期刊名称：Karbala International Journal of Modern Science
印刷版ISSN：2405-609X
电子版ISSN：2405-609X
出版年度：2017
卷号：3
期号：4
页码：202-211
DOI：10.1016/j.kijoms.2017.08.007
语种：English
出版社：Elsevier
摘要：Abstractl-asparaginase is an efficient anti-cancer enzyme due to its remarkable property in hydrolyzing essential amino acid of acute lymphoblastic leukemia cancer (l-asparagine) into aspartic acid and ammonia. Various sources ofl-asparaginase had been identified including extraction from animal or plant as well as through microbial fermentation. Generally, researchers preferred to generatel-asparaginase by engaging microbe as thel-asparaginase producer because the abundant amount ofl-asparaginase can be harvested in an affordable manner. The present study aimed at screening, optimization, and purification of microbial productionl-asparaginase in presence of cooked chicken bone wastes as substrate. Different controlling parameters were studied including physiological (incubation period and temperature, initial pH-value, and substrate concentration), nutritional (carbon and nitrogen sources) and microbial parameters (inoculum sizes). As a result, the highest amount ofl-asparaginase was harvested when the fermentation was incubated at 40 °C for 2 days at pH 9 in presence of 1% w/v of cooked chicken bone waste as a sole substrate. Besides that, starch and ammonium chloride were discovered as the best-supplemented carbon and nitrogen sources respectively when 12% v/v ofEscherichia coliATCC 10536 suspension was inoculated. The harvestedl-asparaginase has proceeded with a series of purification and the specific activity achieved after partial purification was 0.549 IU/mg. In conclusion, optimization of controlling parameters as well as supplementation of cooked chicken bone as substrate capable to further enhance the production ofl-asparaginase.Highlights•l-asparaginase producer was identified after screening process, meanwhile optimization was studied.•Improvement ofl-asparaginase production was seen after being optimized and supplemented with CCB as substrate.•The maximum activity of dialyzed enzyme was identified after characterization study.
