s and C. Caporale and D. Lafiandra and P. Gras and Tatham, {A. S.} and Greenfield, {J. A.} and Halford, {N. G.} and Shewry, {P. R.}",

year = "1998",

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Buonocore, F, Bertini, L, Ronchi, C, Békés, F, Caporale, C, Lafiandra, D, Gras, P, Tatham, AS, Greenfield, JA, Halford, NG & Shewry, PR 1998, 'Expression and functional analysis of M_r 58000 peptides derived from the repetitive domain of high molecular weight glutenin subunit 1Dx5', Journal of Cereal Science, vol. 27, no. 3, pp. 209-215. https://doi.org/10.1006/jcrs.1998.0177

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T1 - Expression and functional analysis of Mr 58000 peptides derived from the repetitive domain of high molecular weight glutenin subunit 1Dx5

AU - Buonocore, F.

AU - Bertini, L.

AU - Ronchi, C.

AU - Békés, F.

AU - Caporale, C.

AU - Lafiandra, D.

AU - Gras, P.

AU - Tatham, A. S.

AU - Greenfield, J. A.

AU - Halford, N. G.

AU - Shewry, P. R.

PY - 1998/5

Y1 - 1998/5

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AB - A highly repetitive Mr 58000 peptide based on residues 102 to 643 of subunit 1Dx5 and forms containing one to four cysteine residues were expressed in E. coli and purified to homogeneity. Incorporation into dough using a 2 g 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 strength, indicating that the repetitive domains of the HMW subunits are sufficient to contribute to dough strength when incorporated into glutenin polymers.

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KW - Protein engineering

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