The Voltammetric Study of β–Glucosidase Hydrolytic Product with Modified Electrode

2016 ◽  
Vol 675-676 ◽  
pp. 671-674
Author(s):  
Chariwat Pitsanuwong ◽  
Sumamal Charernchai ◽  
Wanida Wonsawat
Keyword(s):  
Modified Electrode ◽  
Enzyme Purification ◽  
Activity Measurement ◽  
The Novel ◽  
Activity Assay ◽  
Enzyme Activity Assay ◽  
Hydrolytic Product ◽  
Voltammetric Study ◽  
Screen Printed Carbon Electrode ◽  
Voltammetric Technique

The novel modified electrode of voltammetric technique was applied to detect p-nitrophenol quantity released from the synthetic substrate p-nitrophenyl-β-D-glucopyranoside (pNPG) for β-glucosidase activity measurement. The results from the developed bismuth film modified screen printed carbon electrode (Bi/SPCE) for p-nitrophenol detecting, can be used for enzyme activity assay during purification steps. The further work, the condition of convenient voltammetric method will be optimized the condition suitable for applying to the β-glucosidase enzyme purification from Terminalia ivorensis C. seeds.

Expression and Enzyme Activity Assay of pfu with Molecular Chaperone

2010 ◽  
Vol 31 (6) ◽  
pp. 499-503
Author(s):  
Hai-Jun ZHANG ◽  
Jun YANG ◽  
Xiao-Guang LIU ◽  
Xiang-Yang HU
Keyword(s):  
Enzyme Activity ◽  
Molecular Chaperone ◽  
Activity Assay ◽  
Enzyme Activity Assay

scholarly journals Copper-nickel oxide nanofilm modified electrode for non-enzymatic determination of glucose

2020 ◽  
Vol 10 (3) ◽  
pp. 245-255
Author(s):  
Mahsa Hasanzadeh ◽  
Zahra Hasanzadeh ◽  
Sakineh Alizadeh ◽  
Mehran Sayadi ◽  
Mojtaba Nasiri Nezhad ◽  
...  
Keyword(s):  
Modified Electrode ◽  
Limit Of Detection ◽  
High Sensitivity ◽  
Stability Loss ◽  
The Novel ◽  
Step Potential ◽  
Enzymatic Determination ◽  
Wide Range ◽  
Naoh Solution

CuxO-NiO nanocomposite film for the non-enzymatic determination of glucose was prepared by the novel modifying method. At first, anodized Cu electrode was kept in a mixture solution of CuSO4, NiSO4 and H2SO4 for 15 minutes. Then, a cathodization process with a step potential of -6 V in a mixture solution of CuSO4 and NiSO4 was initiated, generating formation of porous Cu-Ni film on the bare Cu electrode by electrodeposition assisted by the release of hydrogen bubbles acting as soft templates. Optimized conditions were determined by the experimental design software for electrodeposition process. Afterward, Cu-Ni modified electrode was scanned by cyclic voltammetry (CV) method in NaOH solution to convert Cu and Ni nanoparticles to the nano-scaled CuxO-NiO film. The electrocatalytic behavior of the novel CuxO-NiO film toward glucose oxidation was studied by CV and chronoamperometry (CHA) techniques. The calibration curve of glucose was found linear in a wide range of 0.04–5.76 mM, with a low limit of detection (LOD) of 7.3 µM (S/N = 3) and high sensitivity (1.38 mA mM-1 cm-2). The sensor showed high selectivity against some usual interfering species and high stability (loss of only 6.3 % of its performance over one month). The prepared CuxO-NiO nanofilm based sensor was successfully applied for monitoring glucose in human blood serum and urine samples.

scholarly journals PbLAC4-like, activated by PbMYB26, related to the degradation of anthocyanin during color fading in pear

2021 ◽  
Author(s):  
Guangping Zhao ◽  
Fangxin Xiang ◽  
Shichao Zhang ◽  
Junxing Song ◽  
Xieyu Li ◽  
...  
Keyword(s):  
Prokaryotic Expression ◽  
Degradation Mechanism ◽  
Vital Role ◽  
Luciferase Assay ◽  
Activity Assay ◽  
Enzyme Activity Assay ◽  
Red Color ◽  
Color Fading ◽  
Degradation Ability ◽  
Anthocyanin Degradation

Abstract Background Anthocyanin degradation results in the loss of red color in leaves, petals and receptacles during development. But the degradation mechanism is not fully investigated. It is vital to study the degradation mechanism of anthocyanin in pear for promoting the accumulation of anthocyanin and inhibiting the red fading in pear. Results Here, we reported that laccase encoded by PbLAC4-like was associated with anthocyanin degradation in pear. The expression pattern of PbLAC4-like was negatively correlated with the content of anthocyanin during the color fading process of pear leaves, petals and receptacles. Phylogenetic analysis and sequence alignment revealed that PbLAC4-like played a vital role in anthocyanin degradation. Thus, the degradation of anthocyanin induced by PbLAC4-like was further verified by transient assays and prokaryotic expression. More than 80% of anthocyanin compounds were degraded by transiently over-expressed PbLAC4-like in pear fruitlet peel. The activity of crude enzyme to degrade anthocyanin in leaves at different stages was basically consistent with the expression of PbLAC4-like. The anthocyanin degradation ability of prokaryotic induced PbLAC4-like protein was also verified by enzyme activity assay. Besides, we also identified PbMYB26 as a positive regulator of PbLAC4-like. Yeast one-hybrid and dual luciferase assay results showed that PbMYB26 activated PbLAC4-like expression by directly binding to the PbLAC4-like promoter. Conclusions Taken together, the PbLAC4-like activated by PbMYB26, was involved in the degradation of anthocyanin, resulting in the redness fading in different pear tissues.

Impact of enzyme activity assay on indication in liver transplantation for ornithine transcarbamylase deficiency

2012 ◽  
Vol 105 (3) ◽  
pp. 404-407 ◽  
Author(s):  
Taiichi Wakiya ◽  
Yukihiro Sanada ◽  
Taizen Urahashi ◽  
Yoshiyuki Ihara ◽  
Naoya Yamada ◽  
...  
Keyword(s):  
Liver Transplantation ◽  
Enzyme Activity ◽  
Ornithine Transcarbamylase ◽  
Ornithine Transcarbamylase Deficiency ◽  
Activity Assay ◽  
Enzyme Activity Assay
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