scholarly journals Immobilization of the Peroxygenase from Agrocybe aegerita. The Effect of the Immobilization pH on the Features of an Ionically Exchanged Dimeric Peroxygenase

Catalysts ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 560
Author(s):  
Diego Carballares ◽  
Roberto Morellon-Sterling ◽  
Xiaomin Xu ◽  
Frank Hollmann ◽  
Roberto Fernandez-Lafuente
Keyword(s):  
Anion Exchange ◽  
Immobilized Enzyme ◽  
Residual Activity ◽  
Free Enzyme ◽  
The Other ◽  
Vinyl Sulfone ◽  
Agrocybe Aegerita ◽  
Inactive Form ◽  
The Stability

This paper outlines the immobilization of the recombinant dimeric unspecific peroxygenase from Agrocybe aegerita (rAaeUPO). The enzyme was quite stable (remaining unaltered its activity after 35 h at 47 °C and pH 7.0). Phosphate destabilized the enzyme, while glycerol stabilized it. The enzyme was not immobilized on glyoxyl-agarose supports, while it was immobilized albeit in inactive form on vinyl-sulfone-activated supports. rAaeUPO immobilization on glutaraldehyde pre-activated supports gave almost quantitative immobilization yield and retained some activity, but the biocatalyst was very unstable. Its immobilization via anion exchange on PEI supports also produced good immobilization yields, but the rAaeUPO stability dropped. However, using aminated agarose, the enzyme retained stability and activity. The stability of the immobilized enzyme strongly depended on the immobilization pH, being much less stable when rAaeUPO was adsorbed at pH 9.0 than when it was immobilized at pH 7.0 or pH 5.0 (residual activity was almost 0 for the former and 80% for the other preparations), presenting stability very similar to that of the free enzyme. This is a very clear example of how the immobilization pH greatly affects the final biocatalyst performance.

scholarly journals Purification and Characterization of Two Endo-β-1,4-glucanases from Mollusca, Ampullaria crossean

2005 ◽  
Vol 37 (10) ◽  
pp. 702-708 ◽  
Author(s):  
Yan-Hong Li ◽  
Rui Guo ◽  
Qiu-Yu Yin ◽  
Ming Ding ◽  
Si-Liang Zhang ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Carboxymethyl Cellulose ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecylsulfate ◽  
Gel Filtration ◽  
Residual Activity ◽  
Hydrolytic Activity ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
The Stability

Abstract Two novel endo-β-1,4-glucanases, EG45 and EG27, were isolated from the gastric juice of mollusca, Ampullaria crossean, by anion exchange, hydrophobic interaction, gel filtration and a second round of anion exchange chromatography. The purified proteins EG45 and EG27 appeared as a single band on sodium dodecylsulfate polyacrylamide gel electrophoresis with a molecular mass of 45 kDa and 27 kDa, respectively. The optimum pH for CMC activity was 5.5 for EG45 and 4.4-4.8 for EG27. The optimum temperature range for EG27 was broad, between 50 °C and 60 °C; for EG45 it was 50 °C. The analysis on the stability of these two endo-β-1,4-glucanases showed that EG27 was acceptably stable at pH 3.0-11.0 even when the incubation time was prolonged to 24 h at 30 °C, whereas EG45 remained relatively stable at pH 5.0-8.0. About 85% of the activity of EG27 could be retained upon incubation at 60 °C for 24 h. However, less than 10% residual activity of EG45 was detected at 50 °C. Among different kinds of substrates, both enzymes showed a high preference for carboxymethyl cellulose. EG45, in particular, showed a carboxymethyl cellulose hydrolytic activity of 146.5 IU/mg protein. Both enzymes showed low activities to xylan (from oat spelt) and Sigmacell 101, and they were inactive to p-nitrophenyl-β-D-cellobioside, salicin and starch.

scholarly journals Degradation of Anthracene by Immobilizing Laccase From Trametes Versicolor onto Chitosan Beads and Hyacinth Plant

