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Aspergillus oryzae

Aspergillus oryzae is a filamentous fungus commonly used in the production of fermented foods and beverages, such as soy sauce, miso, and sake.
It is known for its ability to produce a variety of enzymes, including amylases, proteases, and lipases, which are important in various industrial applications.
A. oryzae has a long history of use in traditional Japanese and Chinese food production, and its safety and efficacy have been well-established.
This versatile organism continues to be an important research subject, with applications in biotechnology, enzymology, and food science.

Most cited protocols related to «Aspergillus oryzae»

The RIPper was used to determine the occurrence and frequency of RIP mutations in sequences that were experimentally and computationally shown to be affected by RIP.These included particular regions (ranging from 478 to 61,000 bp in size) in the genomes of L. maculans (Plissonneau et al., 2016 (link)), N. crassa (Margolin et al., 1998 (link)), Podospora anserina (Hamann, Feller & Osiewacz, 2000 (link)), Colletotrichum cereale (Crouch et al., 2008 (link)), Aspergillus fumigatus (Paris & Latgé, 2001 (link)), Aspergillus oryzae (Montiel, Lee & Archer, 2006 (link)), Magnaporthe grisea (Nakayashiki et al., 1999 (link)) and Chrysoporthe deuterocubensis (Kanzi et al., 2019 (link)). We also used the genomes of N. crassa strain OR74a and T. reesei strain QM6a, which are known to be RIP competent (Selker et al., 2003 (link); Li et al., 2017 (link)). All these sequences were obtained from the NCBI database using accession numbers GCF_000182925.2/, GCA_002006585.1, KT804641.1, AF181821.1, AJ270953.1, DQ663509.1, AF202956.1, DQ327733.1, AB024423.1 and GCF_001513825.1.
The RIPper was used to determine whether this software was capable of identifying large regions affected by RIP in the sequences analyzed. Additionally, for the N. crassa (OR74a) genome assembly, we also generated genome-wide RIP statistics using the “RIP profile” tool. The genomic locations and RIP statistics of putative LRARs were determined using the “calculate LRAR” tool, while the proportion of individual N. crassa chromosomes affected by RIP were calculated using the “RIP sequence” tool. Also, for the T. reesei (QM6a) genome, chromosome-wide changes in RIP index values were compared to changes in GC content, as it was previously shown that centromeric regions are AT-rich due to RIP mutations (Li et al., 2017 (link)).
All chromosome- and genome-wide analyses used sliding windows of 1,000 bp and 500 bp steps. For particular genomic regions, fine-scale analyses were performed using 100 bp sliding windows with a step size of 50 bp. The genomic sequence containing the mating type region of C. deuterocubensis was analyzed using a 1,000 bp window and a 500 bp step size. The RIPper was used to generate graphs for visualizing changes in RIP index values and GC content across the length of the query sequences. This software was also used to generate RIP summary statistics.
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Publication 2019
Aspergillus fumigatus Aspergillus oryzae BP 100 Centromere Chromosomes Chrysoporthe deuterocubensis Colletotrichum cereale Genome Mutation Podospora anserina Pyricularia grisea Strains
DNA from a single spore culture of Diplodia scrobiculata (CMW30223 = CBS139796) was extracted and sequenced using the Illumina: HiSeq genome analyser platform at Inqaba Biotechnology Industries, South Africa. Reads were subjected to the necessary sequence quality analysis and those of less than 30 bases and poor quality regions of reads were discarded. Remaining reads were assembled into a draft genome using CLC Genomic de novo assembler 7.0, with the minimum contig size set to 500 bases (CLCbio, Aarhus, Denmark). Gene predictions were done using AUGUSTUS (Stanke et al. 2006 (link)) based on the gene models for Aspergillus oryzae (http://bioinf.uni-greifswald.de/webaugustus/prediction). Completeness of the genome was evaluated using the Core Eukaryotic Genes Mapping Approach (CEGMA) analysis (Parra et al. 2007 (link)). Contigs of ≥ 500 bases were submitted to the genome database of NCBI.
