Showing papers on "Aspergillus niger published in 1998"
TL;DR: It is reported that A. tumefaciens can also transfer its T-DNA efficiently to the filamentous fungus Aspergillus awamori, demonstrating DNA transfer between a prokaryote and a filamentous fungi.
Abstract: Agrobacterium tumefaciens transfers part of its Ti plasmid, the T-DNA, to plant cells during tumorigenesis. It is routinely used for the genetic modification of a wide range of plant species. We report that A. tumefaciens can also transfer its T-DNA efficiently to the filamentous fungus Aspergillus awamori, demonstrating DNA transfer between a prokaryote and a filamentous fungus. We transformed both protoplasts and conidia with frequencies that were improved up to 600-fold as compared with conventional techniques for transformation of A. awamori protoplasts. The majority of the A. awamori transformants contained a single T-DNA copy randomly integrated at a chromosomal locus. The T-DNA integrated into the A. awamori genome in a manner similar to that described for plants. We also transformed a variety of other filamentous fungi, including Aspergillus niger, Fusarium venenatum, Trichoderma reesei, Colletotrichum gloeosporioides, Neurospora crassa, and the mushroom Agaricus bisporus, demonstrating that transformation using A. tumefaciens is generally applicable to filamentous fungi.
893 citations
TL;DR: Genetic expression of genes encoding enzymes involved in xylan degradation and two endoglucanases involved in cellulose degradation was studied at the mRNA level in the filamentous fungus Aspergillus niger, indicating that transcriptional regulation by XlnR goes beyond the genes encoding xylanolytic enzymes and includes regulation of two endglucanase-encoding genes.
Abstract: The two most abundant structural polysaccharides in nature are cellulose and the hemicellulose xylan, which are closely associated in plant cell walls (4). Filamentous fungi, particularly Aspergillus and Trichoderma species, are well-known and efficient producers of both cellulolytic and hemicellulolytic enzymes. The cellulase degradation system of these organisms consists of three classes of enzymes (2): endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91), and β-glucosidases (EC 3.2.1.21). Members of all of these classes are necessary to degrade cellulose, a homopolymer of β-1,4-linked d-glucose. Xylan, however, is a heterogeneous polymer with a backbone consisting of β-1,4-linked d-xylose residues, which can be substituted at the C-2 and C-3 positions with various residues, such as acetic acid, α-l-arabinofuranose, (4-o-methyl)glucuronic acid, ferulic acid, and p-coumaric acid (5). Due to this heterogeneous composition, a more complex set of enzymes is required for xylan degradation. The following enzymes have been found to be necessary during the cooperative process of xylan breakdown: endoxylanase (EC 3.2.1.8), β-xylosidase (EC 3.2.1.37), acetylxylan esterase (EC 3.1.1.72), α-l-arabinofuranosidase (EC 3.2.1.55), arabinoxylan arabinofuranohydrolase, β-glucuronidase (EC 3.2.1.139), feruloyl esterase, and p-coumaroyl esterase (3).
The expression of cellulose- and xylan-degrading enzymes by Aspergillus and Trichoderma species has been studied extensively at the cellular level (1, 20, 21, 25). It has been shown that xylanase- and cellulase-encoding genes are regulated at the transcriptional level (10, 23, 31, 43). In the presence of d-glucose the genes are not expressed, and it has been shown that the carbon catabolite repressor protein CreA is involved in transcriptional repression of xylanase-encoding (10) and arabinase-encoding (38) genes in Aspergillus species. It has been demonstrated that in Trichoderma reesei the CreA counterpart Cre1 causes repression of transcription of cellulase-encoding (22, 23) and xylanase-encoding (30, 31) genes. However, far less is known about the mechanism by which cellulase- and xylanase-encoding genes are induced. The inducing abilities of various saccharides have been tested, and some saccharides induce the synthesis of both xylanases and cellulases (10, 21, 31, 37, 48). Nevertheless, on the basis of biochemical data (1, 20, 21) and mRNA expression analysis data (23, 31), a separate induction mechanism has been proposed for these systems in both Aspergillus and Trichoderma.
