scholarly journals Evaluation of Enzymes Production Activity of Trichoderma, Aspergillus and Rhizopus Species in Paraeforce (Herbicide) Degradation

2020 ◽  
pp. 1-7
Author(s):  
F. I. Onianwah ◽  
H. O. Stanley ◽  
V. C. Eze ◽  
V. O. Ifeanyi ◽  
C. J. Ugboma
Keyword(s):  
Hydrogen Peroxide ◽  
Soil Samples ◽  
Laccase Production ◽  
Methyl Red ◽  
Aerobic Incubation ◽  
Fungal Isolation ◽  
Qualitative And Quantitative ◽  
Herbicide Degradation ◽  
Production Activity ◽  
Catalase Peroxidase

The study aims to evaluate enzymes that facilitate fungal degradation of paraeforce. Soil samples for fungal isolation were collected from impacted sites and inoculated on potato dextrose agar (PDA). The isolates were screened for growth and tolerance to paraefoce in 50 mg/l concentration of the test herbicides. Trichoderma, Aspergillus and Rhizopus species were found to grow in paraeforce supplemented PDA. Qualitative and quantitative assay for different enzyme production in hydrogen peroxide, methyl red, guaiacol and hydrogen peroxide-pyrogallol complex proved potential for catalase, lignin peroxidase, laccase and manganese peroxidase production, respectively. The results showed that these three fungi have great potential for catalase, peroxidase and laccase production after six days aerobic incubation in paraeforce and these enzymes facilitated the utilization of the paraeforce.  

Screening and Identification of Laccase Producing Fungi from Environmental Samples

2021 ◽  
Vol 6 (1) ◽  
pp. 91-98
Author(s):  
A. Bello ◽  
◽  
J. B. Ameh ◽  
D. A. Machido ◽  
A. I. Mohammed-Dabo
Keyword(s):  
Tannic Acid ◽  
Fungal Species ◽  
Soil Samples ◽  
Potato Dextrose Agar ◽  
Laccase Production ◽  
Curvularia Lunata ◽  
Main Campus ◽  
Fungal Isolates ◽  
Screening And Identification ◽  
Decaying Wood

Laccases are oxidases with broad substrate specificity and ability to oxidize various phenolic and non-phenolic compounds. This study was carried out to isolate and characterizes laccase producing fungi from environment samples. Soil and decaying wood samples were collected from different locations within Ahmadu Bello University, Zaria Main campus. Suspensions of the samples (1 g in 10 mL sterile distilled water) were serially diluted, inoculated onto Potato Dextrose Agar (PDA) containing 0.01% Chloramphenicol and incubated for 7 days at 30oC.The fungal isolates were characterized macroscopically and microscopically with the aid of an atlas. The identified fungal isolates were screened for laccase production by inoculating onto PDA containing 0.02% Guaiacol, 1mM ABTS (2 2’-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) and 0.5% Tannic acid as indicator compounds and incubated at 250C for 7 days. The laccase producing isolates were confirmed molecularly by ITS rDNA sequence analysis using the FASTA algorithm with the Fungus database from the European Bioinformatics Institute (EBI).A total of 25 fungal species (11 from soil and 14 from decaying wood samples) were isolated. Two isolates from the soil origin identified as Curvularia lunata SSI7 (Accession No. QIE06317.1) and Fusarium clade VII SSI3 (Accession No. GQ505677) were found to produce laccase where Curvularia lunata SSI7 was able to oxidize all the indicator compounds used for the screening. Fusarium clade VII SSI3 was able to oxidize only 0.5% Tannic acid. Laccase producing Curvularia lunata and Fusarium clade VII were isolated from soil samples collected from ABU Zaria Main Campus. Keywords: laccase, fungi, soil, decaying wood

THE OXIDATION OF ESTRONE-16-C14BY PEROXIDASE

1962 ◽  
Vol 40 (1) ◽  
pp. 459-469 ◽  
Author(s):  
P. H. Jellinck ◽  
Louise Irwin
Keyword(s):  
Amino Acids ◽  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Serum Albumin ◽  
Oxidase Activity ◽  
Water Soluble ◽  
The Other ◽  
Aerobic Incubation ◽  
Nitrogenous Compounds ◽  
Initial Generation

