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PubMed2005

Modulation of water activity on fungicide effect on Aspergillus niger growth in Sabouraud dextrose agar medium*.

AIMS: To examine whether water activity (aw) in combination with low concentration of fungicides can be used to effectively control Aspergillus niger van Tieghem growth in cultural medium, the Sabouraud dextrose agar (SDA). The data would be used as baseline information for reducing A. niger contamination in insect artificial diets. METHODS AND RESULTS: Aspergillus niger was isolated from an insect artificial diet. Four concentration levels (i.e. 0, 1, 10 and 20 micromol) of two fungicides (i.e. amphotericin B and itraconazole) were tested against A. niger under four aw levels (i.e. 0.994, 0.961, 0.921 and 0.859) adjusted by including 0, 12.5, 25 and 38% of glycerol in the medium mixture. Aspergillus niger growth was significantly reduced at low fungicide concentration (1 micromol), and at reduced aw. The spore germination was prevented with either higher fungicide concentration (>10 micromol), or low aw in the medium (aw < 0.921). The two ecological determinants (fungicides and aw) showed a significant impact on A. niger survival in the medium (P < 0.0001). Itraconazole is more effective than amphotericin B in controlling A. niger contamination in the agar medium. CONCLUSION: Adjustment of aw (with 12.5% of glycerol) in combination with 1 mumol of itraconazole can effectively prevent A. niger growth in the SDA cultural medium. SIGNIFICANCE AND IMPACT OF THE STUDY: Aspergillus niger contaminations have frequently affected the quality of insects produced from mass rearing facilities. Low aw in combination with low fungicide concentration has the potential to become one of the most cost-effective management strategies to prevent A. niger contamination in insect artificial diets. The effect of fungicides and low aw in artificial diets on insect biology needs to be further examined.

Antifungal Agents↗
PubMed1996

Effect of fermentation conditions on the production of citric acid from cheese whey by Aspergillus niger.

The effect of pH value, methanol, and salt concentration on the production of citric acid from cheese whey by two strains of Aspergillus niger, i.e. CAIM 111 and CAIM 167, was investigated. Lactose concentration, utilized lactose, citric acid concentration, conversion coefficient of lactose to citric acid, and mycelial dry weight were measured during the fermentation process. The maximum citric acid concentration (1.06 and 0.82 g/l), and conversion coefficient (5.58 and 7.45%) were obtained at pH 3.5 after 9 days of fermentation for A. niger CAIM 111 and A. niger CAIM 167, respectively. The presence of 4% (v/v) methanol in the fermentation medium increased the amount of citric acid produced by A. niger CAIM 111 and A. niger CAIM 167 by 23% and 18%, respectively. Both strains showed a high ability to utilize lactose for the production of citric acid when grown in the presence of 10% (w/v) salt. The conversion coefficient of lactose to citric acid was 28.24% for A. niger CAIM 111 and 25.60% for A. niger CAIM 167 when the fermentation medium had a 10% (w/v) level of salt. The cumulative effect of fermentation medium pH (3.5), methanol concentration (4%, v/v) and salt concentration (10%, w/v) during the fermentation process of whey did not enhance the production of citric acid by A. niger CAIM 111, while it did increase the production of citric acid by A. niger CAIM 167 by about 4-fold.

Aspergillus niger↗
PubMed1989

Tryptophan auxotrophic mutants in Aspergillus niger: inactivation of the trpC gene by cotransformation mutagenesis.

Aspergillus niger tryptophan auxotrophic mutants have been isolated after UV irradiation of conidiospores. The mutants belong to two different complementation groups, trpA and trpB, which complement each other in heterokaryons. Neither of the mutations could be complemented with the cloned A. niger trpC gene. To obtain A. niger trpC mutants in a direct way, gene inactivation by cotransformation was performed. For this purpose an in-frame gene fusion between the A. niger trpC and Escherichia coli lacZ genes was constructed and shown to be functionally expressed after introduction into A. niger by cotransformation with the pyrA gene as selective marker. Among the beta-galactosidase expressing cotransformants, obtained with either circular or linearized vectors, no trpC mutants were detected, even after enrichment. Such mutants, however, could be obtained by cotransformation of A. niger with specific fragments of the fusion gene. Biochemical analysis of the cotransformants indicated that in nearly all cases the fusion gene had replaced the wild-type trpC gene. Genetic analysis showed that the trpC mutation is not linked to any of the A. niger loci described so far. The trpC mutants can be complemented by the cloned A. niger trpC gene as well as by the A. nidulans trpC gene.

