Optimization of culture conditions and bench-scale production of anticancer enzyme L-asparaginase by submerged fermentation from Aspergillus terreus CCT 7693

Author(s)

Costa-Silva, T. A. ^[1] ; Camacho-Cordova, D. I. ^[1] ; Agamez-Montalvo, G. S. ^[2] ; Parizotto, L. A. ^[3] ; Sanchez-Moguel, I. ^[1] ; Pessoa-, Jr., A. ^[1]

Affiliation

^[1] Univ Sao Paulo, Fac Pharmaceut Sci, Ave Prof Lineu Prestes 580, B16 Cidade Univ, BR-05508000 Sao Paulo - Brazil

^[2] Univ Fed Ceara, Fortaleza, Ceara - Brazil

^[3] Univ Sao Paulo, Polytech Sch, Sao Paulo - Brazil

• Document type: Journal article
• Source: PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY; v. 49, n. 1, p. 95-104, JAN 2 2019.
• Web of Science Citations: 0

Abstract

L-Asparaginase amidohydrolase (EC 3.5.1.1) has received significant attention owing to its clinical use in acute lymphoblastic leukemia treatment and non-clinical applications in the food industry to reduce acrylamide (toxic compound) formation during the frying of starchy foods. In this study, a sequential optimization strategy was used to determine the best culture conditions for L-asparaginase production from filamentous fungus Aspergillus terreus CCT 7693 by submerged fermentation. The cultural conditions were studied using a 3-level, central composite design of response surface methodology, and biomass and enzyme production were optimized separately. The highest amount of biomass (22.0 g center dot L-1) was obtained with modified Czapek-Dox medium containing glucose (14 g center dot L-1), L-proline (10 g center dot L-1), and ammonium nitrate (2 g center dot L-1) fermented at 37.2 degrees C and pH 8.56; for maximum enzyme production (13.50 U center dot g(-1)), the best condition was modified Czapek-Dox medium containing glucose (2 g center dot L-1), L-proline (10 g center dot L-1), and inoculum concentration of 4.8 x 10(8) espore center dot mL(-1) adjusted to pH 9.49 at 34.6 degrees C. The L-asparaginase production profile was studied in a 7 L bench-scale bioreactor and a final specific activity of 13.81 U center dot g(-1) was achieved, which represents an increase of 200% in relation to the initial non-optimized conditions. (AU)

• FAPESP's process: 13/08617-7 - Production of extracellular L-asparaginase: from bioprospecting to the engineering of an antileukemic biopharmaceutical
• Grantee: Adalberto Pessoa Junior
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 13/19584-2 - Production of extracellular L-asparaginase by fungus Aspergullus terreus
• Grantee: Tales Alexandre da Costa e Silva
• Support Opportunities: Scholarships in Brazil - Post-Doctoral