The stabilizing effects of polyols and sugars on porcine pancreatic lipase

Abstract

Porcine pancreatic lipase (PPL) has been used as a biocatalyst for many years and is one of the most widely used enzymes for biotechnological applications; however, it is a rather complex mixture with various active enzymes. The present study has been undertaken to determine the effects of polyols and sugars (cosolvents) on the thermal stability of PPL preparation. The thermal stability of PPL exposed to 60°C for 10 min was enhanced in the presence of cosolvents in terms of both residual specific activity and conformational stability. Thermal denaturation, changes in circular dichroism, fluorescence spectra, apparent kinetic parameters, activity, and preferential interaction parameter of PPL preparation are discussed in terms of contributions to the mechanism of thermal stability and the activity enhancement. Partial specific volume measurement of PPL in the presence of cosolvents is presented for the first time. The preferential interaction parameter (ξ₃) was negative in all cosolvents used, and maximum hydration was observed in the presence of trehalose, where the preferential interaction parameter was -0.076 g/g. The observed increase in the thermal stability of PPL preparation in the presence of cosolvents is due to the preferential hydration of the enzyme.