Aspergillus niger↗
PubMed1999

Oxalic acid production by Aspergillus niger: an oxalate-non-producing mutant produces citric acid at pH 5 and in the presence of manganese.

The external pH appeared to be the main factor governing oxalic acid production by Aspergillus niger. A glucose-oxidase-negative mutant produced substantial amounts of oxalic acid as long as the pH of the culture was 3 or higher. When pH was decreased below 2, no oxalic acid was formed. The activity of oxaloacetate acetylhydrolase (OAH), the enzyme believed to be responsible for oxalate formation in A. niger, correlated with oxalate production. OAH was purified from A. niger and characterized. OAH cleaves oxaloacetate to oxalate and acetate, but A. niger never accumulated any acetate in the culture broth. Since an A. niger acuA mutant, which lacks acetyl-CoA synthase, did produce some acetate, wild-type A. niger is apparently able to catabolize acetate sufficiently fast to prevent its production. An A. niger mutant, prtF28, previously isolated in a screen for strains deficient in extracellular protease expression, was shown here to be oxalate non-producing. The prtF28 mutant lacked OAH, implying that OAH is the only enzyme involved in oxalate production in A. niger. In a traditional citric acid fermentation low pH and absence of Mn2+ are prerequisites. Remarkably, a strain lacking both glucose oxidase (goxC) and OAH (prtF) produced citric acid from sugar substrates in a regular synthetic medium at pH 5 and under these conditions production was completely insensitive to Mn2+.

Acetate-CoA Ligase↗
PubMed1993

Molecular cloning, expression and structure of the endo-1,5-alpha-L-arabinase gene of Aspergillus niger.

Secretion of endo-1,5-alpha-L-arabinase A (ABN A) by an Aspergillus niger xylulose kinase mutant upon mycelium transfer to medium containing L-arabitol was immunochemically followed with time to monitor its induction profile. A cDNA expression library was made from polyA+ RNA isolated from the induced mycelium. This library was immunochemically screened and one ABN A specific clone emerged. The corresponding abnA gene was isolated from an A. niger genomic library. Upon Southern blot analysis, a 3.1-kb HindIII fragment was identified and subcloned to result in plasmid pIM950. By means of co-transformation using the A. niger pyrA gene as selection marker, the gene was introduced in both A. niger and A. nidulans uridine auxotrophic mutants. Prototrophic A. niger and A. nidulans transformants overproduced A. niger ABN A upon growth in medium containing sugar beet pulp as the sole carbon source, thereby establishing the identity and functionality of the cloned gene. The DNA sequence of the complete HindIII fragment was determined and the structure of the abnA gene as well as of its deduced gene product were analysed. Gene abnA contains three introns within its structural region and codes for a protein of 321 amino acids. Signal peptide processing results in a mature protein of 302 amino acids with a deduced molecular mass of 32.5 kDa. A. niger abnA is the first gene encoding an ABN to be isolated and characterized.

Amino Acid Sequence↗
PubMed2006

Citric acid production by Aspergillus niger on wet corn distillers grains.

AIMS: To determine which citric acid-producing strain of Aspergillus niger utilized wet corn distillers grains most effectively to produce citric acid. METHODS AND RESULTS: Citric acid and biomass production by the fungal strains were analysed on the untreated grains or autoclaved grains using an enzyme assay and a gravimetric method respectively. Fungal citric acid production on the grains was found to occur on the untreated or autoclaved grains. The highest citric acid level on the grains was produced by A. niger ATCC 9142. The autoclaved grains supported less citric acid production by the majority of strains screened. Biomass production by the fungal strains on the untreated or autoclaved grains was quite similar. The highest citric acid yields for A. niger ATCC 9142, ATCC 10577, ATCC 11414, ATCC 12846 and ATCC 26550 were found on the untreated grains. Treatment of the grains had little effect on citric acid yields based on reducing sugars consumed by A. niger ATCC 9029 and ATCC 201122. CONCLUSIONS: It is feasible for citric acid-producing strains of A. niger to excrete citric acid on wet corn distillers grains whether the grains are treated or untreated. The most effective citric acid-producing strain of A. niger was ATCC 9142. SIGNIFICANCE AND IMPACT OF THE STUDY: The study shows that the ethanol processing co-product wet corn distillers grains could be utilized as a substrate for the commercial production of citric acid by A. niger without treatment of the grains.