Publication 2015
Aspergillus oryzae CLCN7 protein, human Diplodia scrobiculata Eukaryota Genes Genome Sequence Analysis Spores
The A. niger strains used were N402 [57] (link) and AB4.1 pyrG[7] (link) or as specified otherwise. Strains were maintained on potato dextrose agar (Oxoid). All AB4.1 cultures were supplemented by 10 mM uridine (Sigma). Cultures were incubated at 28°C until they had conidiated. Spores were harvested into 0.1% (v/v) Tween 20 (Sigma). ΔxlnR and ΔcreA strains are A. niger AB4.1 pyrG containing a deletion of the respective open reading frame. Strains were constructed using the method developed by Scherer and Davis. [58] (link) based on recombination between a plasmid containing the flanking region of the gene of interest and the chromosome. As a selection/counter-selection marker we used the gene coding for the orotidine-5-phosphate decarboxylase [59] (link) (pyrG, from Aspergillus oryzae). After transformation of A. niger, cells were selected for uridine prototrophy, confirming integration of the plasmid into the chromosome. After purification of the transformants, release of the selective pressure for the integrated plasmid was achieved by propagating the clones twice on potato dextrose agar containing 10 mM uridine. Selection for cells that had excised the plasmid from the chromosome was done by plating them on media containing 4 mM of 5-fluoro-orotic acid (Melford) and 1.6 mM uridine. Deletion of creA or xlnR was confirmed by PCR using internal and external oligonucleotide primers and by sequencing around the respective loci.
Liquid batch cultures were inoculated with spores to a final concentration of 106 spores/ml. A. niger was grown in 100 ml of minimal media [all l−1: NaNO3, 6 g; KCl, 0.52 g; MgSO4.7H2O, 0.52 g; KH2PO4, 1.52 g; Na2B4O7.10H2O, 0.008 mg; CuSO4.5H2O, 0.16 mg; FePO4.H2O, 0.16 mg; MnSO4.4H2O, 0.16 mg; NaMoO4.2H2O, 0.16 mg; ZnSO4, 1.6 mg] with the appropriate carbon source added to a final concentration of 1% (w/v) in 250 ml Erlenmeyer flasks at 28°C, shaken at 150 rpm. The standard time-course consisted of growth for 48 h in 1% (w/v) glucose media, after which mycelia were removed by filtration through Miracloth (Merck), washed thoroughly with media devoid of carbon source, and transferred to fresh media containing 1% (w/v) ball-milled wheat straw as sole carbon source. Incubation was continued for 24 h. Glucose was then added exogenously to a final concentration of 1% (w/v) and incubation continued for 5 hours. Figure 1 shows an image of a mycelial clump that was magnified using a Nikon SMZ1000 stereomicroscope and the picture taken using a Nikon 4500 camera.
