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A β-mannan utilisation locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans

Krishnaswamyreddy, Sumitha LU ; Bågenholm, Viktoria LU ; Pudlo, Nicholas A ; Bouraoui, Hanene ; Koropatkin, Nicole M ; Martens, Eric C and Stålbrand, Henrik LU (2016) In FEBS Letters 590(14). p.2106-2118
Abstract

The Bacova_02091 gene in the β-mannan utilisation locus of Bacteroides ovatus encodes a family GH36 α-galactosidase (BoGal36A), transcriptionally upregulated during growth on galactomannan. Characterisation of recombinant BoGal36A reveals unique properties compared to other GH36 α-galactosidases, which preferentially hydrolyse terminal α-galactose in raffinose family oligosaccharides. BoGal36A prefers hydrolysing internal galactose substitutions from intact and depolymerized galactomannan. BoGal36A efficiently releases (>90%) galactose from guar and locust bean galactomannans, resulting in precipitation of the polysaccharides. As compared to other GH36 structures, the BoGal36A 3D model displays a loop deletion, resulting in a wider... (More)

The Bacova_02091 gene in the β-mannan utilisation locus of Bacteroides ovatus encodes a family GH36 α-galactosidase (BoGal36A), transcriptionally upregulated during growth on galactomannan. Characterisation of recombinant BoGal36A reveals unique properties compared to other GH36 α-galactosidases, which preferentially hydrolyse terminal α-galactose in raffinose family oligosaccharides. BoGal36A prefers hydrolysing internal galactose substitutions from intact and depolymerized galactomannan. BoGal36A efficiently releases (>90%) galactose from guar and locust bean galactomannans, resulting in precipitation of the polysaccharides. As compared to other GH36 structures, the BoGal36A 3D model displays a loop deletion, resulting in a wider active site cleft which likely can accommodate a galactose-substituted polymannose backbone. This article is protected by copyright. All rights reserved.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FEBS Letters
volume
590
issue
14
pages
13 pages
publisher
Wiley-Blackwell
external identifiers
  • pmid:27288925
  • scopus:84979600169
  • wos:000380761100007
ISSN
1873-3468
DOI
10.1002/1873-3468.12250
language
English
LU publication?
yes
id
d21192c5-3456-4dcb-9fbd-36a34ee875bc
date added to LUP
2016-06-16 15:06:55
date last changed
2024-10-04 21:30:16
@article{d21192c5-3456-4dcb-9fbd-36a34ee875bc,
  abstract     = {{<p>The Bacova_02091 gene in the β-mannan utilisation locus of Bacteroides ovatus encodes a family GH36 α-galactosidase (BoGal36A), transcriptionally upregulated during growth on galactomannan. Characterisation of recombinant BoGal36A reveals unique properties compared to other GH36 α-galactosidases, which preferentially hydrolyse terminal α-galactose in raffinose family oligosaccharides. BoGal36A prefers hydrolysing internal galactose substitutions from intact and depolymerized galactomannan. BoGal36A efficiently releases (&gt;90%) galactose from guar and locust bean galactomannans, resulting in precipitation of the polysaccharides. As compared to other GH36 structures, the BoGal36A 3D model displays a loop deletion, resulting in a wider active site cleft which likely can accommodate a galactose-substituted polymannose backbone. This article is protected by copyright. All rights reserved.</p>}},
  author       = {{Krishnaswamyreddy, Sumitha and Bågenholm, Viktoria and Pudlo, Nicholas A and Bouraoui, Hanene and Koropatkin, Nicole M and Martens, Eric C and Stålbrand, Henrik}},
  issn         = {{1873-3468}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{14}},
  pages        = {{2106--2118}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{FEBS Letters}},
  title        = {{A β-mannan utilisation locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans}},
  url          = {{http://dx.doi.org/10.1002/1873-3468.12250}},
  doi          = {{10.1002/1873-3468.12250}},
  volume       = {{590}},
  year         = {{2016}},
}