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Ochratoxin A

Ochratoxin A is a mycotoxin produced by certain Aspergillus and Penicillium fungi.
It is a potent nephrotoxin and carcinogen, posing a significant health risk to humans and animals.
Ochratoxin A research is crucial for understanding its mechanisms of toxicity, developing detection methods, and establishing safety guidelines.
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Most cited protocols related to «Ochratoxin A»

Comprehensive Impurity Assessment for Additives

Cited 26 times

The applicant should identify and quantify microbiological and chemical (including residual solvents) impurities, substances with toxic or other undesirable properties that are not intentionally added and do not contribute to the activity of the additive. The applicant should describe which impurities are monitored on a routine basis, the frequency of testing and the action limits set for each monitored impurity. Action limits for contaminants and impurities should respect existing legislation (e.g. Directive 2002/32/EC5 or specifications from European Union (EU) food additive authorisations) and recommendations from internationally recognised sources when these are available (e.g. the Joint FAO/WHO Expert Committee on Food Additives (JECFA) specifications for enzymes; Commission recommendation on the presence of deoxynivalenol, zearalenone, ochratoxin A, T‐2 and HT‐2 and fumonisins in products intended for animal feeding; maximum levels for residual solvents used in veterinary drugs (Veterinary International Conference on Harmonisation (VICH) guidance GL18 (EMA, 2010 )).
Analytical data on the impurities should be provided for at least three production batches, produced within the last 5 years. If an application for an additive covers different manufacturing methods or origins/sources, data from at least three batches should be provided for each. Certificates of analysis indicating the analytical values should be provided; statements of compliance alone are not considered sufficient. The limits of detection (LOD) and quantification (LOQ) of the analytical methods should be given.
Any substance produced via fermentation should be free of antimicrobial activities relevant to the use of antibiotics in humans or animals (see Section 2.2.2.2). In addition, the absence of production organisms in the additive should be confirmed. For fermentation products in which the production strain has genes conferring antibiotic resistance and for products produced with genetically modified microorganisms (GMMs), the absence of the DNA from the production strain in the final product should be demonstrated. For details on how to perform this assessment, please refer to the Guidance on the characterisation of microorganisms used as feed additives or as production organisms.
As a guide, the following should be considered as minimum requirements:

for microorganisms: microbiological contamination (at least Salmonella, Enterobacteriaceae, total yeasts and filamentous fungi, Bacillus cereus for bacilli) and depending on the fermentation media and excipients, mycotoxins,6 lead, mercury, cadmium and arsenic;

for fermentation products (not containing microorganisms as active agents): in addition to the above, the extent to which spent growth medium is incorporated into the final product should also be indicated. For products consisting of or produced by Gram‐negative bacteria, levels of lipopolysaccharides (LPS) should be analysed in the final product. If the production strain is known to be able to produce toxic compounds, the analysis should cover such compounds (see Guidance on the characterisation of microorganisms used as feed additives or as production organisms7);

for plant‐derived substances: microbiological and botanical contamination, mycotoxins, dioxins and the sum of dioxins and dioxin‐like polychlorinated biphenyls (PCBs), pesticides,8 lead, mercury, cadmium and arsenic;

for animal‐derived substances: microbiological contamination, lead, mercury, cadmium and arsenic;

for mineral substances, including compounds of trace elements: lead, mercury, cadmium, arsenic and fluorine, dioxins and the sum of dioxins and dioxin‐like PCBs;

for products produced by chemical synthesis and processes: all chemicals used in the synthetic processes and any intermediate products remaining in the final product shall be identified and their concentrations given.

Rychen G., Aquilina G., Azimonti G., Bampidis V., Bastos M.D., Bories G., Chesson A., Cocconcelli P.S., Flachowsky G., Gropp J., Kolar B., Kouba M., López‐Alonso M., López Puente S., Mantovani A., Mayo B., Ramos F., Saarela M., Villa R.E., Wallace R.J., Wester P., Anguita M., Galobart J, & Innocenti M.L. (2017). Guidance on the identity, characterisation and conditions of use of feed additives. EFSA Journal, 15(10), e05023.

