scholarly journals Complete wastewater discoloration by a novel peroxidase source with promising bioxidative properties

2022 ◽  
Author(s):  
Natalia Klanovicz ◽  
Fábio Spitza Stefanski ◽  
Aline Frumi Camargo ◽  
William Michelon ◽  
Helen Treichel ◽  
...  
Keyword(s):  
Specific Activity ◽  
Residual Activity ◽  
Free Form ◽  
Guaiacol Peroxidase ◽  
The Novel ◽  
Enzymatic Extract ◽  
Toxicological Evaluation ◽  
Microalgal Biomass ◽  
Treatment Technologies ◽  
Ph Range

Abstract BACKGROUND Our study aimed to characterize and prospect immobilization strategies for a novel fungal peroxidase - POD (EC 1.11.1.7) and to insert it in the context of pollutant remediation, since these compounds pose risks to human and environmental health. The enzymatic extract was obtained by submerged fermentation of the fungus Trichoderma koningiopsis in an alternative substrate, consisting of fresh microalgal biomass. The immobilization efficiency was evaluated by monitoring the residual activity (RA) and the discoloration potential (DP) of a synthetic dye solution. Concomitantly, the catalytic properties of free POD were explored, and the most promising storage strategy to maintain the enzymatic activity was studied. RESULTS The novel guaiacol peroxidase expressed specific activity of up to 7801 U mg−1 in the free form, showing stability when subjected to up to 80°C in a pH range between 4.0-8.0. Furthermore, the bioproduct immobilized on magnetic nanoparticles expressed up to 689% RA and 100% DP. An increase in the RA of the enzyme, both in free and immobilized form, was also observed after storage for up to 8 months. The synthesized magnetic nanozymes showed good reusability, maintaining 13546 U mg−1 after ten cycles and removing 94% of color in a second batch. Toxicological evaluation with Allium cepa indicated that the enzymatic process of color removal with immobilized POD was essential to eliminate genotoxic effects. CONCLUSION T. koningiopsis peroxidase production and immobilization presented in our work are promising for the enzyme market and for the wastewater treatment technologies, considering its high bioxidative potential.

scholarly journals Complete wastewater discoloration by a novel peroxidase source with promising bioxidative properties

2021 ◽  
Author(s):  
Natalia Klanovicz ◽  
Fábio Spitza Stefanski ◽  
Aline Frumi Camargo ◽  
William Michelon ◽  
Helen Treichel ◽  
...  
Keyword(s):  
Wastewater Treatment ◽  
Wastewater Treatment Plants ◽  
Specific Activity ◽  
Residual Activity ◽  
Free Form ◽  
Guaiacol Peroxidase ◽  
Enzymatic Extract ◽  
Toxicological Evaluation ◽  
Microalgal Biomass ◽  
Oxidoreductase Enzymes

Abstract The occurrence of micropollutants in aqueous matrices has become a global concern and a challenge for wastewater treatment plants. Monitoring their toxicity has shown that these compounds, even at low concentrations, pose risks to human and environmental health. Therefore, our study aimed to prospect immobilization strategies for non-commercial oxidoreductase enzymes and insert them in the context of pollutant remediation. The enzymatic extract was obtained by submerged fermentation of the fungus Trichoderma koningiopsis in an alternative substrate, consisting of fresh microalgal biomass from the phycoremediation process. The immobilization efficiency of peroxidase (POD) was evaluated by monitoring the residual activity (RA) and the discoloration potential (DP) of a synthetic dye solution. Concomitantly, the catalytic properties of free POD were explored, and the most promising storage strategy to maintain the enzymatic activity was studied. Guaiacol peroxidase from T. koningiopsis expressed specific activity of up to 7801.1 U mg− 1 in the free form, showing stability when subjected to up 80°C in a pH range between 4.0–8.0. Furthermore, the bioproduct immobilized on magnetic nanoparticles expressed up to 688% RA and 100% DP. An increase in the RA of the enzyme, both in free and immobilized form, was also observe after storage for up to 8 months. The synthesized magnetic nanozymes showed good reusability, maintaining 13546.4 U mg− 1 after ten cycles and removing 93% of color in a second batch. Toxicological evaluation with Allium cepa indicated that the enzymatic process of color removal with immobilized POD, despite maintaining unwanted cytotoxic effects, was essential to eliminate genotoxic effects. In this sense, the immobilization processes of T. koningiopsis peroxidase presented in our work are promising for the enzyme market and for the wastewater treatment sector.