Aspergillus niger↗
PubMed1997

The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides.

We report the cloning and characterization of a gene encoding a ferulic acid esterase, faeA, from Aspergillus niger and Aspergillus tubingensis. The A. niger and A. tubingensis genes have a high degree of sequence identity and contain one conserved intron. The gene product, FAEA, was overexpressed in wild-type A. tubingensis and a protease-deficient A. niger mutant. Overexpression of both genes in wild-type A. tubingensis and an A. niger protease-deficient mutant showed that the A. tubingensis gene product is more sensitive to degradation than the equivalent gene product from A. niger. FAEA from A. niger was identical to A. niger FAE-III (C. B. Faulds and G. Williamson, Microbiology 140:779-787, 1994), as assessed by molecular mass, pH and temperature optima, pI, N-terminal sequence, and activity on methyl ferulate. The faeA gene was induced by growth on wheat arabinoxylan and sugar beet pectin, and its gene product (FAEA) released ferulic acid from wheat arabinoxylan. The rate of release was enhanced by the presence of a xylanase. FAEA also hydrolyzed smaller amounts of ferulic acid from sugar beet pectin, but the rate was hardly affected by addition of an endo-pectin lyase.

Amino Acid Sequence↗
PubMed1985

Clinical and immunological reactions to Aspergillus niger among workers at a biotechnology plant.

The workforce at a biotechnology plant producing citric acid by fermentation of molasses with a strain of Aspergillus niger was studied. A combination of a respiratory questionnaire and clinical assessment identified 18 subjects (4.9% of the workforce) with work related bronchospasm. In nine of these evidence of sensitisation to A niger was obtained by skin prick tests and radioallergosorbent test (RAST) using as an antigen an extract of the A niger culture fluid from the process. Of the 325 subjects without work related bronchospasm, only nine (2.7%) had a positive prick test. There were no subjects with symptoms of extrinsic allergic alveolitis. Investigation into the source of the antigen showed that whereas, in some areas of the plant, A niger spores were present, in others there were no detectable spores. In these areas, however, extracts of filters from air samplers were shown by RAST inhibition to contain A niger antigens, indicating that the culture fluid was generating airborne antigen. RAST inhibition studies showed that the A niger culture fluid used in the process contained antigens that were not present in a commercially available A niger extract, thus emphasising the importance in this type of investigation of using antigens prepared from material to which the workers are exposed.

Air Pollutants, Occupational↗
PubMed2005

Perspective: big oil, rural poverty, and environmental degradation in the Niger Delta region of Nigeria.

The Niger Delta region of Nigeria is richly endowed with both renewable and non-renewable natural resources. It contains 20 billion of Africa's proven 66 billion barrels of oil reserves and more than 3 trillion cubic meters of gas reserves. Oil and gas resources of the Niger Delta account for over 85% of the nation's gross domestic product (GDP), over 95% of the national budget, and over 80% of the nation's wealth. Paradoxically, the Niger Delta remains the poorest region, due largely to the ecologically unfriendly exploitation of oil and gas and state policies that expropriate the indigenous peoples of the Niger Delta of their rights to these natural resources. The ecological devastation occasioned by the activities of oil transnational corporations (TNCs) have rendered farming and fishing useless, previously the main occupations of these rural people. The people of the Niger Delta are deprived of their share of the wealth on which the entire nation depends; they "benefit" only from compensation for incidents of oil pollution. At the same time, occurrences of oil spills in the Niger Delta region have increased. In this article, it is argued that the ecologically unfriendly activities of oil TNCs, and the state's petroleum development policies, lead to poverty in the Niger Delta, and poverty in turn leads to environmental degradation. It is the dynamics of this interconnectedness that we wish to explore.

Conservation of Natural Resources↗
PubMed1985

Transformation of Aspergillus niger by the amdS gene of Aspergillus nidulans.