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Publication 2017

Morphological and Molecular Characterization of Aspergillus Section Usti

Cited 13 times

Morphological examination. The strains examined are listed in
Table 1. Both clinical and
environmental strains were grown as 3-point inoculations on Czapek yeast agar
(CYA), malt extract agar (MEA), creatine agar (CREA) and yeast extract sucrose
agar (YES) at 25 °C, and on CYA at 37 °C for 7 d (medium compositions
according to Samson et al. 2004). For micro morphological examination light microscopy
(Olympus BH2 and Zeiss Axioskop 2 Plus) was employed.

Table 1.

Isolates in Aspergillus section Usti and related species
examined in this study.

Species	Strain No.	Source
A. calidoustus	CBS 112452	Indoor air, Germany
A. calidoustus	CBS 113228	ATCC 38849; IBT 13091
A. calidoustus	CBS 114380	Wooden construction material, Finland
A. calidoustus	CBS 121601^T	Bronchoalveolar lavage fluid, proven invasive aspergillosis, Nijmegen, The Netherlands†
A. calidoustus	CBS 121602	Bronchial secretion, proven invasive aspergillosis, Nijmegen, The Netherlands†
A. calidoustus	CBS 121589	Autopsy lung tissue sample, proven invasive aspergillosis, Nijmegen, The Netherlands†
A. calidoustus	CBS 121603	Elevator shaft in hospital, Nijmegen, The Netherlands
A. calidoustus	CBS 121604	Patient room, Nijmegen, The Netherlands
A. calidoustus	CBS 121605	Laboratory, Nijmegen, The Netherlands
A. calidoustus	CBS 121606	Sputum, Nijmegen, The Netherlands
A. calidoustus	CBS 121607	Feces, Nijmegen, The Netherlands
A. calidoustus	CBS 121608	Bronchoalveolar lavage, Nijmegen, The Netherlands
A. calidoustus	7843	Pasteur Institute, Paris, France
A. calidoustus	8623	Oslo, Norway
A. calidoustus	9331	Mouth wash, Nijmegen, The Netherlands
A. calidoustus	9371	Mouth wash, Nijmegen, The Netherlands
A. calidoustus	9420	Bronchial secretion, Nijmegen, The Netherlands
A. calidoustus	9692	Hospital ward, Nijmegen, The Netherlands
A. calidoustus	V02-46	Tongue swab, Nijmegen, The Netherlands
A. calidoustus	V07-21	Bronchial secretion, Nijmegen, The Netherlands
A. calidoustus	V17-43	Bronchial secretion, Nijmegen, The Netherlands
A. calidoustus	V22-60	Skin biopsy, Nijmegen, The Netherlands
A. calidoustus	CBS 121609	Post-cataract surgery endophthalmitis, Turkey
A. calidoustus	907	Post-cataract surgery endophthalmitis, Turkey
A. calidoustus	908	Post-cataract surgery endophthalmitis, Turkey
A. calidoustus	64	Post-cataract surgery endophthalmitis, Turkey
A. calidoustus	67	Post-cataract surgery endophthalmitis, Turkey
A. calidoustus	CBS 121610	Post-cataract surgery endophthalmitis, Turkey
A. calidoustus	351	Osteorickets
A. calidoustus	482	Post-cataract surgery endophthalmitis
A. calidoustus	CBS 121611	Patient 4, Washington, U.S.A.
A. calidoustus	CBS 121616	Environmental, Washington, U.S.A.
A. calidoustus	FH 165	Patient 5b, Washington, U.S.A.
A. calidoustus	CBS 121614	Patient 5a, Washington, U.S.A.
A. calidoustus	CBS 121615	Patient 6, Washington, U.S.A.
A. calidoustus	CBS 121613	Patient 2, Washington, U.S.A.
A. calidoustus	CBS 121612	Patient 1, Washington, U.S.A.
A. calidoustus	FH 91	Patient 1a, Washington, U.S.A.
A. calidoustus	NRRL 26162	Culture contaminant, Peoria, U.S.A.
A. calidoustus	NRRL 281	Thom 5634
A. calidoustus	NRRL 277	Thom 5698.754, Green rubber
A. granulosus	CBS 588.65^T	Soil, Fayetteville, Arkansas, U.S.A.
A. granulosus	CBS 119.58	Soil, Texas, U.S.A.
A. granulosus	IBT 23478 = WB 1932 = IMI 017278iii = CBS 588.65	Soil, Fayetteville, Arkansas, U.S.A.
A. insuetus	CBS 107.25^T	South Africa
A. insuetus	CBS 119.27	Unknown
A. insuetus	CBS 102278	Subcutaneous infection left forearm and hand of 77-year-old woman
A. keveii	CBS 209.92	Soil, La Palma, Spain
A. keveii	CBS 561.65	Soil, Panama
A. keveii	IBT 10524 = CBS 113227 = NRRL 1254	Soil, Panama
A. keveii	IBT 16751 = DMG 153	Galápagos Islands, Ecuador, D.P. Mahoney
A. pseudodeflectus	CBS 596.65	Sugar, U.S.A., Louisiana
A. pseudodeflectus	CBS 756.74^T	Desert soil, Egypt, Western Desert
A. puniceus	CBS 122.33	Unknown
A. puniceus	9377	Mouth wash, Nijmegen, Netherlands
A. puniceus	V41-02	Faeces, Nijmegen, Netherlands
A. puniceus	NRRL 29173	Indoor air, Saskatoon, Canada
A. puniceus	CBS 495.65^T	Soil, Zarcero Costa Rica
A. puniceus	CBS 128.62	Soil, Louisiana, U.S.A.
A. ustus	CBS 116057	Antique tapestries, Krakow, Poland
A. ustus	CBS 114901	Carpet, The Netherlands
A. ustus	CBS 261.67^T	Culture contaminant, U.S.A.
A. ustus	CBS 133.55	Textile buried in soil, Netherlands
A. ustus	CBS 239.90	Man, biopsy of brain tumor, Netherlands
A. ustus	CBS 113233	IBT 14495
A. ustus	CBS 113232	IBT 14932
A. ustus	NRRL 285	Soil, Iowa, U.S.A.
A. ustus	NRRL 280	Bat dung, Cuba
A. ustus	NRRL 1609	Bat dung, Cuba
A. ustus	NRRL 29172	Indoor air, Edmonton, Canada
E. heterothallica	CBS 489.65^T	soil, Costa Rica
E. heterothallica	CBS 488.65	soil, Costa Rica

