Efficiency of Carbohydrate Additives on the Stability of Horseradish Peroxidase (HRP): HRP-Catalyzed Removal of Phenol and Malachite Green Decolorization from Wastewater

2014 ◽  
Vol 43 (6) ◽  
pp. 846-856 ◽  
Author(s):  
Ellappan Kalaiarasan ◽  
Thayumanavan Palvannan
Keyword(s):  
Horseradish Peroxidase ◽  
Malachite Green ◽  
The Stability

scholarly journals METHODS FOR THE STUDY OF SMALL PHAGOSOMES AND THEIR RELATIONSHIP TO LYSOSOMES WITH HORSERADISH PEROXIDASE AS A "MARKER PROTEIN"

1967 ◽  
Vol 15 (7) ◽  
pp. 375-380 ◽  
Author(s):  
WERNER STRAUS
Keyword(s):  
Acid Phosphatase ◽  
Low Temperature ◽  
Horseradish Peroxidase ◽  
Acid Medium ◽  
Tissue Section ◽  
Double Staining ◽  
Marker Protein ◽  
Polar Media ◽  
The Stability ◽  
Blue Reaction

Small phagosomes (micropinocytic vesicles and vacuoles) which had taken up injected horseradish peroxidase were identified by staining for peroxidase with benzidine and H2O2. Because of the small size of the granules and the possibility of artifacts, previously described procedures had to be modified in several respects. Prefixation of the tissue by perfusion at 37°C prevented artifacts of diffusion and adsorption of peroxidase. The blue product of the reaction of peroxidase with benzidine in the small phagosomes was preserved and fading to brown was prevented by cooling the tissue section to –10° to –15°C during its processing through polar media. The blue reaction product was stable as soon as the section was transferred to an apolar medium. Small phagosomes were visualized together with lysosomes and phago-lysosomes in the same cells by double staining for acid phosphatase and peroxidase in contrasting colors. The incubation for acid phosphatase was performed at 4°C since low temperature increased the stability of peroxidase in the acid medium. Factors which form the basis for other improvements of the procedure are discussed.

scholarly journals Engineered Stable 5-Hydroxymethylfurfural Oxidase (HMFO) from 8BxHMFO Variant of Methylovorus sp. MP688 through B-Factor Analysis

Catalysts ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1503
Author(s):  
Qiuyang Wu ◽  
Dong Lu ◽  
Shuming Jin ◽  
Jie Lu ◽  
Fang Wang ◽  
...  
Keyword(s):  
Factor Analysis ◽  
Protein Structure ◽  
Hydrogen Bonds ◽  
Horseradish Peroxidase ◽  
Dynamic Simulation ◽  
Terephthalic Acid ◽  
Biotechnological Processes ◽  
The Stability ◽  
Work Stability ◽  
Low Activity

What is known as Furan-2,5-dicarboxylic acid (FDCA) is an attractive compound since it has similar properties to terephthalic acid. Further, 5-hydroxymethylfurfural oxidase (HMFO) is an enzyme, which could convert HMF to FDCA directly. Most wild types of HMFO have low activity on the oxidation of HMF to FDCA. The variant of 8BxHFMO from Methylovorus sp. MP688 was the only reported enzyme that was able to perform FDCA production. However, the stabilization of 8BxHMFO is still not that satisfactory, and further improvement is necessary for the industrial application of the enzyme. In this work, stability-enhanced HMFO from 8BxHFMO was engineered through employing B-factor analysis. The mutation libraries were created based on the NNK degeneracy of residues with the top ten highest B-factor value, and two of the effective mutants were screened out through the high throughput selection with the horseradish peroxidase (HRP)-Tyr assay. The mutants Q319K and N44G show a significantly increased yield of FDCA in the reaction temperature range of 30 to 40 °C. The mutant Q319K shows the best performance at 35 °C with a FDCA yield of 98% (the original 8BxHMFO was only 85%), and a half-life exceeding 72 h. Moreover, molecular dynamic simulation indicates that more hydrogen bonds are formed in the mutants, which improves the stability of the protein structure. The method could enhance the design of more stable biocatalysts; and provides potential for the further optimization and utilization of HMFO in biotechnological processes.

scholarly journals An accomplished procedure of horseradish peroxidase immobilization for removal of acid yellow 11 in aqueous solutions

2020 ◽  
Vol 81 (12) ◽  
pp. 2664-2673 ◽  
Author(s):  
Melda Altikatoglu Yapaoz ◽  
Azade Attar
Keyword(s):  
Horseradish Peroxidase ◽  
Storage Stability ◽  
Dye Degradation ◽  
Residual Activity ◽  
Immobilized Enzymes ◽  
The Novel ◽  
Optimum Temperature ◽  
Short Term ◽  
Waste Effluents ◽  
The Stability

Abstract Horseradish peroxidase (HRP) characteristics were improved by two techniques, Na-alginate entrapment and glutaraldehyde crosslinking prior to alginate entrapment, in order to enhance the stability, functionality and removal of dyes in waste water. Free, entrapped and crosslinked-entrapped enzymes were compared by activity assays, which indicated the optimum temperature is 25 °C and pH 4.0–5.0. Kinetics results showed that alginate entrapment and crosslinking prior to entrapment increased Vmax and did not cause any significant decrease in Km. The thermal resistance of the free enzyme was short-term, zero residual activity after 250 min, while the immobilized enzymes preserved more than 50% of their activity for 5 h at 60 °C. Immobilized HRP was resistant to methanol, ethanol, DMSO and THF. The storage stability of free HRP ended in 35 days whereas entrapped and crosslinked-entrapped HRPs had 87 and 92% residual activity at the 60th day, respectively. HRP was used in the decolorization of azo dye Acid yellow 11 and total decolorization (>99%) was obtained using crosslinked-entrapped HRP. Reusability studies presented the improvement that crosslinked-entrapped HRP reached 74% decolorization after 10 batches. The results demonstrated that the novel immobilized HRP can be used as an effective catalyst for dye degradation of industrial waste effluents.