Aspergillus niger grows poorly on acetamide as a nitrogen or carbon source and lacks sequences detectably homologous to the amdS gene encoding the acetamidase of Aspergillus nidulans. We have taken advantage of these observations to develop a transformation system for A. niger using the amdS gene as a dominant heterologous marker for selecting transformants on the basis of acetamide utilization. Transformants varied in their ability to grow on amide media and the number of integrated copies of the amdS plasmid ranged from 1 or 2 to greater than 100. Southern analysis of transformants revealed that the multiple copies were integrated into the chromosome in tandem arrays. This result indicates that transformation of A. niger is more similar to mammalian cells than to yeast. Analysis of enzyme activity levels and RNA levels showed that most of the copies of amdS were expressed. Mitotic stabilities of transformants were found to be high. A transformant containing greater than 100 copies of the amdS gene was impaired in omega-amino acid utilization, a result that has also been found in A. nidulans. Since, in A. nidulans, omega-amino acids induce acetamidase via a characterizied regulatory gene (amdR/intA) this observation implies that titration of an analogous A. niger regulatory gene product by multiple amdS copies has occurred. Additional evidence suggested that the amdS gene is regulated in A. niger. It has also been shown that an unselected plasmid can be co-transformed with the amdS plasmid into A. niger.

Amidohydrolases↗
PubMed1997

Overexpression and characterization of Aspergillus awamori wild-type and mutant glucoamylase secreted by the methylotrophic yeast Pichia pastoris: comparison with wild-type recombinant glucoamylase produced using Saccharomyces cerevisiae and Aspergillus niger as hosts.

Glucoamylase from Aspergillus niger (identical to Aspergillus awamori glucoamylase) is an industrially important, multidomain N- and O-glycosylated starch-hydrolase. To produce protein-engineered glucoamylase, heterologous expression is established in the methylotrophic yeast Pichia pastoris. Using the vector pHIL-D2, the cDNA encoding A. awamori glucoamylase is inserted in the yeast genome downstream of the 5' AOX1 promoter to replace the AOX1 gene. Induction by 0.75% methanol for 48 h led to synthesis of secreted glucoamylase to give around 0.4 g/liter, as directed by the A. awamori signal sequence. Recombinant glucoamylase produced in P. pastoris, Saccharomyces cerevisiae, or A. niger displayed similar catalytic properties, thiol content, and isoelectric point. Glucoamylase from P. pastoris, however, has higher thermostability than the enzymes from S. cerevisiae, A. niger, or a commercial preparation of A. niger glucoamylase. The average Mr determined by matrix-assisted laser desorption ionization mass spectrometry of these enzymes is thus 82,327, 83,869, 82,839, and 80,370, respectively, and neutral sugar analysis shows the differences to be due to variation in the extent of glycosylation. Compared to wild-type, single-residue mutation generally reduced the amount of secreted glucoamylase in S. cerevisiae and A. niger. In P. pastoris, however, the Cys320 --> Ala/Glu400 --> Cys double mutant is produced at 0.3 g/liter, or 75% of wild-type glucoamylase, while the corresponding single mutants have been produced at l and 20% of the wild-type level in S. cerevisiae and A. niger, respectively.

Aspergillus niger↗
PubMed2006

Aspergillus niger genomics: past, present and into the future.

Aspergillus niger is a filamentous ascomycete fungus that is ubiquitous in the environment and has been implicated in opportunistic infections of humans. In addition to its role as an opportunistic human pathogen, A. niger is economically important as a fermentation organism used for the production of citric acid. Industrial citric acid production by A. niger represents one of the most efficient, highest yield bioprocesses in use currently by industry. The genome size of A. niger is estimated to be between 35.5 and 38.5 megabases (Mb) divided among eight chromosomes/linkage groups that vary in size from 3.5-6.6 Mb. Currently, there are three independent A. niger genome projects, an indication of the economic importance of this organism. The rich amount of data resulting from these multiple A. niger genome sequences will be used for basic and applied research programs applicable to fermentation process development, morphology and pathogenicity.

Aspergillus niger↗
PubMed1997

Characterization and overexpression of the Aspergillus niger gene encoding the cAMP-dependent protein kinase catalytic subunit.

