Preparation of aqueous polyaniline-vesicle suspensions with class III peroxidases. Comparison between horseradish peroxidase isoenzyme C and soybean peroxidase

2013 ◽  
Vol 67 (8) ◽  
Author(s):  
Katja Junker ◽  
Ivan Gitsov ◽  
Nick Quade ◽  
Peter Walde
Keyword(s):  
Horseradish Peroxidase ◽  
Enzyme Stability ◽  
Class Iii ◽  
Salt Form ◽  
Reaction Conditions ◽  
Soybean Peroxidase ◽  
Peroxidase Isoenzyme ◽  
Complete Inactivation ◽  
Class Iii Peroxidases ◽  
Optimal Reaction

AbstractAniline was polymerised enzymatically in aqueous solution at pH = 4.3 and 25°C in the presence of submicrometer-sized vesicles formed from sodium bis(2-ethylhexyl)sulphosuccinate (AOT). H2O2 served as oxidant and the enzyme used was either horseradish peroxidase isoenzyme C (HRPC) or soybean peroxidase (SBP), both being class III peroxidases. From previous studies with HRPC, it is known that stable vesicle suspensions containing the emeraldine salt form of polyaniline (PANI-ES) can be obtained within 1–2 days with a 90–95 % yield, provided that optimal reaction conditions are applied. Unfortunately, HRPC becomes inactivated during polymerisation. In the present study, a linear dendritic block copolymer was added to HRPC, resulting in higher operational enzyme stability; the stabilising effect, however, was too small to afford a substantial decrease in the required amount of enzyme. Moreover, replacing HRPC with SBP was of no advantage, although SBP is known to be more stable towards inactivation by H2O2 than HRPC. By contrast, SBP was found to be much slower in oxidising aniline, and complete inactivation of SBP occurred before all the aniline monomers were oxidised, leading to low yields and the formation of over-oxidised products. The same was observed for HRP isoenzyme A2. Reactions without vesicles indicated that peroxidase inactivation was probably caused by PANI-ES.

scholarly journals Effect of template type on the preparation of the emeraldine salt form of polyaniline (PANI-ES) with horseradish peroxidase isoenzyme C (HRPC) and hydrogen peroxide

RSC Advances ◽  
2019 ◽  
Vol 9 (57) ◽  
pp. 33080-33095 ◽  
Author(s):  
Tomoyuki Fujisaki ◽  
Keita Kashima ◽  
Sandra Serrano-Luginbühl ◽  
Reinhard Kissner ◽  
Danica Bajuk-Bogdanović ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Emeraldine Salt ◽  
Salt Form ◽  
Peroxidase Isoenzyme ◽  
Different Types

Different types of templates consisting of sulfonate or sulfate groups were compared for the horseradish peroxidase/H2O2-catalysed synthesis of the emeraldine salt form of polyaniline from aniline at pH = 4.3.

scholarly journals Influence of temperature on the enzymic semisynthesis of human insulin by coupling and transpeptidation methods

1986 ◽  
Vol 240 (3) ◽  
pp. 803-810 ◽  
Author(s):  
K Morihara ◽  
Y Ueno ◽  
K Sakina
Keyword(s):  
Human Insulin ◽  
Temperature Effects ◽  
Enzyme Stability ◽  
Product Yield ◽  
Reaction Conditions ◽  
Influence Of Temperature ◽  
Influence Of Temperature On ◽  
The Stability ◽  
Complex Temperature ◽  
Optimal Reaction

The influence of temperature of enzymic semisynthesis of human insulin ester was determined by using coupling and transpeptidation methods with trypsin and Achromobacter lyticus proteinase I as catalysts. The optimal reaction conditions were studied at the selected temperatures of 25, 12 and 4 degrees C. The results showed that the synthesis rates by both methods with trypsin increased as the temperature increased, but the final product yield correspondingly decreased. Therefore the reaction with trypsin should be done below 12 degrees C, preferably at 4 degrees C. This agrees well with the stability of trypsin at these temperatures. When the catalyst was Achromobacter lyticus proteinase I, no such complex temperature effects were observed, and the findings indicated that the reactions should be conducted below 37 degrees C for enzyme stability.

