Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/105833
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Type: Journal article
Title: Variation in barley (1 → 3, 1 →4)-β-glucan endohydrolases reveals novel allozymes with increased thermostability
Other Titles: Variation in barley (1-> 3, 1->4)-beta-glucan endohydrolases reveals novel allozymes with increased thermostability
Author: Lauer, J.
Cu, S.
Burton, R.
Eglinton, J.
Citation: Theoretical and Applied Genetics, 2017; 130(5):1053-1063
Publisher: Springer
Issue Date: 2017
ISSN: 0040-5752
1432-2242
Statement of
Responsibility: 
Juanita C. Lauer, Suong Cu, Rachel A. Burton, Jason K. Eglinton
Abstract: Novel barley (1 → 3, 1 → 4)-β-glucan endohydrolases with increased thermostability. Rapid and reliable degradation of (1 → 3, 1 → 4)-β-glucan to produce low viscosity wort is an essential requirement for malting barley. The (1 → 3, 1 → 4)-β-glucan endohyrolases are responsible for the primary hydrolysis of cell wall β-glucan. The variation in β-glucanase genes HvGlb1 and HvGlb2 that encode EI and EII, respectively, were examined in elite and exotic germplasm. Six EI and 14 EII allozymes were identified, and significant variation was found in β-glucanase from Hordeum vulgare ssp. spontaneum (wild barley), the progenitor of modern cultivated barley. Allozymes were examined using prediction methods; the change in Gibbs free energy of the identified amino acid substitutions to predict changes in enzyme stability and homology modelling to examine the structure of the novel allozymes using the existing solved EII structure. Two EI and four EII allozymes in wild barley accessions were predicted to have improved barley β-glucanase thermostability. One novel EII candidate was identified in existing backcross lines with contrasting HvGlb2 alleles from wild barley and cv Flagship. The contrasting alleles in selected near isogenic lines were examined in β-glucanase thermostability analyses. The EII from wild barley exhibited a significant increase in β-glucanase thermostability conferred by the novel HvGlb2 allele. Increased β-glucanase thermostability is heritable and candidates identified in wild barley could improve malting and brewing quality in new varieties.
Keywords: Barley; glycoside hydrolases
Rights: © Springer-Verlag Berlin Heidelberg 2017
RMID: 0030065412
DOI: 10.1007/s00122-017-2870-z
Grant ID: http://purl.org/au-research/grants/arc/CE110001007
Appears in Collections:Agriculture, Food and Wine publications

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