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Production, isolation, and purification of L-asparaginase from Pseudomonas aeruginosa 50071 using solid-state fermentation
Faculty
Science
Year:
2004
Type of Publication:
Article
Pages:
387-393
Authors:
El-Bessoumy, AA, Sarhan, M, Mansour, J
Journal:
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY SPRINGER SINGAPORE PTE LTD
Volume:
37
Research Area:
Biochemistry \& Molecular Biology
ISSN
ISI:000223025700001
Keywords :
amino acid composition, L-asparaginase, production, Pseudomonas aeruginosa 50071, purification
Abstract:
The L-asparaginase (E. C. 3.5. 1.1) enzyme was purified to homogeneity from Pseudomonas aeruginosa 50071 cells that were grown on solid-state fermentation. Different purification steps (including ammonium sulfate fractionation followed by separation on Sephadex G-100 gel filtration and CM-Sephadex C50) were applied to the crude culture filtrate to obtain a pure enzyme preparation. The enzyme was purified 106-fold and showed a final specific activity of 1900 IU/mg with a 43\% yield. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDSPAGE) of the purified enzyme revealed it was one peptide chain with M, of 160 kDa. A Lineweaver-Burk analysis showed a K-m value of 0.147 mM and V-max of 35.7 IU. The enzyme showed maximum activity at pH 9 when incubated at 37degreesC for 30 min. The amino acid composition of the purified enzyme was also determined.
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