†

These samples were taken from the same patient
(Verweij et al. 1999)

Extrolite analysis. Extrolites were analysed by HPLC using
alkylphenone retention indices and diode array UV-VIS detection as described
by Frisvad & Thrane (1987 (link)),
with minor modifications as described by Smedsgaard
(1997 (link)). Standards of
ochratoxin A and B, aflavinine, asperazine, austamide, austdiol, kotanin and
other extrolites from the collection at Biocentrum-DTU were used to compare
with the extrolites from the species under study.
Isolation and analysis of nucleic acids. The cultures used for the
molecular studies were grown on malt peptone (MP) broth using 10 % (v/v) of
malt extract (Brix 10) and 0.1 % (w/v) bacto peptone (Difco), 2 mL of medium
in 15 mL tubes. The cultures were incubated at 25 °C for 7 d. DNA was
extracted from the cells using the Masterpure™ yeast DNA purification
kit (Epicentre Biotechnol.) according to the instructions of the manufacturer.
Fragments containing the ITS region were amplified using primers ITS1 and ITS4
as described previously (White et
al. 1990). Amplification of part of the β-tubulin gene
was performed using the primers Bt2a and Bt2b
(Glass 1995 (link)). Amplifications
of the partial calmodulin and actin genes were set up as described previously
(Hong et al. 2005 (link)).
Sequence analysis was performed with the Big Dye Terminator Cycle Sequencing
Ready Reaction Kit for both strands, and the sequences were aligned with the
MT Navigator software (Applied Biosystems). All the sequencing reactions were
purified by gel filtration through Sephadex G-50 (Amersham Pharmacia Biotech,
Piscataway, NJ) equilibrated in double-distilled water and analyzed on the ABI
PRISM 310 Genetic Analyzer (Applied Biosystems).
Data analysis. The sequence data was optimised using the software
package Seqman from DNAStar Inc. Sequence alignments were performed by using
CLUSTAL-X (Thompson et al. 1997) and improved manually. The
neighbour-joining (NJ) method was used for the phylogenetic analysis. For NJ
analysis, the data were first analysed using the Tamura-Nei parameter distance
calculation model with gamma-distributed substitution rates
(Tamura & Nei 1993 (link)), which
were then used to construct the NJ tree with MEGA v. 3.1
(Kumar et al. 2004 (link)).
To determine the support for each clade, a bootstrap analysis was performed
with 1000 replications.
For parsimony analysis, the PAUP v. 4.0 software was used
(Swofford 2000 ). Alignment
gaps were treated as a fifth character state and all characters were unordered
and of equal weight. Maximum parsimony analysis was performed for all data
sets using the heuristic search option with 100 random taxa additions and tree
bisection and reconstruction (TBR) as the branch-swapping algorithm. Branches
of zero length were collapsed and all multiple, equally parsimonious trees
were saved. The robustness of the trees obtained was evaluated by 1000
bootstrap replications (Hillis & Bull
1993). An Aspergillus versicolor isolate was used as
outgroup in these experiments. Unique sequences of the ITS, actin, calmodulin
and β-tubulin gene sequences have been deposited in the GenBank under
accession numbers EU076344-EU76377.

