Biochemical Characterization of a Carrageenase, Car1383, Derived From Associated Bacteria of Antarctic Macroalgae

A carrageenase gene, , 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 and exhibited ma...

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Bibliographic Details
Published in:Frontiers in microbiology 2022-03, Vol.13, p.851182-851182
Main Authors: Li, Jiang, Gu, Xiaoqian, Zhang, Qian, Fu, Liping, Tan, Jiaojiao, Zhao, Luying
Format: Article
Language:English
Subjects:
Antarctic macroalgae
associated bacteria
carrageenase
metagenome
Microbiology
site-directed mutagenesis
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Summary:A carrageenase gene, , 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 and exhibited maximal activity at 50°C and pH 6.0, with a of 6.51 mg/ml and a of 55.77 U/mg. Its activity was enhanced by some cations (Na , K , and Fe ), but inhibited or inactivated by others (Sr , Ca , Ni , Ba , Mn , Cu , Fe , and Mg ). Car1383 degraded carrageenan into neocarrabiose and neocarratetraose. Site-directed mutagenesis indicated that putative active sites, E and E , conserved sites, W and G , play important roles in Car1383 activity. This study provides a new candidate for the industrial preparation of bioactive algal oligosaccharides.
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2022.851182