scholarly journals Characterization of EstDR4, a Novel Cold-Adapted Insecticides-Metabolizing Esterase from Deinococcus radiodurans

2021 ◽  
Vol 11 (4) ◽  
pp. 1864
Author(s):  
Yage Zhang ◽  
Wei Lu ◽  
Jin Wang ◽  
Ming Chen ◽  
Wei Zhang ◽  
...  
Keyword(s):  
Deinococcus Radiodurans ◽  
Tween 80 ◽  
Pharmaceutical Products ◽  
High Catalytic Activity ◽  
Biotechnological Applications ◽  
Optimum Temperature ◽  
Initial Activity ◽  
Cold Adapted ◽  
Triton X

Cold-adapted esterases are attracting increasing attention owing to their prospective use in biotechnology. In this study, a novel cold-adapted family Ⅳ esterase EstDR4 was identified and obtained from extremophile Deinococcus radiodurans (D. radiodurans). EstDR4 displayed significant substrate preference towards short and medium chain monoesters (C2–C12). It also showed regioselectivity, enantioselectivity and degradation effects on four insecticides. The optimum temperature and pH for EstDR4 activity were 30 °C and pH 8, respectively. Additionally, EstDR4 exhibited relatively high catalytic activity at 0 °C and high stability from 10–40 °C, with over 80% of its initial activity retained after 1 h of incubation. Moreover, EstDR4 activity was stimulated by Tween 80 and Triton X-100, and inhibited by metal ions such as Co2+, Cu2+ and Zn2+ and several organic solvents. Thus, this enzyme shows development potential for many industrial biotechnological applications, including the manufacture of thermolabile pharmaceutical products, cold-wash detergents and insecticide biodegradation.

scholarly journals Investigation on a Bangladeshi isolate Bacillus aryabhattai for promising biotechnological applications

2018 ◽  
Vol 7 (2) ◽  
pp. 33-45
Author(s):  
Mohammad Shahedur Rahman ◽  
Rasheda Banu ◽  
Ripa Moni ◽  
Nazmul Islam ◽  
Mastura Khatun Ruma ◽  
...  
Keyword(s):  
Soil Sample ◽  
Extracellular Enzymes ◽  
Extreme Conditions ◽  
Biotechnological Applications ◽  
Optimum Temperature ◽  
First Report ◽  
Bacillus Aryabhattai ◽  
Physico Chemical ◽  
Chemical Studies

A new isolate was investigated from soil sample collected from Shahrasti upazilla of Chandpur district of Bangladesh. Based on the physico-chemical studies the strain was identified as gram positive Bacilli. Moleculer characterization of the strain was identified as Bacillus aryabhattai which is the first report in Bangladesh. The strain can survive in extreme conditions of salt, temperature and pH. This strain was further characterized and screened for the ability to produce useful enzymes. The optimum temperature for growth and production of these enzymes was within the temperature range 35oC to 40oC. The pH was found to be 7 for its growth and production of different enzymes when investigated over 48 h of incubation. The isolate produced various extracellular enzymes such as α-amylases, cellulases, β-glucosidases, lipases and proteases. The findings of this study provide useful information of the new strain that has potential biotechnological applications. Jahangirnagar University J. Biol. Sci. 7(2): 33-45, 2018 (December)

scholarly journals Synthesis and Characterization of Surfactant Assisted Copper Nanomaterials

2020 ◽  
Vol 32 (11) ◽  
pp. 2700-2706
Author(s):  
P. Murali Krishna ◽  
K. Hussain Reddy ◽  
N. Rashmitha ◽  
M. Sravanthi ◽  
D. Sujathamma
Keyword(s):  
Low Cost ◽  
Spherical Shape ◽  
Tween 80 ◽  
Synthesis And Characterization ◽  
Synthetic Method ◽  
Ft Ir ◽  
Uv Visible ◽  
Triton X ◽  
Surfactant Assisted

In this work, a simple and low cost synthetic method for four different copper nanomaterials having uniform shape and size using copper(II) acetate and cis-bis(glycinato)copper(II) complex in presence of non-ionic surfactants Tween-80 and Triton X-100 in the presence of ascorbic acid as reducing agent is described. The synthesized nanomaterials were characterized using FT-IR, UV-visible, powder XRD, EDX and SEM techniques. The characterization data reveals that all the copper nanomaterials formed are less than 30 nm size with spherical shape.

scholarly journals Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

Catalysts ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 181 ◽  
Author(s):  
Wesam H. Abdulaal ◽  
Yaaser Q. Almulaiky ◽  
Reda M. El-Shishtawy
Keyword(s):  
Metal Ions ◽  
Immobilized Enzyme ◽  
Pmma Film ◽  
Optimum Temperature ◽  
Initial Activity ◽  
Casting Method ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Triton X ◽  
Enzyme Changes

