Table_1_Biochemical Characterization of a Carrageenase, Car1383, Derived From Associated Bacteria of Antarctic Macroalgae.DOC

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 Escherici...

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Bibliographic Details
Main Authors: Jiang Li, Xiaoqian Gu, Qian Zhang, Liping Fu, Jiaojiao Tan, Luying Zhao
Format: Dataset
Language:unknown
Published: 2022
Subjects:
Microbiology
Microbial Genetics
Microbial Ecology
Mycology
carrageenase
Antarctic macroalgae
associated bacteria
metagenome
site-directed mutagenesis
Antarctic
Antarc*
Online Access:https://doi.org/10.3389/fmicb.2022.851182.s001
https://figshare.com/articles/dataset/Table_1_Biochemical_Characterization_of_a_Carrageenase_Car1383_Derived_From_Associated_Bacteria_of_Antarctic_Macroalgae_DOC/19487201
Description
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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