ABSTRACT

L-asparaginase is the first therapeutic enzyme with antineoplastic properties that has been studied broadly by researchers and scientists far and wide. L-asparaginase was first observed by Lang in 1904. Aspartame is a methyl ester of aspartic acid and phenylalanine dipeptides. The aim of this research was to ascertain the effect of aspartame on L- asparaginase enzyme activities from marine water sample. Soil and water samples from lagoon and ocean were collected for the isolation of Streptomyces spp. Isolation and enumeration were carried out by serial dilution and pour plate method. Pure culture of actinomycetes were obtained by using the streak plate method, Identification of isolated marine actinomycetes was carried out according to Bergy’s Manual of Determinative Bacteriology. Production of L-asparaginase was carried out in Erlenmeyer flask containing Czapek Dox broth supplemented with L-asparaginase (1g/L), with one used as the control and the other with 0.5g aspartame in it, as production medium for 7 days at 120 rpm and at 28 ⁰C. Optical density (growth rate) were determined at 600nm using the spectrophotometer. Aspartame had highest optical density of 0.382667 ± 0.001528 on day 7 of production and the least optical density of 0.094 ± 0.001 on day zero(0). L-asparaginase activity with aspartame was  25 𝜇mol/mL/min on day 7 and the control had activity value of 66.6666 ± 0.052481. It also showed that the source aspartame did not favour the production of L-asparaginase.