title: Production of L-asparaginase, an anticancer agent, from Aspergillus niger using agricultural waste in solid state fermentation.
abstract: This article reports the production of high levels of L-asparaginase from a new isolate of Aspergillus niger in solid state fermentation (SSF) using agro-wastes from three leguminous crops (bran of Cajanus cajan, Phaseolus mungo, and Glycine max). When used as the sole source for growth in SSF, bran of G. max showed maximum enzyme production followed by that of P. mungo and C. cajan. A 96-h fermentation time under aerobic condition with moisture content of 70%, 30 min of cooking time and 1205-1405 micro range of particle size in SSF appeared optimal for enzyme production. Enzyme yield was maximum (40.9 +/- 3.35 U/g of dry substrate) at pH 6.5 and temperature 30 +/- 2 degrees C. The optimum temperature and pH for enzyme activity were 40 degrees C and 6.5, respectively. The study suggests that choosing an appropriate substrate when coupled with process level optimization improves enzyme production markedly. Developing an asparaginase production process based on bran of G. max as a substrate in SSF is economically attractive as it is a cheap and readily available raw material in agriculture-based countries.
authors.affiliation: School of Biochemical Engineering, Institute of Technology, Banaras Hindu University, Varanasi-221005, India. abha91@yahoo.co.in
authors.forename: Abha
authors.initials: A
authors.lastname: Mishra
mesh_terms: D000383:Agriculture; D000970:Antineoplastic Agents / Q000737:chemistry / Q000494:pharmacology*; D001215:Asparaginase / Q000096:biosynthesis* / Q000737:chemistry; D001234:Aspergillus niger / Q000201:enzymology*; D018533:Biomass; D019149:Bioreactors; D001709:Biotechnology / Q000379:methods*; D003470:Culture Media; D005285:Fermentation; D006863:Hydrogen-Ion Concentration; D012037:Refuse Disposal; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors
chemical_list: D000970:Antineoplastic Agents; D003470:Culture Media; D001215:Asparaginase