Effects of chemical modification on stereoselectivity of Pseudomonas cepacia lipase

Article abstract of DOI:10.1016/S0957-4166(00)80115-9

Two chemically modified forms of lipase from Pseudomonas cepacia were prepared by acylation of the free amino groups of the protein with acetic and succinic anhydrides.The catalytic activity, the enantioselectivity and the thermal stability of the modified enzymes were compared with that of the native form.Succinylation determined an increase of stability without affecting the catalytical properties of the enzyme in the hydrolysis of chiral esters.Acetylation resulted in an enhanced catalytic activity coupled to a decreased stereoselectivity and thermal stability.