ArticleCurrent genetics1993
Induction of glucose oxidase, catalase, and lactonase in Aspergillus niger.
Article in Current genetics, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 64 citations in OpenAlex.
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- Forward Genetics by Genome Sequencing Uncovers the Central Role of theFrontiers in microbiology · 2018Article
- Identification of a transcription factor controlling pH-dependent organic acid response in Aspergillus niger.PloS one · 2012Article
- Systemic analysis of the response of Aspergillus niger to ambient pH.Genome biology · 2009Article
- Screening, mutagenesis and protoplast fusion of Aspergillus niger for the enhancement of extracellular glucose oxidase production.Journal of industrial microbiology & biotechnology · 2005Article
- Cloning and characterization of gluconolactone oxidase of Penicillium cyaneo-fulvum ATCC 10431 and evaluation of its use for production of D-erythorbic acid in recombinant Pichia pastoris.Applied and environmental microbiology · 2004Article
- Cloning and characterization of two rhamnogalacturonan hydrolase genes from Aspergillus niger.Applied and environmental microbiology · 1997Article
- A new glucose oxidase from Aspergillus niger: characterization and regulation studies of enzyme and gene.Applied microbiology and biotechnology · 1996Article
- Optimization of glucose oxidase production by Aspergillus niger using genetic- and process-engineering techniques.Applied microbiology and biotechnology · 1995Article
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8 authors at 1 institution in 1 country.
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Abstract
The induction of glucose oxidase, catalase, and lactonase activities was studied both in wild-type and in glucose oxidase regulatory and structural mutants of Aspergillus niger. The structural gene for glucose oxidase was isolated and used for Northern analysis and in transformation experiments using various gox mutations. Wild-type phenotype could be restored in the glucose oxidase-negative mutant (goxC) by transformation with the structural gene. We conclude, therefore, that the goxC marker which is located on chromosome 2 represents the structural gene of glucose oxidase. Glucose and a high oxygen level are necessary for the induction of all three enzyme activities in the wild-type strain and it was shown that both glucose and oxygen effects reflect regulation at the transcriptional level. The goxB mutation results in constitutive expression of all three activities although modulated to some extent by the carbon source. The goxE mutation only has an effect on lactonase and glucose oxidase expression and does not relieve the necessity for a high oxygen level. Catalase and lactonase could not be induced in the glucose oxidase-negative strain (goxC). Addition of H2O2 resulted in the induction of all three enzymes in the wild-type without glucose being present. The H2O2 induction is probably mediated by the goxB product. Besides the H2O2 induction there is still an effect of the carbon source on the induction. A model for induction of glucose oxidase, catalase, and lactonase in A. niger is discussed.(ABSTRACT TRUNCATED AT 250 WORDS)
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