Synthesis of Phosphonates via Michaelis-Arbuzov Reaction

2017 ◽  
Vol 14 (6) ◽  
pp. 883-903 ◽  
Author(s):  
Boppudi Hari Babu ◽  
Gandavaram Syam Prasad ◽  
Chamarthi Naga Raju ◽  
Mandava Venkata Basaveswara Rao
Keyword(s):  
Reaction Times ◽  
Biologically Active ◽  
Fine Tuning ◽  
Arbuzov Reaction ◽  
Reaction Conditions ◽  
Solvent Type ◽  
Potential Applications ◽  
Synthetic Methodologies ◽  
Optimal Reaction ◽  
The Arbuzov Reaction

Background: Michaelis–Arbuzov reaction has played a key role for the synthesis of dialkyl or diaryl phosphonates by reacting various alkyl or aryl halides with trialkyl or triaryl phosphite. This reaction is very versatile in the formation of P-C bond from the reaction of aliphatic halides with phosphinites or phosphites to yield phosphonates, phosphinates, phosphine oxides. The Arbuzov reaction developed some methodologies, possible mechanistic pathways, selectivity, potential applications and biologically active various phosphonates. Objective: The synthesis of phosphonates via Michaelis–Arbuzov reaction with many new and fascinating methodologies were developed and disclosed in the literature, and these are explored in this review. Conclusion: This review has discussed past developments and vast potential applications of Arbuzov reaction in the synthesis of organophosphonates. As presented in this review, various synthetic methodologies were developed to prepare a large variety of phosphonates. Improvements in the reaction conditions of Lewis-acid mediated Arbuzov rearrangement as well as the development of MW-assisted Arbuzov rearrangement were discussed. Finally, to achieve high selectivities and yields, fine-tuning of reaction conditions including solvent type, temperature, and optimal reaction times to be considered.

Amperometric assay of vitamin C using an ascorbate oxidase enzyme electrode

1979 ◽  
Vol 44 (11) ◽  
pp. 3395-3404 ◽  
Author(s):  
Pavel Posádka ◽  
Lumír Macholán
Keyword(s):  
Ascorbic Acid ◽  
Vitamin C ◽  
Oxygen Electrode ◽  
Ascorbate Oxidase ◽  
Current Response ◽  
Reaction Conditions ◽  
Long Term Storage ◽  
Oxidase Enzyme ◽  
Optimal Reaction

An oxygen electrode of the Clark type, coated by a thin, active layer of chemically insolubilized ascorbate oxidase from squash peelings specifically detects by measuring oxygen uptake 10 to 400 μg of ascorbic acid in 3 ml of phosphate buffer. The record of current response to substrate addition lasts 1-2 min. The ascorbic acid values determined in various samples of fruit juices are in good agreement with the data obtained by titration and polarography. The suitable composition of the membrane and its lifetime and stability during long-term storage are described; optimal reaction conditions of vitamin C determination and the possibilities of interference of other compounds are also examined. Of the 35 phenols, aromatic amines and acids tested chlorogenic acid only can cause a positive error provided that the enzyme membrane has been prepared from ascorbate oxidase of high purity.

scholarly journals A Novel Pseudomonas geniculata AGE Family Epimerase/Isomerase and Its Application in d-Mannose Synthesis

Foods ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 1809
Author(s):  
Zhanzhi Liu ◽  
Ying Li ◽  
Jing Wu ◽  
Sheng Chen
Keyword(s):  
3D Structure ◽  
Three Dimensional ◽  
Optimal Temperature ◽  
Reaction Conditions ◽  
Enzymatic Production ◽  
Physiological Properties ◽  
Potential Applications ◽  
Kinetics Of ◽  
Optimal Reaction ◽  
Gene Age