scholarly journals ENHANCED ENZYMATIC ACTIVITY OF STREPTOMYCES GRISEOPLANUS L-ASPARGINASE VIA ITS INCORPORATION IN AN OIL-BASED NANOCARRIER

2020 ◽  
pp. 203-210
Author(s):  
ABEER A. EL-HADI ◽  
HANAN MOSTAFA AHMED ◽  
RANIA A. ZAKI ◽  
AMIRA MOHAMED MOHSEN
Keyword(s):  
Thermal Stability ◽  
Oleic Acid ◽  
Enzymatic Activity ◽  
Specific Activity ◽  
Residual Activity ◽  
Tween 80 ◽  
Biochemical Properties ◽  
Lymphocytic Leukemia ◽  
Tween 20 ◽  
Ph Range

Objective: L-asparaginase (L-asp) is a vital enzyme used as a therapeutic agent in combination with other drugs in the treatment of acute lymphoma, melanosarcoma and lymphocytic leukemia. Immobilization of enzymes through loading on nanoemulsion (NE) results in some advantages such as enhancing their stability and increasing their resistance to proteases. Aim of the present study is to formulate L-asp loaded nanoemulsion to enhance its efficiency and thermal stability. Methods: Nanoemulsion loaded with L-asp crude extract (specific activity 13.23U/mg protein) was prepared employing oleic acid as oil, tween 20/tween 80 as surfactants and propylene glycol (PG) as co-surfactant. L-asp loaded NE underwent several thermodynamic stability studies and the optimized formulae were further examined for their biochemical properties and thermal stability. Results The developed formulations were spherical in shape and their sizes were in the nanometric dimensions with negatively charged zeta potential values. Upon comparing the enzyme activity of L-asp loaded NE employing tween 20 (F1) or tween80 (F4) at different concentrations, the results revealed that F4 NE showed higher enzymatic activity [323 U/ml] compared to F1 NE [197 U/ml] at the same concentration. The nanosized immobilized L-asp was more stable in the pH range from 8 to 8.5 as compared to free L-asp. The immobilized enzyme preserved about 59.11% of its residual activity at 50 °C; while free L-asp preserved about 33.84%. Conclusion: In the view of these results, NE composed of oleic acid, tween 80 and PG represents a promising dosage form for enhancing the activity and stability of Streptomyces griseoplanus L-asp.

An International Collaborative Study to Investigate Standardisation of Hirudin Potency

1993 ◽  
Vol 69 (05) ◽  
pp. 430-435 ◽  
Author(s):  
Colin Longstaff ◽  
Man-Yu Wong ◽  
Patrick J Gaffney
Keyword(s):  
Specific Activity ◽  
Collaborative Study ◽  
Residual Activity ◽  
Quality Standard ◽  
Upper Limit ◽  
Assay Procedure ◽  
Specific Activities ◽  
International Collaborative ◽  
Range Of Values ◽  
International Collaborative Study

SummaryAn international collaborative study has been carried out to investigate the reproducibility of hirudin assays in 13 laboratories using four recombinant hirudins and one natural, sulphated product. A simple assay procedure was proposed involving the titration of α-thrombin with inhibitor and measurement of residual activity using a chromogenic substrate. A standard α-thrombin preparation was supplied to ensure that this reagent was of uniform quality throughout the study. The method appeared to present no difficulties and laboratories reported similar potencies for the 5 hirudin samples, in line with expected values. This gave 200–222 Thrombin Inhibitory Units/ampoule (TIU/ampoule) of lyophilised hirudin, with geometric coefficient of variation (gcv) values ranging from 10.15–15.97%. This corresponds to specific activities of approximately 14,300–15,900 TIU/mg protein. This is close to the upper limit of previously reported values of specific activity. We conclude that the precision of this determination compared with the wider range of values in the literature (8,000–16,000 thrombin inhibitory units [TIU]/mg) results from the use of good quality standard α-thrombin by all laboratories. This study has important implications for hirudin standardisation.

scholarly journals Entrapment of the Fastest Known Carbonic Anhydrase with Biomimetic Silica and Its Application for CO2 Sequestration