2020 ◽  
Vol 31 (3) ◽  
pp. 14
Author(s):  
Ali A. Taha ◽  
Nahida J. Hameed ◽  
Farah Hamed Ali
Keyword(s):  
Polycyclic Aromatic Hydrocarbons ◽  
Aromatic Hydrocarbons ◽  
Trametes Versicolor ◽  
Free Enzyme ◽  
The Other ◽  
Chitosan Beads ◽  
Immobilized Laccase ◽  
Mediator System ◽  
Polycyclic Aromatic ◽  
The Stability

Polycyclic aromatic hydrocarbons (PAHs) are recognized as a toxic, mutagenic and/or carcinogenic compounds, and their pollution of soil and aquifer is of increasing environmentally risk. Laccases (E.C. 1.10.3.2) are phenoloxidases catalyze the oxidation of PAHs in the presence of a mediator compound and hyacinth plant. In this study laccase from Trametes versicolor was immobilized into chitosan, and the potential to oxidize anthracene in the presence of 1-hydroxybenzotriazole (HBT) was examined. Results indicated that the immobilization enhanced the stability of laccase against temperature, pH, inhibitors and loading time compared with the other cases. The immobilized laccase-mediator system was as efficient as the free enzyme for oxidizing the tested PAHs. After 24h. of incubation, immobilized laccase–HBT showed a system oxidization more than immobilized laccase without (HBT) of PAHs; Chitosan with hyacinth plant and (HBT) resulted better conversion than chitosan with or without HBT. These results indicate a new chance for applying the immobilized laccase in bioremediation.

scholarly journals The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix

2022 ◽  
Vol 2022 ◽  
pp. 1-7
Author(s):  
Yandri Yandri ◽  
Ezra Rheinsky Tiarsa ◽  
Tati Suhartati ◽  
Heri Satria ◽  
Bambang Irawan ◽  
...  
Keyword(s):  
Aspergillus Fumigatus ◽  
Half Life ◽  
Thermal Inactivation ◽  
Immobilized Enzyme ◽  
Residual Activity ◽  
Maximum Velocity ◽  
Partial Purification ◽  
Soluble Enzyme ◽  
Optimum Temperature ◽  
The Stability

The stability of the α-amylase enzyme has been improved from Aspergillus fumigatus using the immobilization method on a bentonite matrix. Therefore, this study aims to obtain the higher stability of α-amylase enzyme from A. fumigatus; hence, it is used repeatedly to reduce industrial costs. The procedures involved enzyme production, isolation, partial purification, immobilization, and characterization. Furthermore, the soluble enzyme was immobilized using 0.1 M phosphate buffer of pH 7.5 on a bentonite matrix, after which it was characterized with the following parameters such as optimum temperature, Michaelis constant (KM), maximum velocity V max , thermal inactivation rate constant (ki), half-life (t1/2), and the change of energy due to denaturation (ΔGi). The results showed that the soluble enzyme has an optimum temperature of 55°C, KM of 3.04 mg mL−1 substrate, V max of 10.90 μmole mL−1 min−1, ki of 0.0171 min−1, t1/2 of 40.53 min, and ΔGi of 104.47 kJ mole−1, while the immobilized enzyme has an optimum temperature of 70°C, KM of 8.31 mg mL−1 substrate, V max of 1.44 μmole mL−1 min−1, ki of 0.0060 min−1, t1/2 of 115.50 min, and ΔGi of 107.37 kJ mole−1. Considering the results, the immobilized enzyme retained 42% of its residual activity after six reuse cycles. Additionally, the stability improvement of the α-amylase enzyme by immobilization on a bentonite matrix, based on the increase in half-life, was three times greater than the soluble enzyme.

scholarly journals Fungal α-amylase entrapped in agar-agar organic matrix “beads” enhances fabric starch-desizing potentials and α-amylase-detergent compatibility