Recently, a selection system was developed to isolate Aspergillus niger strains having mutations in a transcription factor involved in induction of expression of xylanolytic genes. Complementation of such a mutation by transformation with a plasmid library led to the isolation of the A. niger xlnR gene, which encodes a transcriptional activator of the A. niger xylanolytic system (44). This xlnR gene encodes a zinc binuclear cluster protein, which is a member of the GAL4 family of transcription factors. Isolation of both the xlnR gene and A. niger xlnR loss-of-function mutants provided an opportunity to study the spectrum of genes that are controlled by XlnR at the transcriptional level.
363 citations
TL;DR: In this article, the effect of pretreatment of Aspergillus niger biomass on biosorption of lead, cadmium, copper and nickel was studied and it was shown that pretreatment with detergent and sodium hydroxide, formaldehyde, dimethyl sulphoxide and detergent resulted in significant improvements in lead, Cadmium and copper in comparison with live A. niger cells.
223 citations
TL;DR: Analysis by 1H NMR spectroscopy during hydrolysis of mannopentaose showed that the enzyme acts by the retaining mechanism, and most probably lacks a cellulose binding domain since it was unable to adsorb on cellulose.
180 citations
TL;DR: The Aspergillus niger strain MTCC 2594 lipase was optimally active at pH 7·0 and 37°C, and was found to be stable between pH 4·0–10–0 and 4–50°C and it could be effectively used for the removal of triglyceride soils in laundry.
177 citations
TL;DR: The grape pomace extracts significantly retarded human low-density lipoprotein oxidation in vitro and varied in response to enzyme type, time of enzyme treatment, particle size of the pomACE, and type of extraction solvent employed.
Abstract: Enzyme-assisted release of phenolic antioxidants from grape pomace from wine production was examined. The enzymes used were Grindamyl pectinase from Aspergillus niger and Celluclast from Trichoderm...
176 citations
TL;DR: Findings confirm that A. niger pH 2.5 acid phosphatase is irreversibly inactivated at temperatures above 80°C and that the capacity of A. fumigatus phytase to refold properly after heat denaturation may favorably affect its pelleting stability.
Abstract: Enzymes that are used as animal feed supplements should be able to withstand temperatures of 60 to 90 degrees C, which may be reached during the feed pelleting process. The thermostability properties of three histidine acid phosphatases, Aspergillus fumigatus phytase, Aspergillus niger phytase, and A. niger optimum pH 2.5 acid phosphatase, were investigated by measuring circular dichroism, fluorescence, and enzymatic activity. The phytases of A. fumigatus and A. niger were both denatured at temperatures between 50 and 70 degrees C. After heat denaturation at temperatures up to 90 degrees C, A. fumigatus phytase refolded completely into a nativelike, fully active conformation, while in the case of A. niger phytase exposure to 55 to 90 degrees C was associated with an irreversible conformational change and with losses in enzymatic activity of 70 to 80%. In contrast to these two phytases, A. niger pH 2.5 acid phosphatase displayed considerably higher thermostability; denaturation, conformational changes, and irreversible inactivation were observed only at temperatures of >/=80 degrees C. In feed pelleting experiments performed at 75 degrees C, the recoveries of the enzymatic activities of the three acid phosphatases were similar (63 to 73%). At 85 degrees C, however, the recovery of enzymatic activity was considerably higher for A. fumigatus phytase (51%) than for A. niger phytase (31%) or pH 2.5 acid phosphatase (14%). These findings confirm that A. niger pH 2.5 acid phosphatase is irreversibly inactivated at temperatures above 80 degrees C and that the capacity of A. fumigatus phytase to refold properly after heat denaturation may favorably affect its pelleting stability.
163 citations
TL;DR: Comparison of enzyme productivities showed that those determined for pectinesterase and polygalacturonase with pectin as a carbon source were three and five times higher by using the solid state rather than the submerged fermentation system.
Abstract: Production of pectinesterase and polygalacturonase by Aspergillus niger was studied in submerged and solid-state fermentation systems With pectin as a sole carbon source, pectinesterase and polygalacturonase production were four and six times higher respectively in a solid state system than in a submerged fermentation system and required a shorter time for enzyme production The addition of glucose increased pectinesterase and polygalacturonase production in the solid state system but in submerged fermentation the production was markedly inhibited A comparison of enzyme productivities showed that those determined for pectinesterase and polygalacturonase with pectin as a carbon source were three and five times higher by using the solid state rather than the submerged fermentation system The productivities of the two enzymes were affected by glucose in both fermentation systems The membranes of cells from the solid state fermentation showed increased levels of C18:1, C16:0 and C18:0 fatty acids Differences in the regulation of enzyme synthesis by Aspergillus niger depended on the fermentation system, favoring the solid state over the submerged fermentation for pectinase production
158 citations
TL;DR: Comparison of this new Thermomyces catalyst with the well-known Aspergillus niger phytase reveals other favorable properties for the enzyme derived from the thermophilic gene donor, including catalytic activity over an expanded pH range.