The gene pkaC encoding the catalytic subunit of cAMP-dependent protein kinase has been isolated from the industrially important filamentous fungus Aspergillus niger. A probe for screening A. niger phage libraries was generated by a polymerase chain reaction using degenerate primers. cDNA and genomic DNA clones were isolated and sequenced. An open reading frame of 1440 bp, interrupted by three short introns, encodes a polypeptide of 480 amino acids with a calculated molecular mass of 53813 Da. The cAMP-dependent protein kinase catalytic subunit (PKA-C) from A. niger has a 126 amino acid extension at the N-terminus compared to the PKA-C of higher eukaryotes that-except for the first 15 amino acids, which are homologous to the Magnaporthe grisea PKA-C-shows no significant similarity to the N-terminal extension of PKA-C of other lower eukaryotes. The catalytic core of PKA-C of A. niger shows extensive homology with the PKA-C isolated from all other eukaryotes. Low-stringency hybridization did not reveal any other pkaC homologue in A. niger. The cloned pkaC was used for transformation of A. niger, leading to increased levels of pkaC mRNA and PKA-C activity. Transformants overexpressing pkaC were phenotypically different with respect to growth, showing a more compact colony morphology, accompanied by a more dense sporulation, especially on media containing trehalose and glycerol. A number of transformants also showed a strongly reduced or complete absence of sporulation. This phenotype was quickly lost upon propagation of the strains.

Amino Acid Sequence↗
PubMed1997

Cloning and characterization of two rhamnogalacturonan hydrolase genes from Aspergillus niger.

A rhamnogalacturonan hydrolase gene of Aspergillus aculeatus was used as a probe for the cloning of two rhamnogalacturonan hydrolase genes of Aspergillus niger. The corresponding proteins, rhamnogalacturonan hydrolases A and B, are 78 and 72% identical, respectively, with the A. aculeatus enzyme. In A. niger cultures which were shifted from growth on sucrose to growth on apple pectin as a carbon source, the expression of the rhamnogalacturonan hydrolase A gene (rhgA) was transiently induced after 3 h of growth on apple pectin. The rhamnogalacturonan hydrolase B gene was not induced by apple pectin, but the rhgB gene was derepressed after 18 h of growth on either apple pectin or sucrose. Gene fusions of the A. niger rhgA and rhgB coding regions with the strong and inducible Aspergillus awamori exlA promoter were used to obtain high-producing A. awamori transformants which were then used for the purification of the two A. niger rhamnogalacturonan hydrolases. High-performance anion-exchange chromatography of oligomeric degradation products showed that optimal degradation of an isolated highly branched pectin fraction by A. niger rhamnogalacturonan hydrolases A and B occurred at pH 3.6 and 4.1, respectively. The specific activities of rhamnogalacturonan hydrolases A and B were then 0.9 and 0.4 U/mg, respectively, which is significantly lower than the specific activity of A. aculeatus rhamnogalacturonan hydrolase (2.5 U/mg at an optimal pH of 4.5). Compared to the A enzymes, the A. niger B enzyme appears to have a different substrate specificity, since additional oligomers are formed.

Amino Acid Sequence↗
PubMed2003

Mannitol is required for stress tolerance in Aspergillus niger conidiospores.

D-Mannitol is the predominant carbon compound in conidiospores of the filamentous fungus Aspergillus niger and makes up 10 to 15% of the dry weight. A number of physiological functions have been ascribed to mannitol, including serving as a reserve carbon source, as an antioxidant, and to store reducing power. In this study, we cloned and characterized the A. niger mpdA gene, which encodes mannitol 1-phosphate dehydrogenase (MPD), the first enzyme in the mannitol biosynthesis pathway. The mpdA promoter contains putative binding sites for the development-specific transcription factors BRLA and ABAA. Furthermore, increased expression of mpdA in sporulating mycelium suggests that mannitol biosynthesis is, to a certain extent, developmentally regulated in A. niger. Inactivation of mpdA abolished mannitol biosynthesis in growing mycelium and reduced the mannitol level in conidiospores to 30% that in the wild type, indicating that MPD and mannitol 1-phosphate phosphatase form the major metabolic pathway for mannitol biosynthesis in A. niger. The viability of spores after prolonged storage and germination kinetics were normal in an mpdA null mutant, indicating that mannitol does not play an essential role as a reserve carbon source in A. niger conidia. However, conidiospores of a DeltampdA strain were extremely sensitive to a variety of stress conditions, including high temperature, oxidative stress and, to a lesser extent, freezing and lyophilization. Since mannitol supplied in the medium during sporulation repaired this deficiency, mannitol appears to be essential for the protection of A. niger spores against cell damage under these stress conditions.

