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Characterization of 1Sty13, a novel high-molecular-weight glutenin subunit from Elymus sibiricus L.

Published online by Cambridge University Press:  25 May 2021

Mei Yan
Affiliation:
School of Life Sciences, Guizhou Normal University, Guiyang, Guizhou Province, China Shandong Luyan Agricultural Co., LTC, Jinan, Shandong Province, China
Muzi Li
Affiliation:
School of Life Sciences, Guizhou Normal University, Guiyang, Guizhou Province, China
Zaidong Yang
Affiliation:
Shandong Luyan Agricultural Co., LTC, Jinan, Shandong Province, China
Feng Yu*
Affiliation:
School of Life Sciences, Guizhou Normal University, Guiyang, Guizhou Province, China
Xuye Du*
Affiliation:
School of Life Sciences, Guizhou Normal University, Guiyang, Guizhou Province, China
*
*Corresponding authors. E-mail: [email protected], [email protected]
*Corresponding authors. E-mail: [email protected], [email protected]

Abstract

High-molecular-weight glutenin subunit (HMW-GS) is a key factor affecting dough-processing quality. 1Sty13 is a novel HMW-GS found in the tetraploid species, Elymus sibiricus L. 1Sty13 has faster electrophoretic mobility than the 1Dy12 subunit on sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis. The gene encoding the 1Sty13 subunit was composed of 1803 nucleotide base pairs with an open reading frame that was 599 amino acids in length. Analysis of the predicted amino acid sequence of 1Sty13 indicated that the N-terminal domain was similar to the y-type subunit, whereas the C-terminal domains were similar to the x-type subunit. Five cysteine residues were found in 1Sty13, which is one less than the published HMW-GS in the St genome. The 1Sty13 protein was purified at a scale sufficient for incorporation into flour for the SDS sedimentation test, which indicated that incorporating 1Sty13 improved dough quality.

Type
Short Communication
Copyright
Copyright © The Author(s), 2021. Published by Cambridge University Press on behalf of NIAB

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Footnotes

Mei Yan and Muzi Li contributed equally to this study.

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