ХАРАКТЕРИСТИКА КАТАЛИТИЧЕСКИХ СВОЙСТВ ДВУХ НОВЫХ РЕКОМБИНАНТНЫХ ФУКОИДАНАЗ ИЗ МОРСКОЙ БАКТЕРИИ FORMOSA ALGAE

Two genes encoding fucoidanase (FFA1 and FFA2) were identified in a genome of the marine bacterium Formosa algae. Bioinformatic analysis of the amino acid sequences revealed to their multidomain organization. Truncated at the C-terminus derivatives of fucoidanases were obtained to identify a function of these domains. Full-length fucoidanases and their truncated derivatives had an enzymatic activity. The presence of activity in truncated derivatives indicates the localization of the active site in the N-terminal portion of these enzymes. FFA1 and FFA2 were activated by the ions Ca2 +, Ba2 +, Mg2 + and Mn2 +, while ions Al3 +, Cu2 +, Sn2 + and Fe3 + inhibited both enzymes. We classified FFA1 and FFA2 as endo-1 → 4-α L-fucanases based on the substrate specificity.