Aerobic incubation of estrone-16-C14with peroxidase in the presence of serum albumin and other proteins resulted in the formation of water-soluble, ether-insoluble metabolites in high percentage yields. Similar products were formed when protein was replaced by cysteine or tryptophan but none of the other amino acids tested had any effect. The evidence points to an initial generation of hydrogen peroxide from these nitrogenous compounds by the enzyme acting as an aerobic oxidase, and the subsequent peroxidation of estrone to highly reactive products. These then combine with the protein or amino acid or else undergo alternative reactions. A strong chemical bond is formed with albumin and attempts to release the estrone metabolites from it were unsuccessful. Uterine homogenates from estrogen-treated rats showing high DPNH oxidase activity contained no "peroxidase" as measured by the formation of water-soluble products from estrone in the presence of protein.

scholarly journals Identification of a Regulator That Controls Stationary-Phase Expression of Catalase-Peroxidase in Caulobacter crescentus

1999 ◽  
Vol 181 (19) ◽  
pp. 6152-6159 ◽  
Author(s):  
Paul S. Rava ◽  
Laura Somma ◽  
Howard M. Steinman
Keyword(s):  
Hydrogen Peroxide ◽  
Stress Response ◽  
Stationary Phase ◽  
Caulobacter Crescentus ◽  
Sequence Similarity ◽  
Enteric Bacteria ◽  
Cross Resistance ◽  
Peptide Antibiotic ◽  
Reading Frame ◽  
Catalase Peroxidase

ABSTRACT Expression of the catalase-peroxidase of Caulobacter crescentus, a gram-negative member of the α subdivision of theProteobacteria, is 50-fold higher in stationary-phase cultures than in exponential cultures. To identify regulators of the starvation response, Tn5 insertion mutants were isolated with reduced expression of a katG::lacZ fusion on glucose starvation. One insertion interrupted an open reading frame encoding a protein with significant amino acid sequence identity to TipA, a helix-turn-helix transcriptional activator in the response ofStreptomyces lividans to the peptide antibiotic thiostrepton, and lesser sequence similarity to other helix-turn-helix regulators in the MerR family. The C. crescentus orthologue of tipA was named skgA (stationary-phase regulation of katG). Stationary-phase expression ofkatG was reduced by 70% in theskgA::Tn5 mutant, and stationary-phase resistance to hydrogen peroxide decreased by a factor of 10. Like the wild type, the skgA mutant exhibited starvation-induced cross-resistance to heat and acid shock, entered into the helical morphology that occurs after 9 to 12 days in stationary phase, and during exponential growth inducedkatG in response to hydrogen peroxide challenge. Expression of skgA increased 5- to 10-fold in late exponential phase.skgA is the first regulator of a starvation-induced stress response identified in C. crescentus. SkgA is not a global regulator of the stationary-phase stress response; its action encompasses the oxidative stress-hydrogen peroxide response but not acid or heat responses. Moreover, SkgA is not an alternative ς factor, like RpoS, which controls multiple aspects of starvation-induced cross-resistance to stress in enteric bacteria. These observations raise the possibility that regulation of stationary-phase gene expression in this member of the α subdivision of the Proteobacteria is different from that inEscherichia coli and other members of the γ subdivision.

scholarly journals Screening, Identification of Alkaline Proteases Producing Fungi from Soil of Different Habitats of Amalner Tahsil [Maharashtra] and Their Applications

2017 ◽  
Vol 5 (3) ◽  
pp. 397-402 ◽  
Author(s):  
H.K. Suryawanshi ◽  
N.D. Pandya
Keyword(s):  
Proteolytic Activity ◽  
Soil Samples ◽  
Precipitation Method ◽  
Diffusion Method ◽  
Clot Lysis ◽  
Partial Purification ◽  
Fungal Isolation ◽  
Lysis Activity ◽  
Stain Removal ◽  
Pharmaceutical Industries

