The purpose of this study is to report a iota-carrageenase which degrades iota-carrageenan yielding neo-iota-carratetraose as the main product in the absence of NaCl. The gene for a new iota-carrageenase, CgiB_Ce, from Cellulophaga sp. QY3 was cloned and sequenced. It comprised an ORF of 1,386 bp encoding for a protein of 461 amino acid residues. From its sequence analysis, CgiB_Ce is a new member of GH family 82 and shared the highest identity of 32 % in amino acids with iota-carrageenase CgiA2 from Zobellia galactanovorans indicating that it is a hitherto uncharacterized protein. The recombinant CgiB_Ce had maximum specific activity (1,870 U/mg) at 45 A degrees C and pH 6.5. It was stable between pH 6.0-9.6 and below 40 A degrees C. Although its activity was enhanced by NaCl, the enzyme was active in the absence of NaCl. CgiB_Ce is an endo-type iota-carrageenase that hydrolyzes beta-1,4-linkages of iota-carrageenan, yielding neo-iota-carratetraose as the main product (more than 80 % of the total product).