Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/105558
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dc.contributor.authorLauer, J.-
dc.contributor.authorYap, K.-
dc.contributor.authorCu, S.-
dc.contributor.authorBurton, R.-
dc.contributor.authorEglinton, J.-
dc.date.issued2017-
dc.identifier.citationJournal of Agricultural and Food Chemistry, 2017; 65(2):421-428-
dc.identifier.issn0021-8561-
dc.identifier.issn1520-5118-
dc.identifier.urihttp://hdl.handle.net/2440/105558-
dc.description.abstractBarley (1→3,1→4)-β-glucan endohydrolases (β-glucanases; EI and EII) are primarily responsible for hydrolyzing high molecular weight (1→3,1→4)-β-glucans (β-glucan) during germination. Incomplete endosperm modification during malting results in residual β-glucan that can contribute to increased wort viscosity and beer chill haze. Four newly identified forms of EI and EII and the reference enzymes EI-a and EII-a were expressed in Escherichia coli, and the recombinant proteins were characterized for enzyme kinetics and thermostability. EI and EII variants that exhibited higher residual β-glucanase activity than EI-a and EII-a after heat treatment also exhibited increased substrate affinity and decreased turnover rates. The novel EII-l form exhibited significantly increased thermostability compared with the reference EII-a when activity was measured at elevated temperature. EII-l exhibited a T50 value, which indicates the temperature at which 50% of β-glucanase activity remains, 1.3 °C higher than that of EII-a. The irreversible thermal inactivation difference between EII-a and EII-l after 5 min of heat treatment at 56 °C was 11.9%. The functional significance of the three amino acid differences between EII-a and EII-l was examined by making combinatorial mutations in EII-a using site-directed mutagenesis. The S20G and D284E amino acid substitutions were shown to be responsible for the increase in EII-1 thermostability.-
dc.description.statementofresponsibilityJuanita C. Lauer, Kuok Yap, Suong Cu, Rachel A. Burton, Jason K. Eglinton-
dc.language.isoen-
dc.publisherAmerican Chemical Society-
dc.rights© 2016 American Chemical Society-
dc.subjectβ-glucanase; thermostability; catalytic efficiency; wild barley-
dc.titleNovel barley (1→3,1→4)-β-glucan endohydrolase alleles confer increased enzyme thermostability-
dc.title.alternativeNovel barley (1->3,1->4)-beta-glucan endohydrolase alleles confer increased enzyme thermostability.-
dc.typeJournal article-
dc.identifier.doi10.1021/acs.jafc.6b04287-
dc.relation.granthttp://purl.org/au-research/grants/arc/CE1101007-
pubs.publication-statusPublished-
dc.identifier.orcidBurton, R. [0000-0002-0638-4709]-
Appears in Collections:Agriculture, Food and Wine publications
Aurora harvest 8

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