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Publication 2012
Agar Aspergillus oryzae Batch Cell Culture Techniques Carbon Cells Chromosomes Clone Cells Deletion Mutation ferric phosphate Filtration Genes Glucose Mycelium Oligonucleotide Primers Orotic Acid Orotidine-5'-Phosphate Decarboxylase Plasmids Pressure Recombination, Genetic Solanum tuberosum Spores Strains Sulfate, Magnesium Triticum aestivum Tween 20 Uridine
Three RNA-seq datasets from the industrial T. versatilis were at our disposal (unpublished data) and were prepared from: 1) growth of the mycelium on MM for 48 h (reference condition); 2) transfer of the water-rinsed mycelium to MM with ball-milled wheat straw 1% (w/v) as carbon source and sampling after 24 h; 3) direct addition of glucose at 1% final concentration to the mycelium exposed to wheat straw, and sampling after 5 h. These RNA-seq data were used for the pre-selection of stable genes (fold change (FC) equal to one, see Additional file 2) after calculating the FC as follow: RPKM (Reads Per Kilobase of exon model per Million mapped reads) value in the sample of interest / RPKM in the reference condition, for each gene. Similarly, FC for candidate reference genes were calculated from RNA-seq data publicly available at the NCBI GEO database [48 (link),49 (link)]. To identify the homologues of T. versatilis selected reference genes in the different fungi, a standard protein BLAST (blastp) using the amino-acid sequence from T. versatilis was performed against protein databases, specifying the organism. Each homologous sequence was then used for a reciprocal BLAST against the T. versatilis database in order to confirm the accuracy of the result. The detailed list of locus tags for each gene in every fungus is available in the Additional file 3. For each GOI in these studies, the ratio between the expression in a condition of interest and the expression in the control condition was calculated. Collected datasets were from Trichoderma reesei ([50 (link)], accession #GSE44648), Aspergillus niger ([51 (link)], #GSE33852), Aspergillus flavus ([52 (link),53 (link)], #GSE40202 and #GSE30031), Aspergillus fumigatus (#GSE30579), Aspergillus oryzae ([54 (link)], #GSE18851), Aspergillus nidulans ([55 (link)], #GSE44100), Blumeria graminis ([11 (link)], #GSE43163), Colletotrichum graminicola ([56 (link)], # GSE34632), Colletotrichum higginsianum ([56 (link)], #GSE33683), Fibroporia radiculosa ([57 (link)], #GSE35333), Magnaporthe oryzae ([58 (link)], #GSE30327), Neurospora crassa ([55 (link)], #GSE44100), ([59 (link)], #GSE35227), ([60 (link)], #GSE36719), Pyronema omphalodes ([61 (link)], #GSE41631), Rhizoctonia solani ([12 (link)], #GSE32577), Sordaria macrospora ([62 (link)], #GSE33668). We also accessed unpublished data from Rhizophagus irregularis ([7 (link)], #SRX375378 at NCBI Short Read Archive) and Leptosphaeria maculans (personal communication from T. Rouxel, INRA-Bioger, Thiverval-Grignon, France).
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Publication 2015
Amino Acid Sequence Aspergillus flavus Aspergillus fumigatus Aspergillus nidulans Aspergillus niger Aspergillus oryzae Blumeria graminis Carbon Colletotrichum graminicola Colletotrichum higginsianum Exons Fibroporia radiculosa Genes Genes, Fungal Glucose Hartnup Disease Homologous Sequences Leptosphaeria maculans Mycelium Neurospora crassa Proteins Pyricularia oryzae Pyronema omphalodes Rhizoctonia solani Rhizophagus irregularis RNA-Seq Sordaria macrospora Trichoderma reesei Triticum aestivum
