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An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5.

Rosengren, Anna LU ; Krishnaswamyreddy, Sumitha LU ; Morrill, Johan LU ; Aurelius, Oskar LU ; Logan, Derek LU ; Kolenová, Katarina LU and Stålbrand, Henrik LU (2014) In Applied Microbiology and Biotechnology 98(24). p.10091-10104
Abstract
β-Mannanases are involved in the conversion and modification of mannan-based saccharides. Using a retaining mechanism, they can, in addition to hydrolysis, also potentially perform transglycosylation reactions, synthesizing new glyco-conjugates. Transglycosylation has been reported for β-mannanases in GH5 and GH113. However, although they share the same fold and catalytic mechanism, there may be differences in the enzymes' ability to perform transglycosylation. Three GH5 β-mannanases from Aspergillus nidulans, AnMan5A, AnMan5B and AnMan5C, which belong to subfamily GH5_7 were studied. Comparative studies, including the GH5_7 TrMan5A from Trichoderma reesei, showed some differences between the enzymes. All the enzymes could perform... (More)
β-Mannanases are involved in the conversion and modification of mannan-based saccharides. Using a retaining mechanism, they can, in addition to hydrolysis, also potentially perform transglycosylation reactions, synthesizing new glyco-conjugates. Transglycosylation has been reported for β-mannanases in GH5 and GH113. However, although they share the same fold and catalytic mechanism, there may be differences in the enzymes' ability to perform transglycosylation. Three GH5 β-mannanases from Aspergillus nidulans, AnMan5A, AnMan5B and AnMan5C, which belong to subfamily GH5_7 were studied. Comparative studies, including the GH5_7 TrMan5A from Trichoderma reesei, showed some differences between the enzymes. All the enzymes could perform transglycosylation but AnMan5B stood out in generating comparably higher amounts of transglycosylation products when incubated with manno-oligosaccharides. In addition, AnMan5B did not use alcohols as acceptor, which was also different compared to the other three β-mannanases. In order to map the preferred binding of manno-oligosaccharides, incubations were performed in H2 (18)O. AnMan5B in contrary to the other enzymes did not generate any (18)O-labelled products. This further supported the idea that AnMan5B potentially prefers to use saccharides as acceptor instead of water. A homology model of AnMan5B showed a non-conserved Trp located in subsite +2, not present in the other studied enzymes. Strong aglycone binding seems to be important for transglycosylation with saccharides. Depending on the application, it is important to select the right enzyme. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Applied Microbiology and Biotechnology
volume
98
issue
24
pages
10091 - 10104
publisher
Springer
external identifiers
  • pmid:24950755
  • wos:000345331700015
  • scopus:84916930435
ISSN
1432-0614
DOI
10.1007/s00253-014-5871-8
language
English
LU publication?
yes
id
d83c3e27-37e7-40f6-84a4-7cddfbc748c8 (old id 4527418)
date added to LUP
2014-08-08 14:55:10
date last changed
2017-09-27 21:57:04
@article{d83c3e27-37e7-40f6-84a4-7cddfbc748c8,
  abstract     = {β-Mannanases are involved in the conversion and modification of mannan-based saccharides. Using a retaining mechanism, they can, in addition to hydrolysis, also potentially perform transglycosylation reactions, synthesizing new glyco-conjugates. Transglycosylation has been reported for β-mannanases in GH5 and GH113. However, although they share the same fold and catalytic mechanism, there may be differences in the enzymes' ability to perform transglycosylation. Three GH5 β-mannanases from Aspergillus nidulans, AnMan5A, AnMan5B and AnMan5C, which belong to subfamily GH5_7 were studied. Comparative studies, including the GH5_7 TrMan5A from Trichoderma reesei, showed some differences between the enzymes. All the enzymes could perform transglycosylation but AnMan5B stood out in generating comparably higher amounts of transglycosylation products when incubated with manno-oligosaccharides. In addition, AnMan5B did not use alcohols as acceptor, which was also different compared to the other three β-mannanases. In order to map the preferred binding of manno-oligosaccharides, incubations were performed in H2 (18)O. AnMan5B in contrary to the other enzymes did not generate any (18)O-labelled products. This further supported the idea that AnMan5B potentially prefers to use saccharides as acceptor instead of water. A homology model of AnMan5B showed a non-conserved Trp located in subsite +2, not present in the other studied enzymes. Strong aglycone binding seems to be important for transglycosylation with saccharides. Depending on the application, it is important to select the right enzyme.},
  author       = {Rosengren, Anna and Krishnaswamyreddy, Sumitha and Morrill, Johan and Aurelius, Oskar and Logan, Derek and Kolenová, Katarina and Stålbrand, Henrik},
  issn         = {1432-0614},
  language     = {eng},
  number       = {24},
  pages        = {10091--10104},
  publisher    = {Springer},
  series       = {Applied Microbiology and Biotechnology},
  title        = {An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5.},
  url          = {http://dx.doi.org/10.1007/s00253-014-5871-8},
  volume       = {98},
  year         = {2014},
}