Functional Characterization of Carbohydrate-Binding Modules in a New Alginate Lyase, TsAly7B, from Thalassomonas sp. LD5
| Autor: | Luyao Tang, Mengmeng Bao, Zhigang Liu, Feng Han, Wengong Yu, Zhelun Zhang |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
enzymatic activity Mutant Pharmaceutical Science 02 engineering and technology product distribution brown algae 03 medical and health sciences Drug Discovery lcsh:QH301-705.5 Pharmacology Toxicology and Pharmaceutics (miscellaneous) carbohydrate-binding module Thermostability chemistry.chemical_classification biology alginate lyase enzymatic characterization 021001 nanoscience & nanotechnology biology.organism_classification Lyase thermostability 030104 developmental biology Enzyme lcsh:Biology (General) Biochemistry chemistry polysaccharide lyase Specific activity Carbohydrate-binding module 0210 nano-technology Function (biology) Bacteria |
| Zdroj: | Marine Drugs, Vol 18, Iss 1, p 25 (2019) Marine Drugs Volume 18 Issue 1 |
| ISSN: | 1660-3397 |
| DOI: | 10.3390/md18010025 |
| Popis: | Alginate lyases degrade alginate into oligosaccharides, of which the biological activities have vital roles in various fields. Some alginate lyases contain one or more carbohydrate-binding modules (CBMs), which assist the function of the catalytic modules. However, the precise function of CBMs in alginate lyases has yet to be fully elucidated. We have identified a new multi-domain alginate lyase, TsAly7B, in the marine bacterium Thalassomonas sp. LD5. This novel lyase contains an N-terminal CBM9, an internal CBM32, and a C-terminal polysaccharide lyase family 7 (PL7) catalytic module. To investigate the specific function of each of these CBMs, we expressed and characterized the full-length TsAly7B and three truncated mutants: TM1 (CBM32-PL7), TM2 (CBM9-PL7), and TM3 (PL7 catalytic module). CBM9 and CBM32 could enhance the degradation of alginate. Notably, the specific activity of TM2 was 7.6-fold higher than that of TM3. CBM32 enhanced the resistance of the catalytic module to high temperatures. In addition, a combination of CBM9 and CBM32 showed enhanced thermostability when incubated at 80 ° C for 1 h. This is the first report that finds CBM9 can significantly improve the ability of enzyme degradation. Our findings provide new insight into the interrelationships of tandem CBMs and alginate lyases and other polysaccharide-degrading enzymes, which may inspire CBM fusion strategies. |
| Databáze: | OpenAIRE |
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