Horseradish peroxidase (HRP) enzyme was effectively encapsulated onto an Fe3O4 nanoparticle–polymethyl methacrylate (PMMA) film via the casting method. The HRP was immobilized on the 0.5% Fe3O4Np–PMMA film and characterized by Fourier transform infrared spectroscopy and field emission scanning electron microscopy. Moreover, the reusability, thermal stability, optimum pH, optimum temperature, the influence of metal ions, and the effects of detergent and organic solvent were investigated. After optimizing the immobilization conditions, the highest efficiency of the immobilized enzyme was 88.4% using 0.5% Fe3O4Np–PMMA. The reusability of the immobilized HRP activity was 78.5% of its initial activity after being repeatedly used for 10 cycles. When comparing the free and immobilized forms of the HRP enzyme, changes in the optimum temperature and optimum pH from 30 to 40 °C and 7.0 to 7.5, respectively, were observed. The Km and Vmax for the immobilized HRP were estimated to be 41 mM, 0.89 U/mL for guaiacol and 5.84 mM, 0.66 U/mL for H2O2, respectively. The high stability of the immobilized HRP enzyme was obtained using metal ions, a high urea concentration, isopropanol, and Triton X-100. In conclusion, the applicability of immobilized HRP involves the removal of phenol in the presence of hydrogen peroxide, therefore, it could be a potential catalyst for the removal of wastewater aromatic pollutants.

scholarly journals CHARACTERIZATION OF PREDICTED BACTERIAL COLD-ADAPTED LIPASE FROM SEAFOOD COLD STORAGE

2022 ◽  
Vol 9 (12) ◽  
pp. 242-250
Author(s):  
Hefti Salis Yufidasari ◽  
Retno Tri Astuti ◽  
Eko Waluyo ◽  
Jekmal Malau
Keyword(s):  
Cold Storage ◽  
Unique Feature ◽  
Lipolytic Activity ◽  
Production Costs ◽  
Addition Reactions ◽  
Optimum Temperature ◽  
Cold Temperatures ◽  
Cold Adapted ◽  
Lower Production

Lipases constitute as top three most important group of enzymes along with  carbohydrases and proteases, and are widely used in various industries. In particular, lipase that perform high activity at low temperatures, or referred as cold adapted lipase (CLPs) considered as attractive catalyst due to its activity at low temperature. This unique feature is the main advantage of cold adapted lipase utilization because it requires a low energy source that is correlated with lower production costs and energy. In addition, reactions occur in cold temperatures may result in better product quality. The purpose of this research was to perform screening and characterization of bacterial cold adapted lipase from seafood cold storage. Among 53 isolates, Kr_16_30, TI_37_14 and Kr_16_28 showed the highest activity with 4.12 U/mL; 3.87 U/mL and 3.21 U/mL, respectively. Isolates Kr_16_30 seemed to be typical cold adapted lipase with optimum temperature at 20°C and pH 7. Isolates Kr_16_28 performed highest lipolytic activity at 30°C while TI_37_14 suspected to be similar to typical mesophilic lipase with optimum temperature at 40°C. Species identification based on 16s rRDA sequencing revealed that isolates Kr_16 30 and Kr_16 28 are belong to genus Pseudomonas and Bacillus, repectively.

Refolding and Activation from Bacterial Inclusion Bodies of Trypsin I from Sardine (Sardinops sagax caerulea)

2019 ◽  
Vol 26 (3) ◽  
pp. 170-175
Author(s):  
Manuel I. Carretas-Valdez ◽  
Francisco J. Cinco-Moroyoqui ◽  
Marina J. Ezquerra-Brauer ◽  
Enrique Marquez-Rios ◽  
Idania E. Quintero-Reyes ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Inclusion Bodies ◽  
Recombinant Expression ◽  
Luria Broth ◽  
Biotechnological Applications ◽  
Trypsin Activity ◽  
Biophysical Characterization ◽  
Cold Adapted ◽  
Sardinops Sagax

Background: Trypsin from fish species is considered as a cold-adapted enzyme that may find potential biotechnological applications. In this work, the recombinant expression, refolding and activation of Trypsin I (TryI) from Monterey sardine (Sardinops sagax caerulea) are reported. Methods: TryI was overexpressed in Escherichia coli BL21 as a fusion protein of trypsinogen with thioredoxin. Refolding of trypsinogen I was achieved by dialysis of bacterial inclusion bodies with a recovery of 16.32 mg per liter of Luria broth medium. Results: Before activation, the trypsinogen fusion protein did not show trypsin activity. Trypsinogen I was activated by adding 0.002 U of native TryI purified from the sardine pyloric caeca (nonrecombinant). The activated recombinant trypsin showed three times more activity than the nonrecombinant trypsin alone. Conclusion: The described protocol allowed obtaining sufficient amounts of recombinant TryI from Monterey sardine fish for further biochemical and biophysical characterization of its coldadaptation parameters.

