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https://hdl.handle.net/2440/105558
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dc.contributor.author | Lauer, J. | - |
dc.contributor.author | Yap, K. | - |
dc.contributor.author | Cu, S. | - |
dc.contributor.author | Burton, R. | - |
dc.contributor.author | Eglinton, J. | - |
dc.date.issued | 2017 | - |
dc.identifier.citation | Journal of Agricultural and Food Chemistry, 2017; 65(2):421-428 | - |
dc.identifier.issn | 0021-8561 | - |
dc.identifier.issn | 1520-5118 | - |
dc.identifier.uri | http://hdl.handle.net/2440/105558 | - |
dc.description.abstract | Barley (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.statementofresponsibility | Juanita C. Lauer, Kuok Yap, Suong Cu, Rachel A. Burton, Jason K. Eglinton | - |
dc.language.iso | en | - |
dc.publisher | American Chemical Society | - |
dc.rights | © 2016 American Chemical Society | - |
dc.source.uri | http://dx.doi.org/10.1021/acs.jafc.6b04287 | - |
dc.subject | β-glucanase; thermostability; catalytic efficiency; wild barley | - |
dc.title | Novel barley (1→3,1→4)-β-glucan endohydrolase alleles confer increased enzyme thermostability | - |
dc.title.alternative | Novel barley (1->3,1->4)-beta-glucan endohydrolase alleles confer increased enzyme thermostability. | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1021/acs.jafc.6b04287 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/CE1101007 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Cu, S. [0000-0002-9233-6673] | - |
dc.identifier.orcid | Burton, R. [0000-0002-0638-4709] | - |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest 8 |
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