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 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.

Abstract licence: CC BY

36 more references, whose wording the paper’s licence keeps private.

A person counts once a day per paper. We keep no cookie and no address: a reader is a hash that changes every day. Any month under five reads shows no number.