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Monomeric and dimeric cyclomaltodextrinases reveal different modes of substrate degradation

Turner, Pernilla LU ; Nilsson, Carina LU ; Svensson, David LU ; Holst, Olle LU ; Gorton, Lo LU and Nordberg Karlsson, Eva LU (2005) In Biologia 60(Suppl. 16). p.79-87
Abstract
Two cyclomaltodextrinases (CDase) of thermophilic origin were investigated for their action on cyclodextrins.

Although most CDases known today are made up of at least homodimers, one of the enzymes studied was shown to be a

monomer in solution, while the other one was a dimer. Interestingly, the dimeric enzyme had a much superior selectivity for a cyclodextrin substrate compared to its monomeric homologue, with a specific activity on α-cyclodextrin around 100 times higher than for the polymeric substrates starch and pullulan. Moreover, the monomeric CDase had a 10 times higher activity on those polymers than the dimer. The degradation pattern on cyclodextrins was examined by high-performance

anion-exchange... (More)
Two cyclomaltodextrinases (CDase) of thermophilic origin were investigated for their action on cyclodextrins.

Although most CDases known today are made up of at least homodimers, one of the enzymes studied was shown to be a

monomer in solution, while the other one was a dimer. Interestingly, the dimeric enzyme had a much superior selectivity for a cyclodextrin substrate compared to its monomeric homologue, with a specific activity on α-cyclodextrin around 100 times higher than for the polymeric substrates starch and pullulan. Moreover, the monomeric CDase had a 10 times higher activity on those polymers than the dimer. The degradation pattern on cyclodextrins was examined by high-performance

anion-exchange chromatography in combination with microdialysis. The final products were almost exclusively maltose and glucose in an approximate molar ratio of 2:1. However, the intermediate product ratios were quite different for the two enzymes, revealing that the monomeric CDase had a more random distribution of transitional products. Moreover, the dimeric CDase accumulated maltotriose, which is believed to be due to transglycosylation. The oligomeric state of the

enzymes is thought to be a key factor for exhibiting high cyclodextrinase as well as transglycosylation activity. (Less)
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in
Biologia
volume
60
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Suppl. 16
pages
79 - 87
publisher
Springer
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  • wos:000234899500011
  • scopus:31844442081
ISSN
0006-3088
language
English
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The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Biotechnology (LTH) (011001037), Analytical Chemistry (S/LTH) (011001004)
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7f12a505-4d7e-44e2-a5d7-d1b00eba342d (old id 159422)
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http://biologia.savba.sk/Suppl_16/Turner_P.pdf
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@article{7f12a505-4d7e-44e2-a5d7-d1b00eba342d,
  abstract     = {Two cyclomaltodextrinases (CDase) of thermophilic origin were investigated for their action on cyclodextrins.<br/><br>
Although most CDases known today are made up of at least homodimers, one of the enzymes studied was shown to be a<br/><br>
monomer in solution, while the other one was a dimer. Interestingly, the dimeric enzyme had a much superior selectivity for a cyclodextrin substrate compared to its monomeric homologue, with a specific activity on α-cyclodextrin around 100 times higher than for the polymeric substrates starch and pullulan. Moreover, the monomeric CDase had a 10 times higher activity on those polymers than the dimer. The degradation pattern on cyclodextrins was examined by high-performance<br/><br>
anion-exchange chromatography in combination with microdialysis. The final products were almost exclusively maltose and glucose in an approximate molar ratio of 2:1. However, the intermediate product ratios were quite different for the two enzymes, revealing that the monomeric CDase had a more random distribution of transitional products. Moreover, the dimeric CDase accumulated maltotriose, which is believed to be due to transglycosylation. The oligomeric state of the<br/><br>
enzymes is thought to be a key factor for exhibiting high cyclodextrinase as well as transglycosylation activity.},
  author       = {Turner, Pernilla and Nilsson, Carina and Svensson, David and Holst, Olle and Gorton, Lo and Nordberg Karlsson, Eva},
  issn         = {0006-3088},
  language     = {eng},
  number       = {Suppl. 16},
  pages        = {79--87},
  publisher    = {Springer},
  series       = {Biologia},
  title        = {Monomeric and dimeric cyclomaltodextrinases reveal different modes of substrate degradation},
  url          = {http://biologia.savba.sk/Suppl_16/Turner_P.pdf},
  volume       = {60},
  year         = {2005},
}