2021 ◽  
Author(s):  
Adedeji Nelson Ademakinwa ◽  
Zainab Adenike Ayinla ◽  
Femi Kayode Agboola
Keyword(s):  
Immobilized Enzyme ◽  
Residual Activity ◽  
Organic Matrix ◽  
Industrial Applications ◽  
Free Enzyme ◽  
Detergent Additive ◽  
Detergent Compatibility ◽  
Washing Efficiency ◽  
And Control ◽  
Catalytic Cycles

Abstract Aureobasidium pullulans α-amylase (ApAmy) mixed with melted agar-agar solution and drop-wisely added to a mixture of organic solvent solution allowed for the entrapment of the α-amylase in the agar-agar organic matrix as beads. The immobilized ApAmy’s characteristics and wash performance were elucidated in comparison with the soluble ApAmy. Agar-agar at 2.0 % (w/v) and toluene: chloroform at 3:1 resulted in the highest immobilization yield retaining about 98% residual activity after ten catalytic cycles. The optimum temperature and pH for the immobilized enzyme were 60ºC and 6.5 respectively. The immobilized ApAmy hydrolysed branched and linear substrates thus establishing its broad substrate specificity. Relatively, the immobilized ApAmy (iApAmy) was more tolerant to organic solvents than the free enzyme. The iApAmy was mildly inhibited by cobalt but metals such as zinc, manganese, calcium and sodium enhanced the free and immobilized ApAmy activity. The iApAmy had a higher washing efficiency (77%) in the presence of detergents than the free enzyme (68%) and control (36%). The iApAmy showed good potentials as a detergent additive and from its characteristics, it could be useful in other industrial applications.

Uniformity of Magnification from Different Electron Microscopes

1967 ◽  
Vol 25 ◽  
pp. 32-33
Author(s):  
Godfrey C. Hoskins ◽  
V. Williams ◽  
V. Allison
Keyword(s):  
Diffraction Grating ◽  
The Other ◽  
Carbon Replica ◽  
Electron Microscopes ◽  
The Stability

The method demonstrated is an adaptation of a proven procedure for accurately determining the magnification of light photomicrographs. Because of the stability of modern electrical lenses, the method is shown to be directly applicable for providing precise reproducibility of magnification in various models of electron microscopes.A readily recognizable area of a carbon replica of a crossed-line diffraction grating is used as a standard. The same area of the standard was photographed in Phillips EM 200, Hitachi HU-11B2, and RCA EMU 3F electron microscopes at taps representative of the range of magnification of each. Negatives from one microscope were selected as guides and printed at convenient magnifications; then negatives from each of the other microscopes were projected to register with these prints. By deferring measurement to the print rather than comparing negatives, correspondence of magnification of the specimen in the three microscopes could be brought to within 2%.

Immobilized Nanoparticles-Mediated Enzymatic Hydrolysis of Cellulose for Clean Sugar Production: A Novel Approach

2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai
Keyword(s):  
Catalytic Activity ◽  
Enzymatic Hydrolysis ◽  
Immobilized Enzyme ◽  
Free Enzyme ◽  
Magnetic Nanomaterials ◽  
Sugar Production ◽  
Cellulase Enzyme ◽  
Enzymatic Hydrolysis Of Cellulose ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.

scholarly journals Black Hole Algorithm for Sustainable Design of Counterfort Retaining Walls

2020 ◽  
Vol 12 (7) ◽  
pp. 2767 ◽  
Author(s):  
Víctor Yepes ◽  
José V. Martí ◽  
José García
Keyword(s):  
Black Hole ◽  
Sustainable Design ◽  
Retaining Walls ◽  
The Other ◽  
Trade Off ◽  
Construction Company ◽  
Geometric Variables ◽  
The Stability ◽  
The Cost ◽  
Black Hole Algorithm