Abstract: The phyA gene encoding an extracellular phytase from the thermophilic fungus Thermomyces lanuginosus was cloned and heterologously expressed, and the recombinant gene product was biochemically characterized. The phyA gene encodes a primary translation product (PhyA) of 475 amino acids (aa) which includes a putative signal peptide (23 aa) and propeptide (10 aa). The deduced amino acid sequence of PhyA has limited sequence identity (ca. 47%) with Aspergillus niger phytase. The phyA gene was inserted into an expression vector under transcriptional control of the Fusarium oxysporum trypsin gene promoter and used to transform a Fusarium venenatum recipient strain. The secreted recombinant phytase protein was enzymatically active between pHs 3 and 7.5, with a specific activity of 110 μmol of inorganic phosphate released per min per mg of protein at pH 6 and 37°C. The Thermomyces phytase retained activity at assay temperatures up to 75°C and demonstrated superior catalytic efficiency to any known fungal phytase at 65°C (the temperature optimum). Comparison of this new Thermomyces catalyst with the well-known Aspergillus niger phytase reveals other favorable properties for the enzyme derived from the thermophilic gene donor, including catalytic activity over an expanded pH range.
131 citations
TL;DR: The natural dihydrate form of calcium sulphate, CaSO 4 .2H 2 O (gypsum), particularly found in gypsiferous soils and in certain building constructions, was found to be effectively solubilized by both Aspergillus niger and Serpula himantioides.
104 citations
TL;DR: The existence of at least two different alpha-galactosidases in Aspergillus niger was confirmed, with one of them showing synergism with beta-mannanase and the other with a different mass after deglycosylation with N-glycanase F.
TL;DR: Beta-Xylosidase from Aspergillus niger is an occupational allergen present in currently used baking additives, which causes sensitization in at least 4% of symptomatic bakers, according to the International Union of Immunological Societies nomenclature.
Abstract: Background: Aspergillus -derived enzymes are used in dough improvers in bakeries. Some of these enzymes are identified as causing IgE-mediated sensitization in up to 25% of bakers with workplace-related symptoms. Objective: The aim of this study was to compare the frequency of sensitization to Aspergillus xylanase, cellulase, and glucoamylase with the sensitization to α-amylase (Asp o 2) and to identify IgE-reactive proteins in enzyme preparations. Methods: Sensitization to Aspergillus -derived enzymes and cross-reactivity were retrospectively studied by enzyme allergosorbent test (EAST) and EAST-inhibition experiments. IgE-reactive proteins were detected by electrophoretic separation and immunoblotting. Liquid chromatography with electrospray ionization mass spectrometry and Edman degradation of tryptic protein fragments were used for the biochemical identification of an unknown IgE-binding protein. Results: Twenty-three percent of 171 tested bakers had specific IgE to α-amylase, 8% reacted to glucoamylase, 13% reacted to cellulase, and 11% reacted to xylanase. Xylanase and cellulase preparations, each containing at least 6 different proteins, showed cross-reactivity in the range of 80%. The main IgE-binding protein in the xylanase preparation recognized in 7 of 8 xylanase-positive subjects was a protein of about 105 kd. This protein was identified as β-xylosidase by peptide mass spectrometric fingerprinting. The identification was confirmed by matching 12 peptide sequences obtained by N-terminal and mass spectrometric sequencing to this protein. Conclusions: β-Xylosidase from Aspergillus niger is an occupational allergen present in currently used baking additives, which causes sensitization in at least 4% of symptomatic bakers. According to the International Union of Immunological Societies nomenclature, we suggest the term Asp n 14 for this allergen. (J Allergy Clin Immunol 1998; 102:256-64.)
TL;DR: Citric acid production was best in flasks, with lower yields being obtained in tray and rotating drum bioreactors, and Aspergillus niger produced the highest amount of citric acid.
