Abstract
The effect of ammonium chloride, urea and sodium nitrate as supplementary nitrogen source on the production of extracellular L-asparaginase using Aspergillus terreus MTCC 1782 was investigated using 5- level Latin square design. The statistical reliability and significance of the variables was studied by performing ANOVA for experimental L-asparaginase activity using Dataplot software. Among the supplementary nitrogen sources studied, ammonium chloride was found to be the best for maximum L-asparaginase activity (confidence level of 96.61%) with less biomass formation (confidence level of 21.93%). The maximum L-asparaginase activity obtained was of 26.47 IU/mL by A. terreus MTCC 1782 using groundnut oil cake powder as natural substrate in submerged fermentation.
Highlights
L-asparaginase (L-asparagine amino hydrolase, E.C.3.5.1.1) catalyzes the hydrolysis of L-asparagine into L-aspartic acid and ammonia
Lasparagine is an essential amino acid for the growth of tumor cells, whereas the growth of normal cells is not dependent on its requirement as it can be synthesized in amounts sufficient for their metabolic needs using their own enzyme L-asparagine synthetase
It converts the amino acid asparagine to aspartic acid reduces acrylamide formation during processing of high starch food products (FAO/WHO, 2001; Pedreschi et al, 2008)
Summary
L-asparaginase (L-asparagine amino hydrolase, E.C.3.5.1.1) catalyzes the hydrolysis of L-asparagine into L-aspartic acid and ammonia. This has been a clinically acceptable anti tumor agent for the effective treatment of acute lymphoblastic leukemia and lymphosarcoma. It converts the amino acid asparagine to aspartic acid reduces acrylamide formation during processing of high starch food products (FAO/WHO, 2001; Pedreschi et al, 2008). The demand for this enzyme is expected to increase several fold in coming years due to its potential industrial application as food processing aid besides clinical applications
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