Sequential processing of mannose-containing glycans by two α-mannosidases from Solitalea canadensis

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• 作者：Fang F. Liu ; Anna Kulinich ; Ya M. Du ; Li Liu ; Josef Voglmeir
• 关键词：Bacterial glycosidases ; Mannosidase ; Mannose ; containing oligosaccharide ; N ; glycans ; Oligomannose ; Solitalea canadensis
• 刊名：Glycoconjugate Journal
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：33
• 期：2
• 页码：159-168
• 全文大小：598 KB
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• 作者单位：Fang F. Liu (1)
  Anna Kulinich (1)
  Ya M. Du (1)
  Li Liu (1) (2)
  Josef Voglmeir (1)
  
  1. Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, People’s Republic of China
  2. Qlyco Ltd., Nanjing, People’s Republic of China
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Pathology
  
• 出版者：Springer Netherlands
• ISSN：1573-4986

文摘

Two putative α-mannosidase genes isolated from the rather unexplored soil bacterium Solitalea canadensis were cloned and biochemically characterised. Both recombinant enzymes were highly selective in releasing α-linked mannose but no other sugars. The α-mannosidases were designated Sca2/3Man2693 and Sca6Man4191, and showed the following biochemical properties: the temperature optimum for both enzymes was 37 °C, and their pH optima lay at 5.0 and 5.5, respectively. The activity of Sca2/3Man2693 was found to be dependent on Ca2+ ions, whereas Cu2+ and Zn2+ ions almost completely inhibited both α-mannosidases. Specificity screens with various substrates revealed that Sca2/3Man2693 could release both α1-2- and α1-3-linked mannose, whereas Sca6Man4191 only released α1-6-linked mannose. The combined enzymatic action of both recombinant α-mannosidases allowed the sequential degradation of high-mannose-type N-glycans. The facile expression and purification procedures in combination with strict substrate specificities make α-mannosidases from S. canadensis promising candidates for bioanalytical applications.