scholarly journals Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

2010 ◽  
Vol 53 (1) ◽  
pp. 35-45 ◽  
Author(s):  
Arlem Nascimento de Oliveira ◽  
Luiz Antonio de Oliveira ◽  
Jerusa Souza Andrade
Keyword(s):  
Amylase Activity ◽  
Tween 80 ◽  
Inhibitory Effect ◽  
Partial Characterization ◽  
Exponential Growth Phase ◽  
Enzyme Preparations ◽  
Amylase Production ◽  
Ph Range ◽  
Triton X

Amylase production and partial characterization of crude enzyme preparations from two rhizobia strains (R-926 and R-991) were evaluated. For both the strains, maximal amylase activities were achieved during the early-to-mid- exponential growth phase; both were active over a pH range from 4.5 to 8.5 and temperature from 30 to 50 ºC. None of the ions studied (K+, Na+, Ca2+, Hg2+, Mg2+, Mn2+, Cu2+ and Zn2+) was required for the catalytic activity of strain R-926; amylase activity of strain R-991 was stimulated in the presence of K+, Hg2+ and Zn2+. The surfactants SDS, Triton X-100 and Tween-80 did not have a pronounced inhibitory effect on enzyme activities; SDS and Tween-80 caused the highest stimulatory effects. Amylase activities from the rhizobia strains were reduced by up to 30% in the presence of EDTA; amylase activity of R-926 was also inhibited by HgCl2, suggesting that Ca2+and cysteine residues could be important for activity of this strain.

scholarly journals Characterization of the Recombinant Thermostable Lipase (Pf2001) from Pyrococcus furiosus: Effects of Thioredoxin Fusion Tag and Triton X-100

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Sylvia Maria Campbell Alquéres ◽  
Roberta Vieira Branco ◽  
Denise Maria Guimarães Freire ◽  
Tito Lívio Moitinho Alves ◽  
Orlando Bonifácio Martins ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Enzyme Activity ◽  
Specific Activity ◽  
Pyrococcus Furiosus ◽  
Optimum Temperature ◽  
Optimal Temperature ◽  
Thermostable Lipase ◽  
Fusion Tag ◽  
Triton X

In this work, the lipase from Pyrococcus furiosus encoded by ORF PF2001 was expressed with a fusion protein (thioredoxin) in Escherichia coli. The purified enzymes with the thioredoxin tag (TRX−PF2001Δ60) and without the thioredoxin tag (PF2001Δ60) were characterized, and various influences of Triton X-100 were determined. The optimal temperature for both enzymes was 80°C. Although the thioredoxin presence did not influence the optimum temperature, the TRX−PF2001Δ60 presented specific activity twice lower than the enzyme PF2001Δ60. The enzyme PF2001Δ60 was assayed using MUF-acetate, MUF-heptanoate, and MUF-palmitate. MUF-heptanoate was the preferred substrate of this enzyme. The chelators EDTA and EGTA increased the enzyme activity by 97 and 70%, respectively. The surfactant Triton X-100 reduced the enzyme activity by 50% and lowered the optimum temperature to 60°C. However, the thermostability of the enzyme PF2001Δ60 was enhanced with Triton X-100.

A Simple, Green and Fast Ultraviolet Spectrophotometric Method for the Carbamide Peroxide Determination in Dental Whitening Products

2019 ◽  
Vol 15 (2) ◽  
pp. 138-144
Author(s):  
Fabiana Vieira Lima ◽  
Aline Farias ◽  
Cassiana Mendes ◽  
Simone Gonçalves Cardoso ◽  
Marcos Antônio Segatto Silva
Keyword(s):  
Hydrogen Peroxide ◽  
Pharmaceutical Products ◽  
Reference Solution ◽  
Iodometric Titration ◽  
Carbamide Peroxide ◽  
Ultraviolet Detection ◽  
Water As Solvent ◽  
Development And Validation ◽  
Dental Whitening

Background: The carbamide peroxide is the most commonly active ingredient used for home dental whitening products, its quantification in pharmaceutical products is of extreme importance due to the relation with the products potency and the previously related low carbamide peroxide stability. Once, there is only one official carbamide peroxide determination based on iodometric titration, this method is time-consuming and generates a lot of residues. The aim of this study was to carry out development and validation of a simple and fast ultraviolet spectrophotometer assay to quantify an innovative dental whitening gel. Methods: The proposed method was validated according international conference on harmonization guideline. Procedure is based on the iodide/iodine redox chemistry; iodine released through the action of hydrogen peroxide of carbamide peroxide with ultraviolet detection at 350 nm. Results: The procedure was linear in the concentration range of 1.0-4.0 µg/mL, specific to the excipients, robust for the evaluated parameters (variation of wavelength (± 5 nm); reagent addition (± 10%)), showing the results of RSD 1.88 and 0.39% respectively. Repeatability precision was RSD = 1.42%, with accurate RSD = 2.15% by adding reference solution. The assay used only water as solvent for sample preparation. In comparison to the pharmacopeial method, the latter is more time-consuming, as it generates a lot of residues, and it could not quantify small CP dosages. Conclusion: Thus, the proposed method was proved to be suitable to determine carbamide peroxide during the development and characterization of nanoparticle formulations in the present study.

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