Patients with chronic hepatitis were enrolled at Nagoya City University Hospital and Hokkaido University Hospital. Healthy volunteers as the controls were randomly selected in Nagoya City University Hospital (70 individuals) and AIST (48 individuals). The institutional ethics committees at Nagoya City University Hospital, Hokkaido University Hospital, and AIST approved this study, and informed consent for the use of their clinical specimens was obtained from all participants before the collection. In addition, we used 1,000 serum samples from virus-negative Caucasians as the normal population, which were purchased from Complex Antibodies Inc. (Fort Lauderdale, FL) and collected under IRB-approved collection protocols. Fibrosis was graded in the patients according to the histological activity index (HAI) using biopsy or surgical specimens. Biopsy specimens were classified as follows: F0, no fibrosis; F1, portal fibrosis without septa; F2, few septa; F3, numerous septa without cirrhosis; and F4, cirrhosis. The three diagnostic targets in this study were defined as significant fibrosis: F2+F3+F4; severe fibrosis: F3+F4; and cirrhosis: F4. Hepatic inflammation was also assessed according to the HAI, as follows: A0, no activity; A1, mild activity; A2, moderate activity; and A3, severe activity. Cirrhosis was confirmed by ultrasonography (coarse liver architecture, nodular liver surface, and blunt liver edges), evidence of hypersplenism (splenomegaly on ultrasonography) and/or a platelet count of < 100,000/mm3. Virological responses during PEG-interferon-α and ribavirin therapy were defined as follows5 (link): SVR, absence of HCV RNA from serum 24 weeks following discontinuation of therapy; nonresponder, failure to clear HCV RNA from serum after 24 weeks of therapy; relapse, reappearance of HCV RNA in serum after therapy was discontinued. For all patients, age and sex were recorded and serum levels of the following were analyzed: aspartate aminotransferase (AST), alanine aminotransferase (ALT), γ-glutamyltransferase (GGT), total bilirubin, albumin, cholinesterase, total cholesterol, platelet count (PLT), hyaluronic acid (HA). The FIB-4 index was calculated as follows: [age (years) × AST (U/L)]/[platelets (109/L) × ALT (U/L)1/2]26 (link). Fibrosis-specific glyco-alteration of α1-acid glycoprotein was determined by lectin–antibody sandwich immunoassays with a combination of three lectins (Datura stramonium agglutinin (DSA), Maackia amurensis leukoagglutinin (MAL), and Aspergillus oryzae lectin (AOL))16 (link). All assays used an automated chemiluminescence enzyme immunoassay system (HISCL-2000i; Sysmex Co., Kobe, Japan)18 (link).
Publication 2013
Acids Agglutinins Albumins Antibodies Aspartate Transaminase Aspergillus oryzae Bilirubin Biological Assay Biopsy Blood Platelets Butyrylcholinesterase Caucasoid Races Chemiluminescent Assays Cholesterol D-Alanine Transaminase Enzymes Fibrosis Glycoproteins Healthy Volunteers Hepatitis, Chronic Hyaluronic acid Hypersplenism Immunoassay Immunoglobulins Inflammation Institutional Ethics Committees Interferon-alpha Jimsonweed Lectin Liver Liver Cirrhosis Maackia amurensis leukoagglutinin Operative Surgical Procedures Patients Platelet Counts, Blood Relapse Ribavirin Serum Tests, Diagnostic Therapeutics Ultrasonography Virus

Most recents protocols related to «Aspergillus oryzae»

For in vitro digestion, the ground chicken muscles were
vacuum-packed and cooked at 80°C to reach a core temperature of
75°C, followed by cooling to 25°C. Cooked samples were chopped to
simulate mastication.
The elderly in vitro digestion model herein was designed based
on previous studies by Hernández-Olivas
et al. (2020)
and Minekus et al.
(2014)
. All the digestive enzymes that were used herein were
purchased from Sigma-Aldrich (St. Louis, MO, USA). The simulated salivary fluid
(pH 7.0), gastric fluid (pH 6.0), and duodenal fluid (pH 7.0) contained 75 U/mL
α-amylase from Aspergillus oryzae (EC 3.2.1.1), 1,500
U/mL pepsin from Porcine mucosa (EC 3.4.23.1), 50 U/mL trypsin
(EC 3.4.21.4) and 12.5 U/mL chymotrypsin (EC 3.4.21.1) from bovine pancreas,
1,000 U/mL pancreatic lipase from porcine pancreas (EC 3.1.1.3), and 5 mM
porcine bile extract (EC 232-369-0). Digestive fluid was mixed with the digesta
from the previous compartment at 50:50 (vol/vol) during digestion. Each
digestion was conducted for 120 min at 37°C and a rotational speed of 100
rpm, except for oral digestion, which was conducted for 2 min. All digesta
samples were stored at −70°C until analysis, immediately after
digestion. Control samples were prepared for digestion under the same conditions
through addition of distilled water instead of meat samples to exclude protein
content from the digestive enzymes.
