XXXX and CD Spectral Analysis for Identification and Structure Prediction of a Purified, Novel, Organic Solvent Stable, Fibrinolytic Metalloprotease from @entity5259 B80.

@entity5259 @entity215 @entity219 @entity214
The ability to predict protein function from structure is becoming increasingly important; hence, elucidation and determination of protein structure become the major steps in proteomics. The present study was undertaken for identification of metalloprotease produced by @entity5259 B80 and recognition of characteristics that can be industrially exploited. The enzyme was purified in three steps combining precipitation and chromatographic methods resulting in 33.5% recovery with 13.1-fold purification of enzyme which was detected as a single band with a molecular mass of 26   kDa approximately in @entity214 -PAGE and zymogram. The @entity215 showed that the enzyme exhibited 70-93% similarity with @entity219 metalloproteases from various strains Bacillus sp. specifically from @entity5259 group. The sequence alignment revealed the presence of @entity219 -binding region VVVHEMCHMV in the most conserved C terminus region. Secondary structure of the enzyme was obtained by CD spectra and I-TASSER. The enzyme kinetics revealed a Michaelis constant (K m ) of 0.140    mol/ml and V max of 2.11    mol/min. The application studies showed that the enzyme was able to hydrolyze various proteins with highest affinity towards casein followed by BSA and gelatin. The enzyme exhibited strong fibrinolytic, collagenolytic, and gelatinolytic properties and stability in various organic solvents.
