Characterization of the biochemical properties of recombinant Xyn10C from a marine bacterium, Saccharophagus degradans 2-40
| Autor: | In Geol Choi, Kyoung Heon Kim, Hyeok-Jin Ko, Ja Kyong Ko |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Aquatic Organisms Hot Temperature Glycoside Hydrolases Bioengineering Xylose law.invention 03 medical and health sciences chemistry.chemical_compound Hydrolysis Bacterial Proteins law Saccharophagus degradans Xylobiose Glycoside hydrolase chemistry.chemical_classification biology General Medicine Hydrogen-Ion Concentration biology.organism_classification Xylan Recombinant Proteins 030104 developmental biology Enzyme Gram-Negative Aerobic Rods and Cocci chemistry Biochemistry Recombinant DNA Xylans Biotechnology |
| Zdroj: | Bioprocess and Biosystems Engineering. 39:677-684 |
| ISSN: | 1615-7605 1615-7591 |
| DOI: | 10.1007/s00449-016-1548-2 |
| Popis: | Endo-1,4-β-xylanases are mostly classified into glycoside hydrolase (GH) family 10 or 11. In this study, we examined the catalytic functions of a recombinant endo-1,4-β-xylanase belonging to GH10 (Xyn10C) from a marine bacterium, Saccharophagus degradans 2-40. Optimal activity of this enzyme was evident at 30 °C and pH 7.0, but activity remained even at low temperatures, indicating its adaptation to cold. With respect to other xylanases known to be active in cold temperatures, Xyn10C is unique in that it showed maximal activity in the presence of 2 M of NaCl. The action patterns of recombinant Xyn10C on xylans from hardwood and softwood differed in part, but the enzyme hydrolyzed polysaccharidic substrates primarily to xylobiose and xylotriose through xylo-oligosaccharides, releasing a small amount of xylose. The K m and V max values on birchwood xylan were 10.4 mg mL(-1) and 253 µmol mg(-1) min(-1), respectively. The efficient catalytic function of Xyn10C on short-length xylo-oligosaccharide chains was similar to the typical function of other known GH10 xylanases. |
| Databáze: | OpenAIRE |
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