Abstract: Aspergillus foetidus ACR I 3996 (=FRR 3558) and three strains of Aspergillus niger ACM 4992 (=ATCC 9142), ACM 4993 (=ATCC 10577), ACM 4994 (=ATCC 12846) were compared for the production of citric acid from pineapple peel in solid-state fermentation. A. niger ACM 4992 produced the highest amount of citric acid, with a yield of 19.4 g of citric acid per 100 g of dry fermented pineapple waste under optimum conditions, representing a yield of 0.74 g citric acid/g sugar consumed. Optimal conditions were 65% (w/w) initial moisture content, 3% (v/w) methanol, 30 degrees C, an unadjusted initial pH of 3.4, a particle size of 2 mm and 5 ppm Fe2+. Citric acid production was best in flasks, with lower yields being obtained in tray and rotating drum bioreactors.
TL;DR: A citric acid-producing strain of Aspergillus niger, grown on olive cake-based medium, was able to solubilize rock phosphate and caused considerable improvement of growth and plant P uptake in a greenhouse experiment.
Abstract: A citric acid-producing strain of Aspergillus niger, grown on olive cake-based medium, was able to solubilize rock phosphate. Solubilization of insoluble phosphate increased during the solid-state fermentation process, reaching a maximum of 164μg/ml. Various combinations of olive cake and rock phosphate, previously treated or untreated by the fungus, were introduced into a calcareous, phosphorus (P)-deficient soil to improve the growth of Trifolium repens in a greenhouse experiment. Synergistic action of both the filamentous and arbuscular fungi caused considerable improvement of growth and plant P uptake. Greater growth and P uptake of mycorrhizal and non-mycorrhizal plants were achieved when microbe-treated olive cake and rock phosphate were applied to soil compared with all other treatments.
TL;DR: The xlnD gene encoding the 85-kDa β-xylosidase was cloned from Aspergillus nidulans and the deduced primary structure of the protein exhibits considerable similarity to the primary structures of the AsperGillus niger and Trichoderma reesei β-zealousases.
Abstract: The xlnD gene encoding the 85-kDa β-xylosidase was cloned from Aspergillus nidulans The deduced primary structure of the protein exhibits considerable similarity to the primary structures of the Aspergillus niger and Trichoderma reesei β-xylosidases and some similarity to the primary structures of the class 3 β-glucosidases xlnD is regulated at the transcriptional level; it is induced by xylan and d-xylose and is repressed by d-glucose Glucose repression is mediated by the product of the creA gene Although several binding sites for the pH regulatory protein PacC were found in the upstream regulatory region, it was not clear from a Northern analysis whether PacC is involved in transcriptional regulation of xlnD
TL;DR: For both fungi tested in this study, the antifungal activity of these spice plants was not affected by acid treatments at pH values 2, 4, or 6, or salt by treatments at concentrations of 0.1, 0.3, and 0.4 M (P > 0.05).
TL;DR: In general, Aspergillus, Fusarium and Trichoderma species grew most rapidly under the combination of a w and temperature conditions in which they were able to grow, while Penicillium species had the slowest growth rates.
TL;DR: Tea waste, supplemented with minerals, was used as the solid substrate for the synthesis of glucoamylase by a strain of Aspergillus niger NCIM 1248 to choose among different carbon sources and malt extract gave the highest enzyme titre.
TL;DR: In this article, Aspergillus niger was found to produce the highest amount of citric acid (250 g/kg dry matter of corncobs) after 72 h of growth at 30°C in the presence of 3% methanol.
TL;DR: Based on the kinetic constants of hexokinase and glucokinase their relative contribution to in vivo glucose phosphorylation was calculated and found to be strongly dependent on intracellular pH and glucose concentration.