d-mannose has exhibited excellent physiological properties in the food, pharmaceutical, and feed industries. Therefore, emerging attention has been applied to enzymatic production of d-mannose due to its advantage over chemical synthesis. The gene age of N-acetyl-d-glucosamine 2-epimerase family epimerase/isomerase (AGEase) derived from Pseudomonas geniculata was amplified, and the recombinant P. geniculata AGEase was characterized. The optimal temperature and pH of P. geniculata AGEase were 60 °C and 7.5, respectively. The Km, kcat, and kcat/Km of P. geniculata AGEase for d-mannose were 49.2 ± 8.5 mM, 476.3 ± 4.0 s−1, and 9.7 ± 0.5 s−1·mM−1, respectively. The recombinant P. geniculata AGEase was classified into the YihS enzyme subfamily in the AGE enzyme family by analyzing its substrate specificity and active center of the three-dimensional (3D) structure. Further studies on the kinetics of different substrates showed that the P. geniculata AGEase belongs to the d-mannose isomerase of the YihS enzyme. The P. geniculata AGEase catalyzed the synthesis of d-mannose with d-fructose as a substrate, and the conversion rate was as high as 39.3% with the d-mannose yield of 78.6 g·L−1 under optimal reaction conditions of 200 g·L−1d-fructose and 2.5 U·mL−1P. geniculata AGEase. This novel P. geniculata AGEase has potential applications in the industrial production of d-mannose.

scholarly journals Efficient Degradation of Mordant Blue 9 Using the Fenton-Activated Persulfate System

Water ◽  
2019 ◽  
Vol 11 (12) ◽  
pp. 2532 ◽  
Author(s):  
Md. Nahid Pervez ◽  
Felix Y. Telegin ◽  
Yingjie Cai ◽  
Dongsheng Xia ◽  
Tiziano Zarra ◽  
...  
Keyword(s):  
Butyl Alcohol ◽  
Textile Dye ◽  
Oh Radicals ◽  
Operational Parameters ◽  
Reaction Conditions ◽  
Tert Butyl Alcohol ◽  
Initial Ph ◽  
Fe Complex ◽  
Optimal Reaction ◽  
Activated Persulfate

In this study, a Fenton-activated persulfate (Fe2+/PS) system was introduced for the efficient degradation of Mordant Blue 9 (MB 9) as a textile dye in an aqueous solution. Results showed that the degradation of MB 9 was markedly influenced by operational parameters, such as initial pH, PS concentration, Fe2+ concentration, and initial dye concentration. Optimal reaction conditions were then determined. Inorganic anions, such as Cl− and HCO3−, enhanced the degradation efficiency of MB 9 under optimal conditions. Addition of HCO3− reduced the degradation performance of MB 9, whereas the addition of Cl− increased the degradation percentage of MB 9. In addition, quenching experiments were conducted using methanol and tert-butyl alcohol as scavengers, and methanol was identified as an effective scavenger. Thus, the degradation of MB 9 was attributed to S O 4 • − and •OH radicals. The degradation and mineralization efficiency of MB 9 was significantly reduced using the conventional Fenton process i.e., Fe2+/ hydrogen peroxide (HP) because of the formation of a Fe complex during degradation. Meanwhile, the Fe2+/persulfate (PS) system improved the degradation and mineralization performance.

scholarly journals Software-guided microscale flow calorimeter for efficient acquisition of thermokinetic data

2021 ◽  
Author(s):  
Timothy Aljoscha Frede ◽  
Marlene Dietz ◽  
Norbert Kockmann
Keyword(s):  
Design Of Experiments ◽  
Process Development ◽  
Reaction Conditions ◽  
Experimental Conditions ◽  
Flow Calorimeter ◽  
Microscale Flow ◽  
Increased Sensitivity ◽  
Important Time ◽  
Optimal Reaction