Polymers ◽  
2021 ◽  
Vol 13 (15) ◽  
pp. 2452
Author(s):  
Chia-Jung Hsieh ◽  
Ju-Chuan Cheng ◽  
Chia-Jung Hu ◽  
Chi-Yang Yu
Keyword(s):  
Carbonic Anhydrase ◽  
High Activity ◽  
Co2 Sequestration ◽  
Residual Activity ◽  
Entrapment Efficiency ◽  
Free Form ◽  
Uncatalyzed Reaction ◽  
The Stability ◽  
Time Required

Capturing and storing CO2 is of prime importance. The rate of CO2 sequestration is often limited by the hydration of CO2, which can be greatly accelerated by using carbonic anhydrase (CA, EC 4.2.1.1) as a catalyst. In order to improve the stability and reusability of CA, a silica-condensing peptide (R5) was fused with the fastest known CA from Sulfurihydrogenibium azorense (SazCA) to form R5-SazCA; the fusion protein successfully performed in vitro silicification. The entrapment efficiency reached 100% and the silicified form (R5-SazCA-SP) showed a high activity recovery of 91%. The residual activity of R5-SazCA-SP was two-fold higher than that of the free form when stored at 25 °C for 35 days; R5-SazCA-SP still retained 86% of its activity after 10 cycles of reuse. Comparing with an uncatalyzed reaction, the time required for the onset of CaCO3 formation was shortened by 43% and 33% with the addition of R5-SazCA and R5-SazCA-SP, respectively. R5-SazCA-SP shows great potential as a robust and efficient biocatalyst for CO2 sequestration because of its high activity, high stability, and reusability.

scholarly journals Bioprospection and characterization of the amylolytic activity by filamentous fungi from Brazilian Atlantic Forest

2017 ◽  
Vol 17 (3) ◽  
Author(s):  
Paula Zaghetto de Almeida ◽  
Marita Gimenez Pereira ◽  
Caio Cesar de Carvalho ◽  
Paulo Ricardo Heinen ◽  
Luciana Sobrani Ziotti ◽  
...  
Keyword(s):  
Filamentous Fungi ◽  
Atlantic Forest ◽  
Rhizopus Oryzae ◽  
Residual Activity ◽  
Brazilian Atlantic Forest ◽  
Tropical Environments ◽  
Aspergillus Brasiliensis ◽  
Significant Difference ◽  
Initial Ph ◽  
Ph Range

Abstract Filamentous fungi are widely diverse and ubiquitous organisms. Such biodiversity is barely known, making room for a great potential still to be discovered, especially in tropical environments - which are favorable to growth and species variety. Filamentous fungi are extensively applied to the production of industrial enzymes, such as the amylases. This class of enzymes acts in the hydrolysis of starch to glucose or maltooligosaccharides. In this work twenty-five filamentous fungi were isolated from samples of decomposing material collected in the Brazilian Atlantic Forest. The two best amylase producers were identified as Aspergillus brasiliensis and Rhizopus oryzae. Both are mesophilic, they grow well in organic nitrogen-rich media produce great amounts of glucoamylases. The enzymes of A. brasiliensis and R. oryzae are different, possibly because of their phylogenetical distance. The best amylase production of A. brasiliensis occurred during 120 hours with initial pH of 7.5; it had a better activity in the pH range of 3.5-5.0 and at 60-75°C. Both fungal glucoamylase had wide pH stability (3-8) and were activated by Mn2+. R. oryzae best production occurred in 96 hours and at pH 6.5. Its amylases had a greater activity in the pH range of 4.0-5.5 and temperature at 50-65ºC. The most significant difference between the enzymes produced by both fungi is the resistance to thermal denaturation: A. brasiliensis glucoamylase had a T50 of 60 minutes at 70ºC. The R. oryzae glucoamylase only had a residual activity when incubated at 50°C with a 12 min T50.

scholarly journals A NewIn VivoModel System to Assess the Toxicity of Semiconductor Nanocrystals

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Angela Tino ◽  
Alfredo Ambrosone ◽  
Lucia Mattera ◽  
Valentina Marchesano ◽  
Andrei Susha ◽  
...  
Keyword(s):  
Semiconductor Nanocrystals ◽  
Minimal Risk ◽  
The Novel ◽  
Toxicological Evaluation ◽  
Hydra Vulgaris ◽  
Population Growth Rates ◽  
Single Structure

