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

• 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

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.