Cleaves the glycosidic bonds of gellan backbone and releases tetrasaccharide units of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the non-reducing terminal. The enzyme is highly specific to the heteropolysaccharide gellan. Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyluronate bonds of gellan backbone releasing tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-glucopyranosyluronic acid at the non-reducing end. The tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-Delta(4)-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp. Activity is stimulated by zinc, potassium, lithium, cobalt, sodium, calcium, iron, manganase, magnesium and mercury ions at a concentration of 1 mM, but inhibited by copper ions at a concentration of 1 mM. Activity is inhibited by potassium, sodium and magnesium ions at a concentration of 1 M. Activity is inhibited by urea, EDTA, dithiothreitol, p-CMB, PSF, natrium lauryl sulfate and N-bromosuccinimide. Most active from pH 5.0 to 8.0. Optimum temperature is 70 degrees Celsius. Active from 50 to 80 degrees Celsius, at 55 degrees Celsius it has 50% of its full activity. Thermostable, retains full activity after heating at 60 degrees Celsius for 24 hours. In the absence of substrate, its half life at 70 degrees Celsius is 50 minutes. In the presence of substrate full activity is retained after incubation at 70 degrees Celsius for 2.5 hours. Multimer. Expressed in the exponential growth phase. By gellan. The order of the peptides shown is unknown.