On the novel inhibitory action of mushroom extract of coriolus versicolor and it’s bioactivity against drug resistant bacteria salmonella typhimurium (MTCC 3241).

The aim of this study was to investigate the effects of the mushroom extract of Coriolus versicolor on drug resistant strain of S. typhimurium experimental results revealed that hot water ethanol extract and Tris- HCl ethanol extract of C. versicolor were not only effective against drug resistant strain of S.typhimurium (MTCC 3214) but also against other pathogenic microorganisms such as K. pneumoniae, S. typhi, E. coli, S. pyogenes and Aspergillus niger. The extracts exerted their effects on the microorganisms by inhibiting their growth.The optimum temperature and pH conditions for mycelial growth of C. versicolor were found to be 28±1ºC and 5.98 pH respectively. Maximum mycelial growth was observed by employing starch and ammonium sulphate as carbon and nitrogen source and on supplementing the cultivation medium with 20% (v/v) culture filtrate of C. versicolor. The present investigation highlights optimization of culture conditions and determination of antimicrobial spectrum C. versicolor .This indicate that the extracts of C. versicolor is a novel inhibitory source against drug resistant bacteria salmonella typhimurium.

L-asparaginase: A promising enzyme for treatment of acute lymphoblastic leukiemia.

Asparaginases are known to be the cornerstone for treatment of acute lymphoblastic leukemia (ALL) and are used for treatment in all pediatric regimens as well as in the majority of adult treatment protocols. Clinical hypersensitivity reactions against commercially available asparaginase have resulted in failure of asparaginase in treatment of ALL in more than 60% of cases. Thus, it is required to search for serologically different asparaginase from new organisms for the patients exhibiting sensitivity to one formulation of asparaginase, so that they can be switched to another to ensure that they receive the most efficacious treatment regimen possible. The present study report E. coli VRY-15, E. coli VRY-8 and E. coli VRY-14 as potent producer of L-asparaginase. The L-asparaginase obtained from E. coli VRY-15 showed highest specific activity i.e., 19.56 µmol/mg. Attempt was made to purify the enzyme. Molecular weight of purified L-asparaginase obtained from E. coli VRY-15 was found to be 56 K Da as determined using Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS- PAGE).