Abstract: The Aspergillus niger hexokinase gene hxkA has been cloned by heterologous hybridisation using the Aspergillus nidulans hexokinase gene as a probe. The DNA sequence of the gene was determined, and the deduced amino acid sequence showed significant similarity to other eukaryotic hexokinase and glucokinase proteins, in particular to those of the budding yeasts. The encoded protein was purified from a multicopy hxkA transformant, and extensively characterised. The hexokinase protein has a molecular mass of 54090, a pI of 4.9 and is a homodimer. D-Glucose, the glucose analogue 2-deoxy-D-glucose, D-fructose, D-mannose and D-glucosamine are phosphorylated by hexokinase, whereas the hexoses D-galactose, L-sorbose, methyl alpha-D-glucoside and the pentoses L-arabinose and D-xylose are not. The enzyme has high affinity for glucose (Km = 0.35 mM at pH 7.5) and for fructose (Km = 2.0 mM at pH 7.5) and is inhibited by ADP. The enzyme is strongly inhibited by physiological concentrations (0.1-0.2 mM) of trehalose 6-phosphate, which may be of importance for in vivo regulation of the enzyme. Inhibition of A. niger hexokinase by trehalose 6-phosphate is competitive towards the sugar substrate (Ki = 0.01 mM). Based on the kinetic constants of hexokinase and glucokinase their relative contribution to in vivo glucose phosphorylation was calculated and found to be strongly dependent on intracellular pH and glucose concentration. At pH 7.5 glucokinase is predominant, whereas at pH 6.5 hexokinase is predominant at glucose concentrations higher than 0.5 mM. Expression of the hexokinase and the glucokinase gene requires active carbon metabolism. Also on carbon sources which are not substrates for hexokinase or glucokinase, clear expression is observed. The hexokinase and glucokinase enzymes are quite stable in vivo. Even in the absence of transcription, active glucokinase and hexokinase remain present in the cells at almost the same level for at least 3-4 h after depletion of the carbon source.
Patent•
24 Mar 1998
TL;DR: In this article, Agrobacterium mediated transformation of moulds comprising species of the fungal sub-divisions Ascomycotina, Basidiomycetina, Deuteromyceto-morphosis, Mastigomycota, and Zygomycotina is described.
Abstract: The invention relates to Agrobacterium mediated transformation of moulds comprising species of the fungal sub-divisions Ascomycotina, Basidiomycotina, Deuteromycotina, Mastigomycotina, and Zygomycotina. Examples demonstrate the transformation of Aspergillus awamori (both protoplasts and conidia), Aspergillus nidulans, Aspergillus niger, Colletovtrichum gloeosporioides, Fusarium solani pisi, Neurospora Crassa, Trichoderma reesei, Pleurotus ostreatus and Agaricus bisporus (all conidia), and Fusarium graminearum (both conidia and rehydrated freeze dried ATCC material). Especially for Aspergillus awamori the transformation frequency is much higher than with conventional mould transformation techniques. It has further been found that not only one expressable gene can be introduced into these moulds, but even multiple copies of such gene, which, moreover, can be targeted e.g. in the chromosomal pyrG locus, as exemplified for A. awamori. These multiple copies can be of a gene encoding a desired, homologous or heterologous, protein.
TL;DR: The use of cellobiose as an activator of the vanillin pathway and the sequential addition of a precursor (ferulic acid) in cultures of selected P. cinnabarinus strains allowed 90 and 300 mg/L of vanillin to be obtained fi om ferulic acid enzymically released from wheat bran and sugar-beet pulp, respectively.
Abstract: The ester-linked ferulic acid of wheat bran and sugar beet pulp can be converted to vanillin using biological transformation. Free ferulic acid from sugar-beet pulp and from wheat bran was almost quantitatively obtained by extensive degradation of the cell-walls using enzyme mixtures complemented with specific ferulic acid esterases. The Basidiomycete Pycnoporus cinnabarinus then converted the released ferulic acid to vanillin. The selection of stable and highly productive strains was achieved using formal genetics. The use of cellobiose as an activator of the vanillin pathway and the sequential addition of a precursor (ferulic acid) in cultures of selected P. cinnabarinus strains, allowed 90 and 300 mg/L of vanillin to be obtained fi om ferulic acid enzymically released from wheat bran and sugar-beet pulp, respectively. This process was adapted into a two-step process involving two filamentous fungi, Aspergillus niger and P. cinnabarinus, with complementary capabilities of transformation.
TL;DR: In vitro results suggest D4E1 is a candidate for transgenic expression in plants to enhance host resistance to fungal infection and more resistant toFungal and plant protease degradation than the natural peptide, cecropin A. flavus.
Abstract: The fungicidal properties of the synthetic peptide D4E1 were studied with nongerminated and germinating conidia of Aspergillus flavus, Aspergillus fumigatus, Aspergillus niger, Fusarium moniliforme...