Houbraken J., Due M., Varga J., Meijer M., Frisvad J.C, & Samson R.A. (2007). Polyphasic taxonomy of Aspergillus section Usti. Studies in Mycology, 59, 107-128.

Publication 2007

Actins Agar Arecaceae asperazine Aspergillosis Aspergillus Aspergillus versicolor austamide austdiol Autopsy Bacto-peptone Biopsy Brain Neoplasms Bronchi Bronchoalveolar Lavage Bronchoalveolar Lavage Fluid Calmodulin Carbohydrates Cataract Extraction Cattle Character Creatine DNA Replication Endophthalmitis Feces Forearm Gamma Rays Gel Chromatography Gene Amplification Genes High-Performance Liquid Chromatographies Infection isolation kotanin Light Microscopy Lung Mouthwashes Nucleic Acids ochratoxin A Oligonucleotide Primers Patients Peptones prisma Reconstructive Surgical Procedures Retention (Psychology) Rubber secretion sephadex G 50 Sequence Alignment Skin Sputum Strains Sucrose Tissues Tongue Trees Tubulin Vaccination Woman Yeast, Dried

Gut Microbiome Profiling by 16S rRNA Sequencing

Cited 11 times

DNA was extracted from the feces and liver using the E.Z.N.A.® soil DNA Kit (Omega Bio-tek, Norcross, GA, USA) according to the protocol for isolation of DNA. Illumina MiSeq sequencing and general data analyses were performed by a commercial company (Majorbio Bio-Pharm Technology, Shanghai, China). Because of initially low bacterial DNA concentrations in some samples, a nested PCR was applied to increase specificity and amplicon yield [73 (link), 74 (link)]. The V3–V4 hypervariable regions of the bacteria 16S rRNA gene were amplified with primers 338F (5′-ACT CCT ACG GGA GGC AGC AG-3′) and 806R (5′-GGA CTA CHV GGG TWT CTA AT-3′) by thermocycler PCR system (GeneAmp 9700, ABI, USA). The PCR reactions were conducted using the following program: 3 min of denaturation at 95 °C, 27 cycles of 30 s at 95 °C, 30s for annealing at 55 °C, 45 s for elongation at 72 °C, and a final extension at 72 °C for 10 min. PCR reactions were performed in triplicate 20 μL mixture containing 4 μL of 5 × FastPfu Buffer, 2 μL of 2.5 mM dNTPs, 0.8 μL of each primer (5 μM), 0.4 μL of FastPfu Polymerase, and 10 ng of template DNA. The resulted PCR products were extracted from a 2% agarose gel and further purified using the AxyPrep DNA Gel Extraction Kit (Axygen Biosciences, Union City, CA, USA) and quantified using QuantiFluor™-ST (Promega, USA) according to the manufacturer’s protocol. Purified amplicons were pooled in equimolar and paired-end sequenced (2 × 300) on an Illumina MiSeq platform (Illumina, San Diego, USA) according to the standard protocols by Majorbio Bio-Pharm Technology Co. Ltd. (Shanghai, China). Raw fastq files were demultiplexed, quality-filtered by Trimmomatic, and merged by FLASH with the following criteria: (a) The reads were truncated at any site receiving an average quality score < 20 over a 50-bp sliding window. (ii) Primers were exactly matched allowing two nucleotide mismatching, and reads containing ambiguous bases were removed. (iii) Sequences whose overlap longer than 10 bp were merged according to their overlap sequence. Operational taxonomic units (OTUs) were clustered with 97% similarity [75 (link)] cutoff using UPARSE (version 7.1 http://drive5.com/uparse/) and chimeric sequences were identified and removed using UCHIME. The taxonomy of each 16S rRNA gene sequence was analyzed by RDP Classifier algorithm (http://rdp.cme.msu.edu/) against the Silva (SSU123) 16S rRNA database using a confidence threshold of 70%.