scholarly journals Chemically glycosylation improves the stability of an amperometric horseradish peroxidase biosensor

2015 ◽  
Vol 854 ◽  
pp. 129-139 ◽  
Author(s):  
Griselle Hernández-Cancel ◽  
Damaris Suazo-Dávila ◽  
Johnsue Medina-Guzmán ◽  
María Rosado-González ◽  
Liz M. Díaz-Vázquez ◽  
...  
Keyword(s):  
Horseradish Peroxidase ◽  
The Stability

Additive Effect of Dextrans on the Stability of Horseradish Peroxidase

2011 ◽  
Vol 30 (2) ◽  
pp. 84-90 ◽  
Author(s):  
Melda Altikatoglu ◽  
Yeliz Basaran
Keyword(s):  
Horseradish Peroxidase ◽  
Additive Effect ◽  
The Stability

scholarly journals Mg-Al/Biochar Composite with Stable Structure for Malachite Green Adsorption from Aqueous Solutions

2021 ◽  
Vol 16 (1) ◽  
pp. 149-160
Author(s):  
Arini Fousty Badri ◽  
Patimah Mega Syah Bahar Nur Siregar ◽  
Neza Rahayu Palapa ◽  
Risfidian Mohadi ◽  
Mardiyanto Mardiyanto ◽  
...  
Keyword(s):  
Malachite Green ◽  
Physical Adsorption ◽  
Stable Structure ◽  
Maximum Adsorption Capacity ◽  
X Ray Diffraction ◽  
Effects Of Temperature ◽  
The Stability ◽  
Double Hydroxide ◽  
Adsorption Desorption ◽  
Open Access Article

Mg-Al-layered double hydroxide (LDH) was fabricated using a coprecipitation method at pH 10. Thereafter, Mg-Al-LDH was impregnated with biochar to manufacture a Mg-Al/Biochar composite. The composite was characterized using powder X-ray diffraction (XRD), Fourier-transform infrared (FTIR) spectroscopy, N2 adsorption—desorption, thermogravimetry-differential thermal analysis (TG-DTA), and scanning electron microscopy (SEM) experiments, and was subsequently used for malachite green (MG) adsorption. MG adsorption experiments were performed in a batch system, and the effects of temperature and adsorption kinetic and isotherm parameters on the adsorption process were analyzed. The stability of Mg-Al/Biochar was evaluated using regeneration experiments over three cycles. The peaks at 11.47° (003), 22.86° (002), 34.69° (012), and 61.62° (116), in the XRD profile of Mg-Al/Biochar suggested that Mg-Al/Biochar was successfully fabricated. The surface area of Mg-Al/Biochar was up to five times larger than that of pristine Mg-Al-LDH. The adsorption of MG on Mg-Al/Biochar was dominated by interactions at the surface of the adsorbent and was classified as physical adsorption; moreover the maximum adsorption capacity ofMg-Al/Biochar was 70.922 mg/g. Furthermore, the MG removal of Mg-Al/Biochar during three successive adsorption cycles (i.e. 66.73%, 65.57%, and 65.77% for the first, second, and third adsorption cycle) did not change significantly, which indicated the stable structure of the adsorbent. Copyright © 2021 by Authors, Published by BCREC Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0). 

scholarly journals Additional factors influencing sensitivity in the tetramethyl benzidine method for horseradish peroxidase neurohistochemistry.

1980 ◽  
Vol 28 (11) ◽  
pp. 1255-1259 ◽  
Author(s):  
M M Mesulam ◽  
E Hegarty ◽  
H Barbas ◽  
K A Carson ◽  
E C Gower ◽  
...  
Keyword(s):  
Horseradish Peroxidase ◽  
Wheat Germ ◽  
Storage Medium ◽  
Neural Connections ◽  
Long Term Stability ◽  
Factors Influencing ◽  
Duration Of Storage ◽  
The Stability ◽  
Tetramethyl Benzidine

In experiments that use horseradish peroxidase (HRP) and tetramethyl benzidine (TMB) for tracing neural connections, the activity of tissue-bound enzyme as well as the stability of the resultant reaction product are influenced by the duration of storage, the composition of the storage medium, the type of counterstaining and even the details of histological dehydration. Furthermore, the conditions for preserving HRP activity are very different from those necessary for preserving the stability of the tetramethyl benzidine (TMB) reaction product. Thus, tissue-bound HRP activity is stable at a neutral pH, while a much lower pH, around 3.3, is required for preserving the stability of the TMB reaction product. Recent evidence indicates that the stabilization bath in sodium nitroferricyanide that was previously recommended is not necessary. However, gradual dehydration of mounted sections is essential for long-term stability. Excessive counterstaining and excessive dehydration interfere with the detection of reaction product. These considerations are pertinent to experiments using free HRP as well as to those where the enzyme has been conjugated to wheat germ agglutinin.

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