May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. This enzyme has a broad substrate specificity, and shows strong preference for glucose pentaacetate, beta-naphthylacetate, and p-nitrophenyl acetate (pNPA). Also active toward acetylated xylan. Almost completely inhibited by diethylpyrocarbonate at 5 mM and completely inhibited by phenylmethylsulfonyl fluoride (PMSF) at 50 mM. Dimethyl phosphite achieves only a 53% inhibition. Also inhibited by metal ions (magnesium, manganese and calcium) and chelating agent (EDTA) at the same level. Optimum pH is 8.5. The enzyme is more active in the 7.5-9.0 range, achieving a sharp decrease in the activity below pH 7.0. Optimum temperature is 35 degrees Celsius. The enzyme is quite thermostable in the range of 35 to 40 degrees Celsius, and suffering a decrease in thermostability above 45 degrees Celsius. Monomer. Up-regulated by growth on type I rhamnogalacturonan. Belongs to the 'GDSL' lipolytic enzyme family.