Fungal proteases had wide applications in textile, leather, food and Pharmaceutical industries. As proteases shows proteolytic activity they are helpful in proteinic stain removal hence also used in various commercial detergent industries. For fungal isolation soil samples were collected from different sites of Amalner tahsil. (Maharashtra) e.g. crop fields, near dairy areas, poultry farms etc. Those soil samples showing alkaline pH were selected for isolation of fungi on Potato Dextrose Agar plates. Then among 14 different isolates 2 were selected for their most proteolytic activity after screening on casein agar, skimmed milk agar and gelatine agar. For submerged fermentation, these selected isolates were inoculated in production media in shake flask. After 72 hrs, plate assay was performed by taking crude enzyme after filtration and centrifugation as well as by taking partially purified enzyme.(partial purification done by ammonium sulphate precipitation method). Protease activity assay was performed by agar well diffusion method, as well as blood clot lysis activity and blood stain removal ability of protease obtained from selected isolates was studied.Selected isolates were identified,among them Aspergillus niger gives more proteolytic activity than Trichoderma longibrachiatum. Int. J. Appl. Sci. Biotechnol. Vol 5(3): 397-402

scholarly journals Regulation of Brucella abortusCatalase

2000 ◽  
Vol 68 (7) ◽  
pp. 3861-3866 ◽  
Author(s):  
Jeong-a Kim ◽  
Zengyu Sha ◽  
John E. Mayfield
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Pathogenic Bacteria ◽  
Sublethal Concentration ◽  
Subsequent Exposure ◽  
Catalase Peroxidase ◽  
Increased Sensitivity ◽  
Analysis Survival ◽  
Hostile Environments

ABSTRACT All aerobic organisms have mechanisms that protect against oxidative compounds. Catalase, peroxidase, superoxide dismutase, glutathione, and thioredoxin are widely distributed in many taxa and constitute elements of a nearly ubiquitous antioxidant metabolic strategy. Interestingly, the regulatory mechanisms that control these elements are rather different depending on the nature of the oxidative stress and the organism. Catalase is well documented to play an important role in protecting cells from oxidative stress. In particular, pathogenic bacteria seem to use this enzyme as a defensive tool against attack by the host. To investigate the significance of catalase in hostile environments, we made catalase deletion mutations in two different B. abortus strains and used two-dimensional gel analysis, survival tests, and adaptation experiments to explore the behavior and role of catalase under several oxidative stress conditions. These studies show that B. abortus strains that do not express catalase activity exhibit increased sensitivity to hydrogen peroxide. We also demonstrate that catalase expression is regulated in this species, and that preexposure to a sublethal concentration of hydrogen peroxide allows B. abortus to adapt so as to survive subsequent exposure to higher concentrations of hydrogen peroxide.

scholarly journals Isolation and characterization of phosphate solubilizing bacteria from corn rhizosfer

2021 ◽  
Vol 911 (1) ◽  
pp. 012063
Author(s):  
Haswania ◽  
H Karim ◽  
A.A. Azis ◽  
N Iriany ◽  
O Jumadi
Keyword(s):  
Soil Samples ◽  
Phosphate Solubilizing Bacteria ◽  
Methyl Red ◽  
Biochemical Tests ◽  
Gram Staining ◽  
Isolation And Characterization ◽  
Sucrose Fermentation ◽  
Phosphate Solubilizing ◽  
Sample Dilution

Abstract The aim of this study was to isolate and characterize the Phosphate solubilizing bacteria from the rhizosphere of Zea mays L., Jeneponto Regency. This research was conducted in several stages; i.e, sampling, medium preparation, sample dilution, isolation, characterization in the form of gram staining, biochemical tests, and quantitative tests of phosphate solubility. Soil samples were diluted in 0.9% NaCl and soil containing microbes was isolated on the Picovskaya medium. Three isolates were obtained which could dissolve phosphate, namely J2KN1, J3KR2, and J3TG3 isolates. The isolates were generally round in shape with raised elevations, white, slimy, smooth, shiny surface, milky white, shape like coccus and bacillus, and gram-negative. Some of the isolates had positive motility, indole, voges, methyl red, glucose, and sucrose fermentation in the biochemical test. The quantitative tests of the ability to dissolve phosphate showed that J2KN1 isolate had the highest concentration of 51.1 μM, and the J3KR1 and J3TG3 isolates had a concentration of 45.2 μM and 37.6 μM, respectively.

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