In the emerging area of nanotechnology, a key issue is related to the potential impacts of the novel nanomaterials on the environment and human health, so that this technology can be used with minimal risk. Specifically designed to combine on a single structure multipurpose tags and properties, smart nanomaterials need a comprehensive characterization of both chemicophysical properties and adequate toxicological evaluation, which is a challenging endeavour; thein vitrotoxicity assays that are often employed for nanotoxicity assessments do not accurately predictin vivoresponse. To overcome these limitations and to evaluate toxicity characteristics of cadmium telluride quantum dots in relation to surface coatings, we have employed the freshwater polypHydra vulgarisas a model system. We assessedin vivoacute and sublethal toxicity by scoring for alteration of morphological traits, population growth rates, and influence on the regenerative capabilities providing new investigation clues for nanotoxicology purposes.

Mechanism of secretion of plasma insulin-like growth factor-I into milk of lactating goats

1991 ◽  
Vol 131 (3) ◽  
pp. 459-466 ◽  
Author(s):  
C. G. Prosser ◽  
I. R. Fleet ◽  
A. J. Davis ◽  
R. B. Heap
Keyword(s):  
Growth Factor ◽  
Time Course ◽  
Specific Activity ◽  
Gel Filtration ◽  
Free Form ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Lactating Goats ◽  
Igf I ◽  
Growth Factor I

ABSTRACT 125I-Labelled insulin-like growth factor-I (IGF-I) was infused as the free form directly into the pudic artery supplying one gland of lactating goats (n = 6). The infusion was for 60 min and 0·4±0·09% (s.e.m.) of the infusate was secreted into milk from the infused gland during its first passage through that gland. A large proportion of the 125I-labelled IGF-I escaped into the systematic circulation and was secreted into milk of both glands. A total of 5·2±0·4% of infused radioactivity was recovered in milk from both glands from 0 to 720 min. Radioactivity consisted of trichloroacetic acid (TCA)-precipitable and -soluble counts which were shown by gel filtration to be authentic IGF-I and degraded products of the peptide. The amount and time course of TCA-soluble radioactivity in milk from both glands was similar, suggesting degradation of 125I-labelled IGF-I at extramammary sites. Maximum specific activity for 125I-labelled IGF-I in milk from the infused gland was reached 80–120 min after the start of infusion and was 2·5-fold greater than milk from the non-infused gland. The time course of appearance of 125I-labelled IGF-I in milk suggests that transfer was via the transcellular pathway and this was further supported by comparing the pattern of transfer of [14C]sucrose and [14C]amino acids. When excess unlabelled IGF-I was included in the infusate, specific activity in milk from the infused gland was reduced to that of the non-infused gland, indicating a competitive and saturable mechanism of secretion for 125I-labelled IGF-I. Comparison of uptake and secretion of 125I-labelled IGF-I into milk from the non-infused gland with that of endogenous immunoreactive IGF-I suggests that vectorial transport of IGF-I across the mammary gland may be a significant contributor of IGF-I levels in milk. Journal of Endocrinology (1991) 131, 459–466

scholarly journals Digestive Proteases From Fish Processing Wastes: Their Partial Characterization and Comparison

2020 ◽  
Author(s):  
Ivana Soledad Friedman ◽  
Leonel Agustín Behrens ◽  
Nair A Pereira ◽  
Edgardo Contreras ◽  
Analia Verónica Fernández-Gimenez
Keyword(s):  
Residual Activity ◽  
Fish Processing ◽  
Intestinal Enzymes ◽  
Optimum Ph ◽  
Digestive Proteinases ◽  
Wide Ph Range ◽  
Processing Wastes ◽  
Reducing Costs ◽  
Ph Range ◽  
Percophis Brasiliensis