Herein, the size fractionation of the digesta was conducted to determine protein
digestibility after in vitro digestion. After sequential
filtration using a centrifugal filter with molecular weight cut-offs of 10 and 3
kDa (Amicon Ultra-15, Millipore, Billerica, MA, USA) according to the
manufacturer’s protocol, the protein content of the filtrate and whole
digesta was measured using the Kjeldahl method to represent the amount of
protein digested under 3 kDa. Protein digestibility was calculated using the
following Eq. (1):
Publication 2023
Aged Amylase Aspergillus oryzae Bile Bos taurus Chewing Chickens Chymotrypsin Digestion Duodenum Enzymes Fractionation, Chemical Lipase Meat Mucous Membrane Muscle Tissue Pancreas Pepsin A Pigs Proteins Stomach Trypsin
In this study, the fully sequenced Aspergillus sp. Aspergillus niger ATTC 1015 [38 ], Aspergillus terreus NIH 2624 [39 ], and Aspergillus oryzae RIB40 [40 ] were used. These strains were provided by Matthias Brock (University of Nottingham, UK).
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Publication 2023
Aspergillus Aspergillus niger Aspergillus oryzae Aspergillus terreus Strains
The ingredient and nutrient composition of the positive control and basal diets are presented in Table 1. The positive control diet was adequate in energy and nutrients, whereas the basal diet was deficient in Ca and P but supplemented with 1,000 FYT phytase/kg feed (HiPhorius, DSM Nutritional Products, Switzerland). The phytase was encoded by a 6-phytase gene from Citrobacter braakii and expressed in a strain of Aspergillus oryzae. The rice hulls in the basal diet were replaced by 0.05%, 0.25%, 0.45%, 0.65%, or 0.85% limestone to establish five experimental diets corresponding to total Ca/total P ratios of 0.55, 0.73, 0.90, 1.07, and 1.24. Titanium dioxide was included at 3 g/kg feed as an indigestible marker to enable the measurement of apparent total tract digestibility (ATTD) of Ca and P in all diets. All the diets were pelleted with a conditioning temperature at 75°C.
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Publication 2023
Aspergillus oryzae Citrobacter braakii Diet Genes Limestone Nutrients Oryza sativa Phytase Strains titanium dioxide

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Publication 2023
alum, potassium Anesthesia Animals Animals, Laboratory Aspergillus oryzae Eosinophil IGFBP-2 protein, human Injections, Intraperitoneal Males Mesenchyma Mice, House Mice, Inbred BALB C Mucous Membrane Nose Ovalbumin PF 573228 Phenotype Specific Pathogen Free TGF-beta1
Escherichia coli DH5α
was used for cloning following standard recombinant DNA techniques. E. coli BL21(DE3) was used for expression of protein. Aspergillus oryzae NSAR1 (niaD, sC, ΔargB, adeA) and A. oryzae NSPlD1 (niaD, sC, ΔpryG, ΔligD) were used as the host for fungal expression. Discosia sp. batta1 was used for genomic DNA preparation
and draft genome sequencing. Pestalotiopsis fici MAFF
237190, P. microspora NBRC 30316, and Aspergillus
candidus
NBRC 8816 were used for genomic DNA preparation.
Publication 2023
Aspergillus oryzae Escherichia coli Genome Microspora Pestalotiopsis fici Proteins Recombinant DNA

Top products related to «Aspergillus oryzae»

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α-amylase from Aspergillus oryzae is an enzyme that catalyzes the hydrolysis of starch, glycogen, and related polysaccharides. It is derived from the fungus Aspergillus oryzae.
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α-amylase is an enzyme commonly used in laboratory settings. It functions by catalyzing the hydrolysis of starch, glycogen, and related polysaccharides into smaller carbohydrate units such as maltose and glucose.
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β-galactosidase from Aspergillus oryzae is an enzyme that catalyzes the hydrolysis of β-galactosides, such as lactose, into monosaccharides. It is derived from the fungus Aspergillus oryzae.
