Garcia-Junceda_1991_Enzyme.Microb.Technol_13_275

Orsellinate depside hydrolase (EC. 3.1.1.40) is produced by lichen cells, in which it hydrolyses depsides to monocyclic phenols. The hydrolase, which uses evernic acid as a substrate, has been purified 40-fold and entrapped in 20% polyacrylamide gel. The Km value of immobilized enzyme was 7.5 mM for the substrate. The entrapped hydrolase has a pH optimum of 6.5 and is highly thermostable. Orcinol, a well-known inhibitor of free hydrolase, does not have any significant effect on the entrapped enzyme. After 2 months of storage at 25C, the immobilized enzyme retains about one-half the initial activity.