Abstract Fish processing generates a lot of wastes which are discarded resulting in environmental problems. However, this material represents a significant source of high-value bioproducts with potential biotechnological applications. The objective of this study was to characterize and to compare specific activities of acid and alkaline proteases recovered from the viscera of Merluccius hubbsi (Mh), Percophis brasiliensis (Pb), Urophyis brasiliensis (Ub), and Cynoscion guatucupa (Cg) under different pH and temperature conditions. Stomach proteinases from four species had a higher activity at pH 2, with stability in the range of pH 2-4. Optimum pH from intestinal enzymes of Cg was 11.5, while for the crude extract of Mh, Pb, and Ub catalytic activity was registered over a wide pH range range from 7 to 11.5. Stomach proteinases from four studied species had a higher activity at 30 °C and 50 °C, with stability at 10 °C and 30 °C. Optimum temperature from intestinal enzymes of the four tested species was 50 °C with high stability at 10 °C and 30 °C. Alkaline proteinase from all species and acid proteinases from Cg was inactivated at 70ºC, while stomach enzymes of Mh, Pb, and Ub had a residual activity lower than 5% at 80 °C after 5, 10 y 20 minutes of pre-incubation, respectively. Digestive proteinases recovered in this study could be used as biocatalysts in industrial processes, reducing costs, adding value to the fishery waste, and contributing to the reduction of environmental pollution.

scholarly journals Introducing a Thermo-Alkali-Stable, Metallic Ion-Tolerant Laccase Purified From White Rot Fungus Trametes hirsuta

2021 ◽  
Vol 12 ◽  
Author(s):  
Jing Si ◽  
Hongfei Ma ◽  
Yongjia Cao ◽  
Baokai Cui ◽  
Yucheng Dai
Keyword(s):  
Specific Activity ◽  
Endocrine Disrupting Chemicals ◽  
Environmental Pollutants ◽  
Fold Increase ◽  
Industrial Applications ◽  
White Rot ◽  
White Rot Fungus ◽  
Metallic Ions ◽  
Trametes Hirsuta ◽  
Ph Range

This study introduces a valuable laccase, designated ThLacc-S, purified from white rot fungus Trametes hirsuta. ThLacc-S is a monomeric protein in nature with a molecular weight of 57.0 kDa and can efficiently metabolize endocrine disrupting chemicals. The enzyme was successfully purified to homogeneity via three consecutive steps consisting of salt precipitation and column chromatography, resulting in a 20.76-fold increase in purity and 46.79% yield, with specific activity of 22.111 U/mg protein. ThLacc-S was deciphered as a novel member of the laccase family and is a rare metalloenzyme that contains cysteine, serine, histidine, and tyrosine residues in its catalytic site, and follows Michaelis-Menten kinetic behavior with a Km and a kcat/Km of 87.466 μM and 1.479 s–1μM–1, respectively. ThLacc-S exerted excellent thermo-alkali stability, since it was markedly active after a 2-h incubation at temperatures ranging from 20 to 70°C and retained more than 50% of its activity after incubation for 72 h in a broad pH range of 5.0–10.0. Enzymatic activities of ThLacc-S were enhanced and preserved when exposed to metallic ions, surfactants, and organic solvents, rendering this novel enzyme of interest as a green catalyst for versatile biotechnological and industrial applications that require these singularities of laccases, particularly biodegradation and bioremediation of environmental pollutants.

scholarly journals Production and Characterization of Esterase in Lantinus tigrinus for Degradation of Polystyrene

2013 ◽  
Vol 62 (1) ◽  
pp. 101-108 ◽  
Author(s):  
LUBNA TAHIR ◽  
MUHAMMAD ISHTIAQ ALI ◽  
MUHAMMAD ZIA ◽  
NAIMA ATIQ ◽  
FARIHA HASAN ◽  
...  
Keyword(s):  
Acidic Medium ◽  
Specific Activity ◽  
Mineral Salt Medium ◽  
Tween 80 ◽  
Synthetic Polymers ◽  
Ftir Analysis ◽  
Polystyrene Film ◽  
Biological Degradation ◽  
Ph Range

Polystyrene is considered stable to biological degradation. Lantinus tigrinus isolated from wood sample produced esterase in growth medium under normal conditions. However, acidic medium, 37 degrees C temperature, presence of tween 80; and urea and yeast extract in mineral salt medium enhance the production of esterase and specific activity. Purified esterase was active at broad pH range and 45 degrees C. FTIR analysis confirmed that esterase produced by Lantinus tigrinus effectively degraded polystyrene film and broke macromolecules down to non-toxic molecules. This study concludes that the presence of Lantinus tigrinus at dumping sites can be exploited for waste management containing high molecular weight synthetic polymers.

Sign in / Sign up

Export Citation Format

Share Document