AbstractFast chemical process development is inevitably linked to an optimized determination of thermokinetic data of chemical reactions. A miniaturized flow calorimeter enables increased sensitivity when examining small amounts of reactants in a short time compared to traditional batch equipment. Therefore, a methodology to determine optimal reaction conditions for calorimetric measurement experiments was developed and is presented in this contribution. Within the methodology, short-cut calculations are supplemented by computational fluid dynamics (CFD) simulations for a better representation of the hydrodynamics within the microreactor. This approach leads to the effective design of experiments. Unfavourable experimental conditions for kinetics experiments are determined in advance and therefore, need not to be considered during design of experiments. The methodology is tested for an instantaneous acid-base reaction. Good agreement of simulations was obtained with experimental data. Thus, the prediction of the hydrodynamics is enabled and the first steps towards a digital twin of the calorimeter are performed. The flow rates proposed by the methodology are tested for the determination of reaction enthalpy and showed that reasonable experimental settings resulted. Graphical abstract A methodology is suggested to evaluate optimal reaction conditions for efficientacquisition of kinetic data. The experimental design space is limited by thestepwise determination of important time scales based on specified input data.

scholarly journals Genome-wide identification and analysis of class III peroxidases in Betula pendula

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Kewei Cai ◽  
Huixin Liu ◽  
Song Chen ◽  
Yi Liu ◽  
Xiyang Zhao ◽  
...  
Keyword(s):  
Stress Responses ◽  
Betula Pendula ◽  
Expression Patterns ◽  
Class Iii ◽  
Physiological Processes ◽  
Plant Life ◽  
Genome Wide ◽  
Plant Life Cycle ◽  
Class Iii Peroxidases ◽  
And Function

Abstract Background Class III peroxidases (POD) proteins are widely present in the plant kingdom that are involved in a broad range of physiological processes including stress responses and lignin polymerization throughout the plant life cycle. At present, POD genes have been studied in Arabidopsis, rice, poplar, maize and Chinese pear, but there are no reports on the identification and function of POD gene family in Betula pendula. Results We identified 90 nonredundant POD genes in Betula pendula. (designated BpPODs). According to phylogenetic relationships, these POD genes were classified into 12 groups. The BpPODs are distributed in different numbers on the 14 chromosomes, and some BpPODs were located sequentially in tandem on chromosomes. In addition, we analyzed the conserved domains of BpPOD proteins and found that they contain highly conserved motifs. We also investigated their expression patterns in different tissues, the results showed that some BpPODs might play an important role in xylem, leaf, root and flower. Furthermore, under low temperature conditions, some BpPODs showed different expression patterns at different times. Conclusions The research on the structure and function of the POD genes in Betula pendula plays a very important role in understanding the growth and development process and the molecular mechanism of stress resistance. These results lay the theoretical foundation for the genetic improvement of Betula pendula.

scholarly journals Synthesis of propylene carbonate from urea and 1,2-propylene glycol over metal carbonates

2011 ◽  
Vol 17 (3) ◽  
pp. 323-331 ◽  
Author(s):  
Jiancheng Zhou ◽  
Wu Dongfang ◽  
Birong Zhang ◽  
Yali Guo
Keyword(s):  
Reaction Time ◽  
Propylene Glycol ◽  
Propylene Carbonate ◽  
Reaction Temperature ◽  
Reaction Conditions ◽  
Lead Carbonate ◽  
Synthetic Process ◽  
Metal Carbonates ◽  
Optimal Reaction ◽  
Mixed Carbonate

A series of single-metal carbonates and Pb-Zn mixed-metal carbonates were prepared as catalysts for alcoholysis of urea with 1,2-propylene glycol (PG) for the synthesis of propylene carbonate (PC). The mixed carbonates all show much better catalytic activities than the single carbonates, arising from a strong synergistic effect between the two crystalline phases, hydrozincite and lead carbonate. The mixed carbonate with Pb/Zn=1:2 gives the highest yield of PC, followed by the mixed carbonate with Pb/Zn=1:3. Furthermore, Taguchi method was used to optimize the synthetic process for improving the yield of PC. It is shown that the reaction temperature is the most significant factor affecting the yield of PC, followed by the reaction time, and that the optimal reaction conditions are the reaction time at 5 hours, the reaction temperature at 180 oC and the catalyst amount at 1.8 wt%, resulting in the highest PC yield of 96.3%.

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