Wang W., Zhai S., Xia Y., Wang H., Ruan D., Zhou T., Zhu Y., Zhang H., Zhang M., Ye H., Ren W, & Yang L. (2019). Ochratoxin A induces liver inflammation: involvement of intestinal microbiota. Microbiome, 7, 151.

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Publication 2019

Quantifying Mycotoxin-Albumin Interactions

Cited 8 times

Fluorescent measurements were performed employing a Hitachi F-4500 fluorescence spectrophotometer (Tokyo, Japan). In order to mimic extracellular physiological conditions, mycotoxin-albumin interactions were studied in PBS (pH 7.4). All measurements were carried out at 25 °C in the presence of air.
Complex formation of 2′R-OTA with HSA was examined applying the Stern-Volmer equation:

\frac{I_{0}}{I} = 1 + K_{S V} \times [Q]

where I and I₀ denote the fluorescence intensities of HSA in the absence and presence of 2′R-OTA, respectively. K_SV (with the unit of L/mol) is the Stern-Volmer quenching constant and [Q] is the molar concentration of the quencher (2′R-OTA). In order to eliminate the inner-filter effect, UV-Vis spectrum of 2′R-OTA was recorded using a Specord Plus 210 spectrophotometer (Analytic Jena AG, Jena, Germany), and fluorescence intensities were corrected applying the following equation [21 (link)]:

I_{cor} = I_{obs} \times e^{(A_{ex} + A_{em}) / 2}

where I_cor and I_obs are the corrected and observed fluorescence emission intensities, respectively; while A_ex and A_em are the absorption values of 2′R-OTA at 295 and 340 nm, respectively.
Overall and stepwise binding constants were calculated by non-linear fitting using the fluorescence emission data obtained for all the performed experiments (quenching of the fluorescence of HSA by 2′R-OTA, fluorescence enhancement induced by the energy transfer between HSA and 2′R-OTA, and fluorescence enhancement of 2′R-OTA by HSA) with the Hyperquad2006 program package. To calculate the stability constants associated with the complex formation between HSA and 2′R-OTA, the following equations are implemented in the Hyperquad code [18 (link),22 (link)]:

p HSA + q OTA \leftrightarrow {HSA}_{p} {OTA}_{q}

β_{pq} = \frac{[{HSA}_{p} {OTA}_{q}]}{{[HSA]}^{p} {[OTA]}^{q}}

where p and q are the coefficients which indicate the stoichiometry associated with the possible equilibrium in the solution. In the Hyperquad2006 computer fitting program, all equilibrium constants are defined as overall binding constants.

HSA + OTA \leftrightarrow HSA OTA β_{1} = \frac{[HSAOTA]}{[HSA] [OTA]}

HSA + q OTA \leftrightarrow {HSA OTA}_{q} β_{q} = \frac{[{HSA OTA}_{q}]}{[HSA] {[OTA]}^{q}}

The relationship between the overall binding constants and the stepwise binding constants calculated by the Hyperquad is the following.

