%0 Journal Article
%T Thrombolytic Activity of Alkaline Protease Purified from a Mutant Strain Bacillus licheniformis MZK05M9
%A ATM Zafrul Azam
%A Md Abdul Mazid
%A Md Arafat Al Mamun
%A Md Asad Uz Zaman
%A Md Mozammel Hoq
%A Taqiyah Akhtar
%J Bangladesh Pharmaceutical Journal
%D 2018
%R https://doi.org/10.3329/bpj.v21i1.37908
%X Investigations were performed to find out new microbial enzymes as thrombolytics having better efficacy and specificity. Mutant strain of Bacillus species, B. licheniformis MZK05M9 was cultured in modified urea-glucose media followed by purification using ammonium sulphate precipitation and ultrafiltration through centricon tube of specific MWCO value. The production method yielded 823.42 units/mg of the crude enzyme from mutant strain MZK05M9 and after purification 37695.64 units/mg. The molecular weight of the purified enzyme was estimated as 27.2 kDa and purification increased its specific activity to 16.5 fold with a recovery of 10%. The purified proteases were identified as serine proteases by irreversible inhibition of activity with phenylmethylsulfonyl fluoride (PMSF) and it exhibited 32.84% thrombolytic activity, by in vitro clot lysis assay. Stability studies showed that crude enzyme from mutant strain MZK05M9 remained stable up to a temperature of 45£¿C and showed maximum stability at pH range 7.5 to 8.5. Our observation indicates that proteases produced by Bacillus licheniformis mutant have the potential to be developed as a viable thrombolytic agent. Bangladesh Pharmaceutical Journal 21(1): 63-70, 2018
%K Bacillus licheniformis
%K protease
%K purification
%K thrombolytic activity
%U https://www.banglajol.info/index.php/BPJ/article/view/37908