Biochemical Characterization of a Carrageenase, Car1383, Derived From Associated Bacteria of Antarctic Macroalgae
A carrageenase gene, car1383 , was obtained from the metagenome of Antarctic macroalgae-associated bacteria. The amino acid sequence of its product showed up to 33% similarity with other carrageenases and contained a GH16-family motif. The recombinant Car1383 was heterologously expressed in Escheric...
| Published in: | Frontiers in Microbiology |
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| Main Authors: | , , , , , |
| Format: | Article in Journal/Newspaper |
| Language: | unknown |
| Published: |
Frontiers Media SA
2022
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.3389/fmicb.2022.851182 https://www.frontiersin.org/articles/10.3389/fmicb.2022.851182/full |
| Summary: | A carrageenase gene, car1383 , was obtained from the metagenome of Antarctic macroalgae-associated bacteria. The amino acid sequence of its product showed up to 33% similarity with other carrageenases and contained a GH16-family motif. The recombinant Car1383 was heterologously expressed in Eschericia coli and exhibited maximal activity at 50°C and pH 6.0, with a K m of 6.51 mg/ml and a V max of 55.77 U/mg. Its activity was enhanced by some cations (Na + , K + , and Fe 2+ ), but inhibited or inactivated by others (Sr 2+ , Ca 2+ , Ni 2+ , Ba 2+ , Mn 2+ , Cu 2+ , Fe 3+ , and Mg 2+ ). Car1383 degraded carrageenan into neocarrabiose and neocarratetraose. Site-directed mutagenesis indicated that putative active sites, E 190 and E 195 , conserved sites, W 183 and G 255 , play important roles in Car1383 activity. This study provides a new candidate for the industrial preparation of bioactive algal oligosaccharides. |
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