The optimization of the cost and CO 2 emissions in earth-retaining walls is of relevance, since these structures are often used in civil engineering. The optimization of costs is essential for the competitiveness of the construction company, and the optimization of emissions is relevant in the environmental impact of construction. To address the optimization, black hole metaheuristics were used, along with a discretization mechanism based on min–max normalization. The stability of the algorithm was evaluated with respect to the solutions obtained; the steel and concrete values obtained in both optimizations were analyzed. Additionally, the geometric variables of the structure were compared. Finally, the results obtained were compared with another algorithm that solved the problem. The results show that there is a trade-off between the use of steel and concrete. The solutions that minimize CO 2 emissions prefer the use of concrete instead of those that optimize the cost. On the other hand, when comparing the geometric variables, it is seen that most remain similar in both optimizations except for the distance between buttresses. When comparing with another algorithm, the results show a good performance in optimization using the black hole algorithm.

scholarly journals Radiation-Induced Asymmetric Grafting of Different Monomers into Base Films to Prepare Novel Bipolar Membranes

Molecules ◽  
2021 ◽  
Vol 26 (7) ◽  
pp. 2028
Author(s):  
Shin-ichi Sawada ◽  
Yasunari Maekawa
Keyword(s):  
Acrylic Acid ◽  
Anion Exchange ◽  
Graft Polymerization ◽  
The Other ◽  
Practical Applications ◽  
Bipolar Membranes ◽  
Graft Polymers ◽  
Grafting Reactions ◽  
Radiation Induced

We prepared novel bipolar membranes (BPMs) consisting of cation and anion exchange layers (CEL and AEL) using radiation-induced asymmetric graft polymerization (RIAGP). In this technique, graft polymers containing cation and anion exchange groups were introduced into a base film from each side. To create a clear CEL/AEL boundary, grafting reactions were performed from each surface side using two graft monomer solutions, which are immiscible in each other. Sodium p-styrenesulfonate (SSS) and acrylic acid (AA) in water were co-grafted from one side of the base ethylene-co-tetrafluoroethylene film, and chloromethyl styrene (CMS) in xylene was simultaneously grafted from the other side, and then the CMS units were quaternized to afford a BPM. The distinct SSS + AA- and CMS-grafted layers were formed owing to the immiscibility of hydrophilic SSS + AA and hydrophobic CMS monomer solutions. This is the first BPM with a clear CEL/AEL boundary prepared by RIAGP. However, in this BPM, the CEL was considerably thinner than the AEL, which may be a problem in practical applications. Then, by using different starting times of the first SSS+AA and second CMS grafting reactions, the CEL and AEL thicknesses was found to be controlled in RIAGP.

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 A Fractional SAIDR Model in the Frame of Atangana–Baleanu Derivative

2021 ◽  
Vol 5 (2) ◽  
pp. 32
Author(s):  
Esmehan Uçar ◽  
Sümeyra Uçar ◽  
Fırat Evirgen ◽  
Necati Özdemir
Keyword(s):  
Existence And Uniqueness ◽  
Laplace Transformation ◽  
Cell Phones ◽  
Mobile Network ◽  
The Other ◽  
Banach Fixed Point Theorem ◽  
Propagation Models ◽  
Computer Worms ◽  
Computer Viruses ◽  
The Stability

It is possible to produce mobile phone worms, which are computer viruses with the ability to command the running of cell phones by taking advantage of their flaws, to be transmitted from one device to the other with increasing numbers. In our day, one of the services to gain currency for circulating these malignant worms is SMS. The distinctions of computers from mobile devices render the existing propagation models of computer worms unable to start operating instantaneously in the mobile network, and this is particularly valid for the SMS framework. The susceptible–affected–infectious–suspended–recovered model with a classical derivative (abbreviated as SAIDR) was coined by Xiao et al., (2017) in order to correctly estimate the spread of worms by means of SMS. This study is the first to implement an Atangana–Baleanu (AB) derivative in association with the fractional SAIDR model, depending upon the SAIDR model. The existence and uniqueness of the drinking model solutions together with the stability analysis are shown through the Banach fixed point theorem. The special solution of the model is investigated using the Laplace transformation and then we present a set of numeric graphics by varying the fractional-order θ with the intention of showing the effectiveness of the fractional derivative.

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