Hemocompatible glutaminase free l-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression. Issue 31 (9th March 2016)

• Record Type: Journal Article
• Authors: Shakambari, Ganeshan; Birendranarayan, Anand Kumar; Angelaa Lincy, Maria Joseph; Rai, Sameer Kumar; Ahamed, Quazi Taushif; Ashokkumar, Balasubramaniem; Saravanan, Matheshwaran; Mahesh, Ayyavu; Varalakshmi, Perumal
• Is Part Of: RSC advances. Volume 6:Issue 31(2016)
• Page Start: 25943
• Page End: 25951
• Publication Date: 2016-03-09
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c6ra00727a
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : Glutaminase freel -asparaginase from a marine isolate Bacillus tequilensis PV9W: production, purification, characterization and its biological applications. Abstract : Bacillus tequilensis PV9W, a marine bacterial isolate obtained from Gulf of Mannar, Rameswaram, India, produced glutaminase freel -asparaginase which was purified to homogeneity with a significant increase (13 fold) in specific activity. The apparent K m (0.045 ± 0.013 mM) and V max (7.465 ± 0.372 μmol ml −1 min −1 ) values of this purifiedl -asparaginase was identified and it was found that the maximum activity of thel -asparaginase was at a pH 8.5 and a temperature of 35 °C. The enzyme is a mixed α/β protein and the influence of different effectors were documented. The purifiedl -asparaginase had effective acrylamide degradation activity (6 IU per ml) and cytotoxic activity against HeLa cell lines with an IC50 of 0.036 ± 0.009 IU per ml. Furthermore, the purified enzyme showed p53 dependent G2 arrest in HeLa cells analyzed by FACS and was hemocompatible. Thus, this study highlights the marine isolate PV9W as a potential source for glutaminase freel -asparaginase with industrial as well as pharmaceutical applications. This study also paves a way for a possible therapeutic drug with the least amount of side effects.