Purification and properties of utral protense isolated from goat skin

Abstract

A neutral proteinase isolated from goat skin was purified and its physico-chemical properties were studied. The six different treatments when given successively to the original enzyme extract resulted in a I22-fold purification retaining59% of the original activity. The purified enzyme was found to be homogeneous and capable of hydrolysing casein, egg albumin and haemoglobin although to different degrees. Of the skin proteins studied, albumin, globulin and mucoid were readily hydrolysed hy the proteinase, whereas collagen and elastin remained unaffected. The enzyme activity was optimum between pH 7.5 and 8.0 in case of almost all protein substrates. The enzyme was found to be quite stable at a pH range of 6.5 to 8.5. The enzyme was fairly thermolabile and was found to lose its activity when healed at a temperature above 60° C and exposed to ultraviolet rays. The enzyme was inactivated by thiol group, metal chelating agents and heavy metal ions.