β_{1} = K_{1}; β_{q} = K_{1} \times K_{2} \dots \times K_{q}

The stoichiometry and binding constant of 2′R-OTA-HSA complex were determined by the model associated with the lowest standard deviation.
Fluorescence anisotropy (r) data were determined using the following equation:

r = \frac{(I_{VV} - G \times I_{VH})}{(I_{VV} + 2 \times {G \times I}_{VH})}

where I_VV and I_VH are fluorescence emission intensities measured in vertical position of polarizer at pre-sample site and at vertical and horizontal position of the post-sample polarizer, respectively, while G is the instrumental factor. Considering the additive behavior of anisotropy, the following equation can be described:

r = f_{f} \times r_{f} + f_{b} \times r_{b}

where f_f and f_b are the free and HSA-bound fractions of 2′R-OTA in the solution, respectively, while r_f and r_b are the anisotropies of free and HSA-bound 2′R-OTA, respectively. The free HSA-bound fractions of 2′R-OTA can be described from the rearrangement of Equation (9).

f_{f} = \frac{(r - r_{b})}{(r_{f} - r_{b})}

f_{b} = 1 - f_{f}

Furthermore, assuming 1:1 stoichiometry of complex formation as well as through the application of Equations (10) and (11), the binding constant (K) can be expressed with the following equation:

K = \frac{f_{b} / θ}{f_{f} \times [HSA]}

where [HSA] is the albumin concentration, and θ is the change in quantum yield (I_b and I_f are the fluorescence emission intensities of HSA-bound and free 2′R-OTA, respectively).

θ = \frac{I_{b}}{I_{f}}

Sueck F., Poór M., Faisal Z., Gertzen C.G., Cramer B., Lemli B., Kunsági-Máté S., Gohlke H, & Humpf H.U. (2018). Interaction of Ochratoxin A and Its Thermal Degradation Product 2′R-Ochratoxin A with Human Serum Albumin. Toxins, 10(7), 256.

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Publication 2018

Identification and Characterization of Fungal NRPSs

Cited 5 times

A set of fungal NRPSs with known chemical products was extracted from the NCBI database (Additional file 10), aligned using MUSCLE [102 (link)] with the 13 NRPSs identified previously in the Dothideomycete, C. heterostrophus C4 strain [10 (link)], and used to construct an initial HMMER model of fungal NRPS A domains using HMMER 2.0 http://hmmer.janelia.org (Additional file 11). This model was tested for specificity and ability to identify NRPSs proteins in fungal genomes for which NRPSs have been well characterized (e.g., C. heterostrophus and Gibberella zeae/Fusarium graminearum) and was found to correctly identify all known NRPSs in the genomes of these species as top hits. Protein datasets of a taxonomically representative sample of fungal genomes (Additional file 12) were downloaded and searched using both a local and global version of the fungal NRPS HMMER model. Proteins that were hit by our A domain model with an e-value less than 1 were considered possible NRPSs. A similar search strategy was employed on the nucleotide genome sequences using GENEWISE [103 (link)] and the same HMMER model to identify candidates that might have been missed or mis-annotated by automated gene calling programs. This approach did not identify any additional genes but did identify missed domains and also revealed a number of split gene annotations in the automated protein calls which we have reannotated. These included BC1G09040_09041.1, BC1G07441_07442.1, and FGSG11659.3 and FGSG11630.3 which we conclude represents a single gene corresponding to the MIPS and version 2 broad annotation (FG_00042.1), (Additional file 2).
For each fungal genome, A domains from all candidate NRPSs were aligned, using MUSCLE [102 (link)], with A domains from the 12 NRPSs previously identified from C. heterostrophus [10 (link)] (Additional file 1) and with A domains from related adenylating enzymes in the AMP-binding family (PFAM PF00501) [e.g., acyl CoA ligases (ACoAL), acetyl CoA synthetases (ACoAS), acyl AMP ligases (AAL), homologs of C. heterostrophus CPS1 (CPS1) [54 (link)], long chain fatty acid ligases (LCFAL), and homologs of Ochratoxin synthetase (OCHRA) [104 (link)] (Additional file 5). An initial phylogenetic analysis was conducted using the WAG+G model in PhyML to define a set of candidate NRPS proteins for each genome. Proteins from each genome grouping within a monophyletic group containing A domains of the known C. heterostrophus NRPS proteins and separated from the outgroup proteins with consistently high bootstrap support (>90), were retained in the dataset as candidate NRPSs or NRPS-like proteins. We chose to use individual A domains, rather than to include only proteins containing a complete A-T-C module as has been used in previous studies [105 (link)] because the latter would miss several putative NRPS or NRPS-like proteins (e.g. C. heterostrophus NPS10 and NPS12 [10 (link)]) that lack a complete A-T-C module. In addition, freestanding A domains in bacterial NRPSs have been shown to catalyze NRPS biosynthesis by activating and transferring substrates in trans to separate NRPSs [5 (link)] and the evolutionary relationship between monomodular NRPS-like proteins and multimodular NRPSs was also of interest.

