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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Optimization of nutrient medium components for production of a client endo-beta-1,4-xylanase from Aspergillus fumigatus var. niveus using a recombinant Aspergillus nidulans strain

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Author(s):
Abdella, Asmaa [1, 2, 3] ; Segato, Fernando [4] ; Wilkins, Mark R. [1, 2, 5]
Total Authors: 3
Affiliation:
[1] Univ Nebraska, Dept Biol Syst Engn, 3605 Fair St, Lincoln, NE 68583 - USA
[2] Univ Nebraska, Ind Agr Prod Ctr, 3605 Fair St, Lincoln, NE 68583 - USA
[3] Univ Sadat City, Genet Engn & Biotechnol Res Inst, Dept Ind Biotechnol, POB 79, Sadat City 22857 - Egypt
[4] Univ Sao Paulo, Lorena Sch Engn, Dept Biotechnol, Synthet & Mol Biol Lab, Estr Municipal Campinho S-N, Lorena, SP - Brazil
[5] Univ Nebraska, Dept Food Sci & Technol, 1901 N 21st St, Lincoln, NE 68588 - USA
Total Affiliations: 5
Document type: Journal article
Source: BIOCATALYSIS AND AGRICULTURAL BIOTECHNOLOGY; v. 20, JUL 2019.
Web of Science Citations: 0
Abstract

The goal of this study was to optimize a nutrient medium to maximize production of endo-beta-1,4-xylanase (hereafter referred to as xylanase) using an Aspergillus nidulans modified by integration of an AFUMN-GH10 gene from Aspergillus fumigants var. niveus. This modification resulted in high-yield secretion and accumulation of recombinant protein. Xylanases are an industrially relevant enzyme class used in food production and bioprocessing. High-titer production of xylanase was achieved by the cultivation of A. nidulans in the presence of maltose. A 2-level Plackets-Burman design was used to determine which medium components significantly affected xylanase production. NaNO3, maltose and KCl showed significant effects on xylanase production. These three medium components were further optimized using a 3-level Box-Behnken design, and their optimum levels were maltose, 120 g/L; NaNO3, 12 g/L and KCl, 2 g/L. A xylanase activity of 1,620 U/mL, (12,460 U/g of maltose) was observed when using the optimum medium, which was 280% greater than the maximum level obtained with the basic medium. Pyridoxine concentration in the optimum medium was reduced to limit growth and divert substrate toward enzyme production. Reducing pyridoxine from 1,000 mu g/ml to 300 mu g/ml increased xylanase activity to 1,790 U/ml. Optimized medium with reduced pyridoxine was then tested in a stirred tank bioreactor, which resulted in 112% more xylanase activity and 43% less dry cell weight compared with the medium containing 1,000 mu g/ml of pirydoxine. (AU)

FAPESP's process: 14/06923-6 - Sugar cane biomass recalcitrance: basic knowledge related to the cell wall construction, pretreatment and enzymatic digestion, applied for the development of innovative biorefinery models
Grantee:Andre Luis Ferraz
Support Opportunities: Program for Research on Bioenergy (BIOEN) - Thematic Grants
FAPESP's process: 14/18714-2 - Enzymatic oxidation of sugarcane bagasse: discovery, characterization and new application of oxidative enzymes active in carbohydrates, applied to the enhancement of a fungal cell factory
Grantee:Fernando Segato
Support Opportunities: Program for Research on Bioenergy (BIOEN) - Young Investigators Grants