Interest in lipases has markedly increased to their potential industrial
applications. Because of the interest and largest producer of Turkey, In this study, it was aimed that Lipase from hazelnut seed identified as yomra species isolated, purified and characterized.
Lipase from hazelnut seed was purified 1255 fold to homogeneous state by ammonium sulfate precipitation, dialysis and Sephadex G-100 gel filtration chromatography after by defatting from hazelnut proteins.
The purified enzyme showed single band when it was subjected to SDSPAGE. The molecular weight determined by SDS-PAGE was 20 kDa. Purified lipase from hazelnut seed exhibited the maximum activity at pH 9.0 and 50˚C, stable under alkaline conditions (pH 7.0-10.0) and at temperatures between 20-55˚C.
Lipase from hazelnut seed was determined more specific versus triolein, tributyrin and olive oil among the natural oils as substrate.
To determine the storage stability of lipase from hazelnut seed, the activity assays carried out for a period of one year. it was observed that about 83% of its activity was retained of 9 months at -20˚C. Then the lipase activity retains constant.
In the presence of 1.0mM CaCl2, the lipase activity was considerably increased by 77%. Km and Vmax values of purified lipase from hazelnut seed versus triolein as substrate calculated 4.545mM and 80 U/dk.mg.Enzyme, respectively.