Characterization of SdGA, a cold adapted glucoamylase from Saccharophagus degradans.

WAYLLACE, NATAEL; HEDÍN, NICOLAS; BUSI, MARIA VICTORIA; DIEGO FABIAN GOMEZ CASATI

Virtual

Congreso; Reunión conjunta 2020 SAIB-SAMIGE; 2020

SAIB

We investigated the structural and functionalproperties of SdGA, a glucoamylase (GA) from Saccharophagus degradans, a marine bacterium which degradesdifferent complex polysaccharides athigh rate. SdGA is composed mainly by aN-terminal GH15_N domain linked to a C-terminal catalyticdomain (CD) found inthe GH15 family of glycosylhydrolases with an overall structure similar tootherbacterial GAs. The protein was expressed in Escherichia coli cells,purified and its biochemical properties were investigated. Although SdGA has amaximum activity at 39°C and pH 6.0, it also shows high activity in a widerange, from low to mild temperatures, like cold-adapted enzymes. Furthermore,SdGA has a higher content of flexible residues and a larger CD due to variousamino acid insertions compared to other thermostable GAs. We propose that thisnovel SdGA, is a cold-adapted enzyme that might be suitable for use indifferent industrial processes that require enzymes which act at low or mediumtemperatures.