01 Jan 1998
TL;DR: To ascertain the microbial origin of the commercial preparations, Western blots utilizing monoclonal antibodies specific for Trichoderma reesei CBH I and Aspergillus niger β-d-glucosidase were developed.
Abstract: Commercial cellulase enzymes have been used in the food, detergent, and textile industries, and are potentially effective for processing biomass feedstocks. A survey was undertaken to identify major manufacturers/distributors of cellulases in the USA and to evaluate 13 representative commercial preparations for enzyme activity, protein concentration, and chemical composition. Samples were subjected to activity measurements using filter paper, carboxymethylcellulose, cellobiose, and p-nitrophenyl-b-D-glucopyranoside as substrates. To ascertain the microbial origin of the commercial preparations, Western blots utilizing monoclonal antibodies specific for Trichoderma reesei CBH I and Aspergillus niger b-D-glucosidase were developed. Eleven of the cellulases tested were of T. reesei or T. viride origin and two were from A. niger.
TL;DR: An extracellular beta-glucosidase II (beta-Glu II) has been purified to homogeneity by column chromatography from Aspergillus niger CCRC 31494 and was competitively inhibited by glucose with a K(i) of 5.7 mM.
Abstract: An extracellular β-glucosidase II (β-Glu II) has been purified to homogeneity by column chromatography from Aspergillus niger CCRC 31494. Its molecular mass was estimated to be 360 kDa by gel filtration and 120 kDa by SDS−PAGE. The enzyme has a pI of 4.0 and has optimum activity at pH 4.5 and 60 °C. The β-Glu II was completely inhibited by 5.0 mM Fe2+. Methanol (20%, v/v) activated the enzyme activity at 1.8-fold. Vmax values of 10.2 and 464 units/mg were found for p-nitrophenyl β-d-glucoside (Km = 2.2 mM) and for cellobiose (Km = 15.4 mM). The enzyme was strongly inhibited by substrates, p-nitrophenyl β-d-glucopyranoside in excess of 7.5 mM and cellobiose in excess of 50 mM, and was competitively inhibited by glucose with a Ki of 5.7 mM. Transglucosylation products of cellotriose, methyl β-glucoside and ethyl β-glucoside, were obtained under neutral conditions and in the presence of methanol and ethanol, respectively. Keywords: β-Glucosidase; Aspergillus niger; purification; kinetics; transglucosylation
TL;DR: Glucoamylase in both free and immobilized forms was used to hydrolyze maltose, finding the temperature of 50°C and pH 4.5 were found as the optimum conditions in the aspects of activity and stability.
TL;DR: In this paper, a multi-layer packed-bed reactor was designed and operated in an attempt to understand mass and heat transfer during the fermentation of kumara, a starch-containing root crop.
TL;DR: The feasibility of using thin stillage from a rice-spirit distillery as a substrate for the production of acid protease by Aspergillus niger was evaluated and maximum activity of 200 U ml−1 was achieved in an 8-day fermenter culture under the optimal conditions.
TL;DR: This is the first report on induction of LOX activities in groundnut on treatment with a PGPR strain Bacillus subtilis AF 1, and with crown-rot pathogen, A. niger.
Abstract: Metabolic products of polyunsaturated fatty acids have been variously implicated in control of microbial pathogens. Induced resistance has been shown as one of the mechanisms of biological control by plant growth promoting rhizobacteria (PGPR). This paper reports a significant lipoxygenase (LOX) activity in groundnut seedlings with production of 13-hydroperoxyoctadecadienoic acid (13-HPODE) and 13-hydroperoxyoctadecatrienoic acid (13-HPOTrE) as major products with linoleic acid (LA) and α-linolenic acid (ALA), respectively. Both the hydroperoxides are inhibitory to the growth of Aspergillus niger as measured in micro titer plates. Ours is the first report on induction of LOX activities in groundnut on treatment with a PGPR strain Bacillus subtilis AF 1, and with crown-rot pathogen, A. niger. Treatment with B. subtilis AF 1 enhanced LOX levels in groundnut similarly but earlier to A. niger – treatment. This induction of LOX during activation of growth and pathogen infection was discussed in light of the reported involvement of LOX both in growth and development as well as in plant-pathogen interaction, particularly induced disease resistance.
TL;DR: Correlations were made between CFUs, seed infection, growth rates and niche overlap indices and hyphal interactions to try and link key indicators of competitiveness and dominance by an individual species.