Partial purification and properties of penicillium chrysogenum lipase

ABSTRACT

A purification procedure of Penicillium chrysogenum S-J5 lipase was developed. The purification process has been achieved by dialysis, precipitation with ammonium sulfate, gel-filtration [sephadex G-200 employed] techniques associated with T.C.Z. "Tributyrin-clearing zone", assay resulted in 14 purification folds with a maximum specific activity of 108.83 mu g Lipase/mg protein. The purified enzyme preparation showed optimal activity at pH 8.8 using tris-HCI buffer at 0.2% tributyrin [Substrate] concentration. Some ions caused activation of this enzyme viz. K+ [1-103ppm], Li+ [1-103ppm], Co++ [1 ppm], Mn++ [1 and 10 ppm] and Fe+++ [1 ppm]. Other ions caused inhibition viz. Cu++ 1-103 ppm], Fe+++ [10-103ppm], Co++ [101- 103ppm], Sb++ [1-103ppm], Ca++ [101-103ppm] Mn++ [100-103ppm]. The effect of certain commercial market drugs on the activity of the purified preparation enzyme resulted in a stimulatory effect of chloramphenicol [0.08 and 0.1% dose]. Sulphadiazine, streptomycin and salicylic acid exhibited no effect. Analgine, sulpha guanidine and tetracycline showed inhibitory effects