Bushley K.E, & Turgeon B.G. (2010). Phylogenomics reveals subfamilies of fungal nonribosomal peptide synthetases and their evolutionary relationships. BMC Evolutionary Biology, 10, 26.

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Publication 2010

Acetate-CoA Ligase Anabolism Bacteria Base Sequence Biological Evolution Catalysis Coenzyme A Ligases Enzymes Fatty Acids Fungal Proteins Fusarium graminearum Gene Annotation Genes Genome Genome, Fungal Ligase Macrophage Inflammatory Protein-1 Muscle Tissue Ochratoxins Protein Domain Proteins SET protein, human Staphylococcal Protein A Strains

Most recents protocols related to «Ochratoxin A»

Quantifying Ochratoxin A by U-HPLC

OTA was quantified following the methodology described by Vecchio et al. (2012) [59 (link)]. Determinations were performed by ultra-high performance liquid chromatography (U-HPLC) (Agilent 1290 Infinity II, Santa Clara, CA, USA), equipped with a 20 μL loop and connected to a spectrofluorometer detector, Perkin Elmer Fluorescence Detector Series 200. The excitation and emission wavelengths were 330 and 460 nm. Chromatography was carried out isocratically using 4 mM sodium acetate/acetic acid (19:1): acetonitrile (60:40) as the mobile phase at a 1.0 mL/min flow rate. The working standard solution and sample volumes of 20 μL were injected in triplicate. The parameters were validated by six replicates. The LOD was 1.60 × 10⁻⁵ mg/kg, the LOQ was 4.80 × 10⁻⁵ mg/kg and the linearity coefficient (R²) was 9.997 × 10⁻¹. The retention time was 9.09 ± 0.08 min.

Guadalupe G.A., Grandez-Yoplac D.E., Arellanos E, & Doménech E. (2024). Probabilistic Risk Assessment of Metals, Acrylamide and Ochratoxin A in Instant Coffee from Brazil, Colombia, Mexico and Peru. Foods, 13(5), 726.

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Publication 2024

Mycotoxin Detection in Samples

The samples were washed with 10 mL of methanol aqueous solution (7:3, v/v). The concentration of ochratoxin A (OTA) and aflatoxin B1 (AFB1) was detected by using an ELISA kit (Suwei Microbiology Research, Wuxi, China), according to the manufacturer protocol [24 (link)].

Qiu Z., Wu F., Hu H., Guo J., Wu C., Wang P., Ling J., Cui Y., Ye J., Fang G, & Liu X. (2024). Deciphering the Microbiological Mechanisms Underlying the Impact of Different Storage Conditions on Rice Grain Quality. Foods, 13(2), 266.

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Publication 2024

Ochratoxin A Extraction from Milk

Not available on PMC !

Milk samples were thawed immediately before extraction. First, they were centrifuged in a centrifuge for 15 minutes at a centrifugation speed of 7,500 rpm. After centrifugation, 20 cm 3 of milk was passed through an OchraPrep immunoaffinity column (R-Biopharm Rhône LTD). After the samples passed through the column, they were washed with 20 cm 3 of deionized water and air dried. The next step was to elute the OTA through 1.5 cm 3 of ACN:MeOH mixture (3:2). In the final step, the samples were evaporated to dryness in a stream of nitrogen at 40 °C. Immediately before the samples were analyzed by liquid chromatography with fluorescence detection (HPLC -FLD), they were dissolved in 1 cm 3 of mobile phase.

Duliński R., & Byczyński Ł. (2024). THE EFFECT OF A DIET ON THE OCCURRENCE OF OCHRATOXIN A IN BODY FLUIDS. Żywność, 31(1), 160-176.

Publication 2024

Quantitative Determination of Ochratoxin A

Not available on PMC !

