Partial Purification of Gelatinase Enzyme from Local Isolate of Brevibacillus laterosporus

Abstract

A solid state fermentation system consisting of 1:2 w/w wheat bran/fish scales
was used for the production of gelatinase enzyme activity. The activity has been screened
from a local isolate of Brevibacillus laterosporus at 37 ºC and using Tris-HCl buffer pH
7.5.
Maximum activity obtained was 3.5 U/ml. Gelatinase protein content was
precipitated using 60% ammonium sulfate. The enzyme has been partially purified on
column chromatography technique using Sephadex G-150 column (1.5X30 cm).
The elution was carried out using buffer phosphate pH 7.4. Three isoform peaks
were recorded from degraded gelatin. The obtained purification fold and recovery were
(10.58) and (43.42) % respectively.
Results indicated the possibility of using purified gelatinase in industry fields.