Mutagenesis of Aspergillus oryzae IPT-301 to improve the production of β-fructofuranosidase

Maresma, Beatriz Guilarte; Castillo, Boris; Fernandez, Rubén Cuervo; Silva, Elda Sabino da; Maiorano, Alfredo Eduardo; Rodrigues, Maria Filomena de Andrade

doi:10.1590/s1517-83822010000100027

Cited by 14 publications

(7 citation statements)

References 25 publications

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“…Khattab and Bazaraa (2005) used 2-deoxy-D-glucose to examine the resistance of mutants produced after UV and EMS for the enhanced production of glucose oxidase. 2-Deoxy-D-glucose has been also used as a criterion for the selection of positive mutants for the enhanced production of amylase, glucose-6-phosphate dehydrogenase, catalase and β-fructofuranosidase (Maresma et al, 2010). The mutants having the greater resistance against 2-deoxy-D-glucose were subjected to enzyme diffusion zone test for visual analysis and quantitative analysis using spectrophotometer.…”

Section: Resultsmentioning

confidence: 99%

Enhanced production and characterization of a novel -D-glucose:oxygen-1-oxidoreductase by using Aspergillus niger UV-180-C mutant strain

Rasul¹,

Zia²,

Sheikh³

et al. 2011

Afr. J. Biotechnol.

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Along with other emerging health consequences, diabetes mellitus is one of the critical threats spreading all over the world with continuity. The investigation of glucose level in diabetic patients requires the key enzyme β-D-glucose:oxygen-1-oxidoreductase/glucose oxidase, where its optimized production by mutant derived strain could affect the economic burden and accuracy of the test. Wild type Aspergillus niger was subjected to ultraviolet radiation for enhanced production of glucose oxidase. It was found that UV-180-C is a potential mutant derived strain, screened by using 2-deoxy-Dglucose. Optimum production of glucose oxidase from A. niger UV-180-C was carried out by using CSL (2%), fermentation period (36 h), pH (5.5 and 4.5 for wild and mutant respectively), temperature (30°C), MgSO 4 .7H 2 O (0.0%), CaCO 3 (0.1%), KH 2 PO 4 (0.8 and 1.0% for wild and mutant strains), Urea (0.3%). Crude enzyme was subjected to ammonium sulfate precipitation and resulted into 145.8 UmL-1 activity. Glucose oxidase from mutant derived A. niger exhibited optimum pH at 6, temperature 20°C, K m 10mM and V max 142 UmL-1. The pyridoxal phosphate caused significant inhibition to the enzyme which indicates the presence of lysyl residues near or at the active site of the enzyme from both wild and mutant derived strains.

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Section: Resultsmentioning

confidence: 99%

Enhanced production and characterization of a novel -D-glucose:oxygen-1-oxidoreductase by using Aspergillus niger UV-180-C mutant strain

Rasul¹,

Zia²,

Sheikh³

et al. 2011

Afr. J. Biotechnol.

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“…; Maresma et al . ) with slight modification. The induction of mutagenesis was carried out by UV irradiation at 30 cm under a UV lamp (25 W).…”

Section: Methodsmentioning

confidence: 99%

“…The mutants were determined according to previous complex mutagenesis method (Sun et al 2008;Maresma et al 2010) with slight modification. The induction of mutagenesis was carried out by UV irradiation at 30 cm under a UV lamp (25 W).…”

Section: Mutagenesis Proceduresmentioning

confidence: 99%

“…The results indicated that an increase in SDS concentration over 0.006 g/L caused a significant decrease. Consequently, SDS was added to the culture medium to establish toxic conditions to the cells; thus, mutants that had become resistant to a certain level of SDS were screened (Maresma et al 2010). At concentrations of 0.008 and 0.016 g/L, colonies with diameter averages of 9.5 and 3.9 mm in 5 days were obtained in further mutagenesis experiments.…”

Section: Mutagenesis Analysismentioning

confidence: 99%

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Improvement of Laccase Production and its Characterization by Mutagenesis

Sun²,

Liang

et al. 2015

Journal of Food Biochemistry

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In this study, laccase production was enhanced using mutant Shiraia sp. The Shiraia sp. GZS1 strain was mutated using ultraviolet irradiation, followed by screening of strains that were resistant to certain stressors. The mutant GZ11K2 was selected and used for further studies. 2,2′-Azino-bis(3-ethylben-zothiazoline-6-sulfonate) was used as substrate for both wild and mutant laccases at optimal pH (4.0). The mutant laccase exhibited a broader active pH range. The mutant laccase also showed a higher optimal catalytic temperature, more active under alkaline conditions, and higher temperature range than the wild one. The mutant strains produced higher yield of laccase than the wild strain even at high salinity of 3 g/L NaCl. Both laccases were mildly inhibited by sodium dodecyl sulfate (0.5 mM), ethanol (50%) and ethylenediaminetetraacetic acid (1 mM), and almost completely inhibited by NaN3 (20 μM) and DTT (1 mM), stable in the presence of metal ions except Ag + and Hg 2+. PRACTICAL APPLICATIONSLaccase is extensively used in various applications, such as pulp delignification, decoloration, biopolymer modification, biotransformation and food dechlorination. A newly isolated laccase-producing strain Shiraia sp. GZS1 and a genetically stable mutant GZ11K2 were established with 1.82 times laccase activity compared with that of the wild strain. The mutant Shiraia sp. GZ11K2 laccase was active over a wider pH and temperature ranges and more stable than the wild strain under neutral and alkaline conditions. The laccase from the mutant GZ11K2 with higher laccase productivity and enhanced enzyme properties can be used in biotechnological and industrial applications.

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“…Over the past several decades, great efforts have been made to enhance riboflavin production and develop better production media. Many different methods have been used to improve the productivity of the wild strain, such as UV irradiation (6, 11, 14), chemical-induced mutagenesis (20), antimetabolite mutagenesis (13, 19) and metabolic engineering approaches (5, 18). …”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of an Ashbya gossypii mutant for improved riboflavin production

Wei¹,

Hurley²,

Jiang³

et al. 2012

Braz. J. Microbiol.

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The use of the filamentous fungus, Ashbya gossypii, to improve riboflavin production at an industrial scale is described in this paper. A riboflavin overproducing strain was isolated by ultraviolet irradiation. Ten minutes after spore suspensions of A. gossypii were irradiated by ultraviolet light, a survival rate of 5.5% spores was observed, with 10% of the surviving spores giving rise to riboflavin-overproducing mutants. At this time point, a stable mutant of the wild strain was isolated. Riboflavin production of the mutant was two fold higher than that of the wild strain in flask culture. When the mutant was growing on the optimized medium, maximum riboflavin production could reach 6.38 g/l. It has even greater promise to increase its riboflavin production through dynamic analysis of its growth phase parameters, and riboflavin production could reach 8.12 g/l with pH was adjusted to the range of 6.0-7.0 using KH2PO4 in the later growth phase. This mutant has the potential to be used for industrial scale riboflavin production.

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Mutagenesis of Aspergillus oryzae IPT-301 to improve the production of β-fructofuranosidase

Cited by 14 publications

References 25 publications

Enhanced production and characterization of a novel -D-glucose:oxygen-1-oxidoreductase by using Aspergillus niger UV-180-C mutant strain

Enhanced production and characterization of a novel -D-glucose:oxygen-1-oxidoreductase by using Aspergillus niger UV-180-C mutant strain

Improvement of Laccase Production and its Characterization by Mutagenesis

Isolation and characterization of an Ashbya gossypii mutant for improved riboflavin production

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