Aspergillus niger↗
PubMed1996

Lysis and biological control of Aspergillus niger by Bacillus subtilis AF 1.

A biocontrol rhizobacterial strain of Bacillus subtilis AF 1 grown for 6 h was coinoculated with Aspergillus niger at different time intervals and microscopic observations revealed adherence of bacterial cells to the fungal mycelium. Bacterial cells multiplied in situ and colonized the mycelial surface. Growth of AF 1 resulted in damage to the cell wall, followed by lysis. AF 1 inoculation into media containing A. niger at 0, 6, and 12 h suppressed > 90% fungal growth, while in 18- and 24-h cultures fungal growth inhibition was 70 and 56%, respectively, in terms of dry weight. In dual culture the fungal growth was not accompanied by formation of spores. The mycelial preparation of A. niger as principal carbon source supported the growth of B. subtilis, as much as chitin. Extracellular protein precipitate from B. subtilis culture filtrate had a significant growth-retarding effect on A. niger. Groundnut seeds bacterized with B. subtilis showed a reduced incidence of crown rot in a niger infested soil, suggesting a possible role of A. subtilis in biological control of A. niger.

Antibiosis↗
PubMed2006

Generation, annotation, and analysis of an extensive Aspergillus niger EST collection.

BACKGROUND: Aspergillus niger, a saprophyte commonly found on decaying vegetation, is widely used and studied for industrial purposes. Despite its place as one of the most important organisms for commercial applications, the lack of available information about its genetic makeup limits research with this filamentous fungus. RESULTS: We present here the analysis of 12,820 expressed sequence tags (ESTs) generated from A. niger cultured under seven different growth conditions. These ESTs identify about 5,108 genes of which 44.5% code for proteins sharing similarity (E < or = 1e(-5)) with GenBank entries of known function, 38% code for proteins that only share similarity with GenBank entries of unknown function and 17.5% encode proteins that do not have a GenBank homolog. Using the Gene Ontology hierarchy, we present a first classification of the A. niger proteins encoded by these genes and compare its protein repertoire with other well-studied fungal species. We have established a searchable web-based database that includes the EST and derived contig sequences and their annotation. Details about this project and access to the annotated A. niger database are available. CONCLUSION: This EST collection and its annotation provide a significant resource for fundamental and applied research with A. niger. The gene set identified in this manuscript will be highly useful in the annotation of the genome sequence of A. niger, the genes described in the manuscript, especially those encoding hydrolytic enzymes will provide a valuable source for researchers interested in enzyme properties and applications.

Aspergillus niger↗
PubMed2006

Mutagenesis and analysis of mold Aspergillus niger for extracellular glucose oxidase production using sugarcane molasses.

Aspergillus niger ORS-4.410, a mutant of A. niger ORS-4, was generated by repeated ultraviolet (UV) irradiation. Analysis of the UV treatment dose on wild-type (WT) A. niger ORS-4, conidial survival, and frequency of mutation showed that the maximum frequency of positive mutants (25.5%) was obtained with a 57% conidial survival rate after the second stage of UV irradiation. The level of glucose oxidase (GOX) production from mutant A. niger ORS-4.410 thus obtained was 149% higher than that for WT strain A. niger ORS-4 under liquid culture conditions using hexacyanoferrate (HCF)-treated sugarcane molasses (TM) as a cheaper carbohydrate source. When subcultured monthly for 24 mo, the mutant strain had consistent levels of GOX production (2.62 +/- 0.51 U/mL). Mutant A. niger ORS-4.410 was markedly different from the parent strain morphologically and was found to grow abundantly on sugarcane molasses. The mutant strain showed 3.43-fold increases in GOX levels (2.62 +/- 0.51 U/mL) using HCF-TM compared with the crude form of cane molasses (0.762 +/- 0.158 U/mL).

Aspergillus niger↗