A 20 µl portion of internal standard ( 13 C-OTA) and 20 µl of β-glucoronidase were added to 1 cm 3 of serum. The samples were then incubated for 18 hours at 37 o C. After the incubation, 1 cm 3 of MeOH and 1.96 cm 3 of ACN were added to the mixture. Subsequently, the solution was vortexed for 2 minutes and centrifuged in a centrifuge for 10 minutes at 7,000 rpm. A 3 ml portion of the supernatant was transferred to a 50 cm 3 tube and evaporated in a stream of nitrogen. After evaporation, the samples were dissolved in 1 cm 3 of MeOH, first for 3 minutes in an ultrasonic cleaner and subsequently for 5 minutes in a shaker. In the next step, 25 cm 3 of PBS was added to the solution. The solution was quantitatively transferred to an OchraPrep immunoaffinity column (R-Biopharm Rhône LTD). After the sample passed through the column, it was washed with 20 cm 3 of distilled water and air dried. OTA was eluted by 1.5 cm 3 of MeOH:CH 3 COOH (98:2) into a 2 ml tube. Subsequently, it was evaporated in a stream of nitrogen at 40 o C. Immediately before LC -MS/MS analysis, the samples were dissolved in 150 µl of H 2 O:MeOH (7:3) mixture.

Duliński R., & Byczyński Ł. (2024). THE EFFECT OF A DIET ON THE OCCURRENCE OF OCHRATOXIN A IN BODY FLUIDS. Żywność, 31(1), 160-176.

Publication 2024

Ochratoxin A Determination in Urine

Not available on PMC !

A 10 cm 3 portion of urine was diluted with 10 cm 3 of 5 % NaHCO 3 solution. The samples were then mixed on a vortex. The next step involved the filtering of the solution through a smooth filter. A 10 cm 3 filtered solution was put into an OchraPrep immunoaffinity column (R-Biopharm Rhône LTD). After the samples passed through the column, they were washed with a 10 cm 3 portion of distilled water and air dried. In the next step, OTA was eluted by 2 cm 3 of MeOH. The final step was evaporation of the mixture in a stream of nitrogen at 40 o C. Immediately before the samples were analyzed by liquid chromatography with fluorescence detection (HPLC -FLD), they were dissolved in 1 cm 3 of mobile phase.

Duliński R., & Byczyński Ł. (2024). THE EFFECT OF A DIET ON THE OCCURRENCE OF OCHRATOXIN A IN BODY FLUIDS. Żywność, 31(1), 160-176.

Publication 2024

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What is Ochratoxin A and why is it important to study?

Ochratoxin A is a potent mycotoxin produced by certain Aspergillus and Penicillium fungi. It is a powerful nephrotoxin and carcinogen, posing a significant health risk to humans and animals. Studying Ochratoxin A is crucial for understanding its mechanisms of toxicity, developing effective detection methods, and establishing safety guidelines to protect public health.

How can PubCompare.ai assist with Ochratoxin A research?

PubCompare.ai is an AI-driven platform that can optimize your Ochratoxin A research by helping you locate the best protocols from literature, preprints, and patents using AI-powered comparisons. This cutting-edg technology can streamline your research process and maximize your results, allowing you to experiance the future of scientific research today. PubCompare.ai allows you to: 1) Screen protocol literature more efficiently, and 2) Leverage AI to pinpoint critical insights that help researchers identify the most effective protocols related to Ochratoxin A for your specific research goals. The platform's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy.

Are there different variations or types of Ochratoxin A?

Yes, there are different variants of Ochratoxin A that researchers need to be aware of. While Ochratoxin A is the most well-known and widely studied form, there are also structural analogs like Ochratoxin B and Ochratoxin C that exhibit similar toxicological properties. Understanding the unique characteristics and potential impacts of these various Ochratoxin types is essential for comprehensive research and risk assessment.

What are some specific applications of Ochratoxin A research?

Ochratoxin A research has a wide range of important applications, including: 1. Food and feed safety: Developing accurate detection methods and establishing regulatory limits for Ochratoxin A contamination in food and animal feed. 2. Toxicology and risk assessment: Elucidating the mechanisms of Ochratoxin A toxicity and carcinogenicity to better understand its health impacts. 3. Environmental monitoring: Tracking Ochratoxin A levels in agricultural products, water, and other environmental samples. 4. Decontamination and remediation: Exploring strategies to remove or neutralize Ochratoxin A in contaminated materials.

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