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DPPH is a chemical compound used as a free radical scavenger in various analytical techniques. It is commonly used to assess the antioxidant activity of substances. The core function of DPPH is to serve as a stable free radical that can be reduced, resulting in a color change that can be measured spectrophotometrically.
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Aspergillus oryzae is a filamentous fungus commonly used in the production of various fermented foods and beverages. It is a key ingredient in the fermentation processes for soy sauce, miso, and sake. This fungus is known for its ability to produce a variety of enzymes that can facilitate the breakdown of complex carbohydrates and proteins.
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Flavourzyme is a food-grade enzyme preparation containing a complex of proteolytic enzymes from Aspergillus oryzae. It is used to hydrolyze proteins, producing peptides and amino acids that can enhance the flavor profile of food products.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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The Folin-Ciocalteu reagent is a colorimetric reagent used for the quantitative determination of phenolic compounds. It is a mixture of phosphomolybdic and phosphotungstic acid complexes that undergo a color change when reduced by phenolic compounds.
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Gallic acid is a naturally occurring organic compound that can be used as a laboratory reagent. It is a white to light tan crystalline solid with the chemical formula C6H2(OH)3COOH. Gallic acid is commonly used in various analytical and research applications.
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Acetonitrile is a colorless, volatile, flammable liquid. It is a commonly used solvent in various analytical and chemical applications, including liquid chromatography, gas chromatography, and other laboratory procedures. Acetonitrile is known for its high polarity and ability to dissolve a wide range of organic compounds.

More about "Aspergillus oryzae"

Aspergillus oryzae, commonly known as the 'koji mold,' is a versatile filamentous fungus that has been widely utilized in the production of various fermented foods and beverages.
This versatile microorganism is renowned for its ability to produce a diverse array of enzymes, including amylases, proteases, and lipases, which play crucial roles in numerous industrial applications.
With its long-standing history in traditional Japanese and Chinese cuisine, A. oryzae has become an integral part of the food production landscape.
Its safety and efficacy have been extensively studied and well-established, making it a trusted and reliable organism for various culinary and industrial purposes.
The α-amylase enzyme produced by A. oryzae is a key component in the production of soy sauce, miso, and sake, where it helps to break down starches into simpler sugars.
Similarly, the β-galactosidase enzyme from A. oryzae is utilized in the production of lactose-free dairy products, catering to the needs of lactose-intolerant individuals.
Beyond its applications in food production, A. oryzae has also found use in the field of biotechnology.
Researchers continue to explore its potential in areas such as enzymology, where the organism's ability to produce a wide range of enzymes is of great interest.
Additionally, A. oryzae-derived enzymes, such as Flavourzyme, have been used in the pharmaceutical and cosmetic industries for their diverse functionalities.
In the realm of analytical chemistry, A. oryzae-derived enzymes have been employed in the assessment of various compounds.
For instance, the DPPH assay, which measures antioxidant activity, often utilizes A. oryzae-derived enzymes to facilitate the reaction and enhance the accuracy of the measurements.
As the scientific community delves deeper into the study of A. oryzae, innovative platforms like PubCompare.ai have emerged to streamline the research process.
This AI-driven platform helps researchers locate relevant protocols from literature, preprints, and patents, while also providing AI-driven comparisons to identify the best protocols and products.
By leveraging these tools, researchers can enhance the reproducibility and accuracy of their A. oryzae studies, ultimately advancing our understanding of this remarkable fungus and its multifaceted applications.
In conclusion, Aspergillus oryzae, with its rich history, diverse enzyme production capabilities, and versatile applications, continues to be a subject of intense research and interest in the fields of food science, biotechnology, and beyond.
The availability of innovative tools like PubCompare.ai further facilitates the exploration and optimization of A. oryzae-related studies, paving the way for new discoveries and advancements in this captivating area of scientific inquiry.