Selective isolation of Aspergillus niger mutants with enhanced glucose oxidase production

Gromada, A.; Fiedurek, J.

doi:10.1111/j.1365-2672.1997.tb02875.x

Cited by 12 publications

(16 citation statements)

References 18 publications

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“…Screening, genetic improvement, and evaluation of new GODoverproducing strains is very important in improving the efficiency and economics of the industrial process. Several attempts have been made to improve GOD production in A. niger by strain selection using classical screening and mutagenesis techniques [4,6,16,20], optimizing of cultivation conditions [7,8,12,18], and genetic engineering [8,19,21].…”

Section: Introductionmentioning

confidence: 99%

Screening, mutagenesis and protoplast fusion of Aspergillus niger for the enhancement of extracellular glucose oxidase production

Khattab

Bazaraa

2005

J IND MICROBIOL BIOTECHNOL

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Various strains of Aspergillus niger were screened for extracellular glucose oxidase (GOD) activity. The most effective producer, strain FS-3 (15.9 U mL(-1)), was mutagenized using UV-irradiation or ethyl methane sulfonate. Of the 400 mutants obtained, 32 were found to be resistant to 2-deoxy D: -glucose, and 17 of these exhibited higher GOD activities (from 114.5 to 332.1%) than the original FS-3 strain. Following determination of antifungal resistance of the highest producing mutants, four mutants were selected and used in protoplast fusions in three different intraspecific crosses. All fusants showed higher activities (from 285.5 to 394.2%) than the original strain. Moreover, of the 30 fusants isolated, 19 showed higher GOD activity than their corresponding higher-producing parent strain.

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Section: Introductionmentioning

confidence: 99%

Screening, mutagenesis and protoplast fusion of Aspergillus niger for the enhancement of extracellular glucose oxidase production

Khattab

Bazaraa

2005

J IND MICROBIOL BIOTECHNOL

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“…This resulted in producing a large biomass (18.6 g / L) and extracellular catalase activity (47.5 U / ml). A few rapports have been published on the production of extracellular catalase by Aspergillus niger on a synthetic medium (Nishikawa et al 1993, Gromada andFiedurek 1997). However, to our knowledge, no work has been published on the production of extracellular catalase by fungi on natural media composed essentially of date extract.…”

Section: Discussionmentioning

confidence: 86%

Decommissioned dates: chemical composition and fermentation substrate for the production of extracellular catalase by an Aspergillus phoenicis mutant

Kacem-Chaouche¹,

Dehimat²,

Meraïhi³

et al. 2013

ABJNA

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The recovery of dates downgraded as a fermentation medium for the production of extracellular catalase by Aspergillus phoenicis K30 was studied. Analysis of the chemical composition of pulp and kernel flour of dates showed that the pulp had a considerably greater carbohydrate content compared to the kernel (84 vs 2.93% respectively). However, the kernel flour was richer in nitrogen (0.68% vs 0.34), mineral elements (3.63 vs 1.28%) and in essential fatty acids C18: 2 vs C18: 3 than the pulp flour. The soluble extract of the date flour showed that sugars solubilised at 90% consisted of sucrose, fructose and glucose. Therefore, this extract, being an important source of carbon and energy, was used in the current study as a fermentation medium (after supplementation with 20% of corn steep) for the production of extracellular catalase by A. Phoenicis K30. During the course of this fermentation, the biomass was estimated at 18.6 g / L after 72 h of culture, while the maximum concentration of extracellular catalase (47.5 U / ml) was reached at 96 h of fermentation. The mycelium obtained in pellet form is suitable for industrial exploitation of this process.

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“…2-deoxy-D-glucose (2dDG) acts as a catabolic repressor and was used in this study for the selection of mutants as described by Gromada and Fiedurek (1997). It suppresses/inhibits the growth of parent spores, but mutant spores appear on PDA.…”

Section: Selection and Evaluation Of Mutantsmentioning

confidence: 99%

Hyperproduction of Manganese Peroxidase through Chemical Mutagenesis of Trametes versicolor IBL-04 and Optimization of Process Parameters

Ramzan¹,

Asgher²,

Sheikh³

et al. 2013

BioResources

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This is the first report on chemical mutagenesis of Trametes versicolor IBL-04 to develop a hyper-producing mutant for overproduction of manganese peroxidase (MnP) using sugarcane bagasse as a substrate. A freshly prepared inoculum of indigenously isolated T. versicolor IBL-04 was treated with 100 µg mL -1 (v/v) ethyl methane sulfonate (EMS) and ethidium bromide (EB) separately for different time periods. The selected mutants and parent strain were cultured in solid-state fermentation (SSF) conditions to select the hyper-producing mutants. After selection of hyper-producing EMS-and EB-treated mutants, the fermentation parameters, including substrate type, incubation time, initial pH of the medium, temperature, moisture level, and carbon-to-nitrogen ratio (C:N), were optimized by adopting the Classical Optimization Strategy. T. versicolor IBL-04 treated for 90 min with EMS (EMS-90 mutant) gave maximum MnP production (935 U mL -1 ) after 8 days of fermentation. Supplementation with carbon and nitrogen sources significantly enhanced mutant growth, and under optimum conditions, the maximum MnP production by the mutant strain increased to 3045 U mL -1. The results indicated that the random chemical mutagenesis significantly enhanced the MnP production. The increased production of MnP by the EMS-90 mutant strain suggest its potential for commercial-scale enzyme production and biotechnological applications.

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Selective isolation of Aspergillus niger mutants with enhanced glucose oxidase production

Cited by 12 publications

References 18 publications

Screening, mutagenesis and protoplast fusion of Aspergillus niger for the enhancement of extracellular glucose oxidase production

Screening, mutagenesis and protoplast fusion of Aspergillus niger for the enhancement of extracellular glucose oxidase production

Decommissioned dates: chemical composition and fermentation substrate for the production of extracellular catalase by an Aspergillus phoenicis mutant

Hyperproduction of Manganese Peroxidase through Chemical Mutagenesis of Trametes versicolor IBL-04 and Optimization of Process Parameters

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