10.22376/ijpbs.2019.10.1.p1-12 Volume 6 Issue 2 2015 (April - June) L-asparaginase is an anti-cancer enzyme used in lymphoblastic leukaemia chemotherapy. Bacterial isolates were screened for potential producers of L-asparaginase using a phenol red indicator in growth medium and those microbial culture displayed pink red coloured colony was selected for further studies and was identified as lessThan i greaterThan Grimontia hollisae (Vibrio) lessThan /i greaterThan by using fatty acid methyl ester (FAME) analysis. The enzyme production was carried out by submerged fermentation. The enzyme was partially purified by ammonium sulphate precipitation and dialysis was carried out to remove the excess salt. A Lineweaver-Burk analysis showed a lessThan i greaterThan Km lessThan /i greaterThan value of 5.95 mM and lessThan i greaterThan Vmax lessThan /i greaterThan of 0.588 IU/min. The characterised enzyme exhibited maximal enzyme activity at pH 8 and temperature 37°C. The activity of L-asparaginase is activated by mono-cations K lessThan sup greaterThan + lessThan /sup greaterThan , Na lessThan sup greaterThan + lessThan /sup greaterThan and various effectors including 2-mercaptoethanol, whereas it is moderately inhibited by various divalent ions Hg lessThan sup greaterThan ++ lessThan /sup greaterThan , Cu lessThan sup greaterThan ++ lessThan /sup greaterThan and Zn lessThan sup greaterThan ++ lessThan /sup greaterThan . Substrate specificity studies indicated that, L-asparaginase has greater affinity towards L-asparagine. The amino acid composition of L-asparaginase was also determined. C.N.KHOBRAGADE,SHWETA R GOPHANE AND MENKA G JAYEBHAYE L-asparaginase, Amino acid composition, purification, Grimontia hollisae (vibrio), FAME-GC Analysis 1372-1386