Quantum dot-based nanosensors for diagnosis via enzyme activity measurement

2013 ◽  
Vol 13 (4) ◽  
pp. 367-375 ◽  
Author(s):  
Birgitta R Knudsen ◽  
Morten Leth Jepsen ◽  
Yi-Ping Ho
Keyword(s):  
Enzyme Activity ◽  
Quantum Dot ◽  
Activity Measurement

Enzyme activation for activator and enzyme activity measurement☆

1993 ◽  
Vol 8 (6) ◽  
pp. 291-297 ◽  
Author(s):  
Ulla Wollenberger ◽  
Frieder W. Scheller
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activation ◽  
Activity Measurement

scholarly journals Screening Cellulolytic Bacteria from the Digestive Tract Snail (Achatina fulica) and Test the Ability of Cellulase Activity

2016 ◽  
Vol 8 (3) ◽  
pp. 386
Author(s):  
Wijanarka Wijanarka ◽  
Endang Kusdiyantini ◽  
Sarjana Parman
Keyword(s):  
Enzyme Activity ◽  
Digestive Tract ◽  
Generation Time ◽  
Cellulase Activity ◽  
Biology Education ◽  
Activity Measurement ◽  
Bacterial Isolates ◽  
Achatina Fulica ◽  
Cellulolytic Bacteria ◽  
Activity Measurements

<p>On the research of enzyme production levels observed cellulase produced by bacteria in the digestive tract of the isolation of the Snail (<em>Achatina fulica</em>). Isolation of bacteria based on the ability of bacteria to grow on CMC media. The purpose of this study was to determine cellulase activity by cellulolytic bacteria. Some bacterial isolates were identified as cellulolytic bacteria, they were KE-B1, KE-B2, KE-B3, KE-B4, KE-B5, and KE-B6. Isolates KE-B6 was the best isolates. Furthermore KE-B6 isolates were grown on media production to determine the pattern of growth and enzyme activity. Measurement of cell growth was conducted by inoculating starter aged 22 hours at CMC production of liquid medium. Cellulase enzyme activity measurements was performed by the DNS method. The results showed that the highest activity by new isolate bacteria KE-B6 and its value of the activity of 0.4539 U/mL, growth rate (µ) 0.377/hour and generation time (g) 1.84 hour. This research expected cellulase of producing bacteria were easy, inexpensive and efficient. This enzyme can be used as an enzyme biolytic once expected to replace expensive commercial enzyme. The biotylic enzyme can be applied to strains improvement (protoplast fusion).</p><p><strong>How to Cite</strong></p><p>Wijanarka, W., Kusdiyantini, E. &amp; Parman, S. (2016). Screening Cellulolytic Bacteria from the Digestive Tract Snail (<em>Achatina fulica</em>) and Test the Ability of Cellulase Activity. <em>Biosaintifika: Journal of Biology &amp; Biology Education</em>, 8(3), 386-392. </p>

Microfluidics-Enabled Enzyme Activity Measurement in Single Cells

2015 ◽  
pp. 209-219 ◽  
Author(s):  
Cinzia Tesauro ◽  
Rikke Frøhlich ◽  
Magnus Stougaard ◽  
Yi-Ping Ho ◽  
Birgitta R. Knudsen
Keyword(s):  
Enzyme Activity ◽  
Single Cells ◽  
Activity Measurement

Purification and immunochemical quantitation of Penicillium roqueforti acid aspartyl proteinase

1997 ◽  
Vol 64 (1) ◽  
pp. 105-113 ◽  
Author(s):  
EMMANUELLE BRACQ ◽  
ANNIE LEVIEUX ◽  
DIDIER LEVIEUX
Keyword(s):  
Enzyme Activity ◽  
Sandwich Elisa ◽  
Exchange Chromatography ◽  
Site Directed Mutagenesis ◽  
Size Exclusion ◽  
Activity Measurement ◽  
Penicillium Roqueforti ◽  
Protein Ratio ◽  
Culture Filtrates ◽  
Exclusion Chromatography

Acid aspartyl proteinase of Penicillium roqueforti was purified from culture filtrates using FPLC ion-exchange chromatography on Mono Q and size exclusion chromatography on Superdex 75. The purity obtained allowed us to produce, using rabbits, a specific antiserum which was then used to develop a sandwich ELISA. The test was sensitive (detection limit, 0·25 ng/ml), reproducible (CV, 3·1–6·9%) and closely correlated with enzyme activity measurement (r=0·995, P<0·001). This ELISA should be a valuable tool for monitoring acid aspartyl proteinase level in culture filtrates and for determining the enzyme activity[ratio ]enzyme protein ratio of acid aspartyl proteinase obtained after genetic recombinations or site-directed mutagenesis.

Enzyme activity measurement via spectral evolution profiling and PARAFAC

2013 ◽  
Vol 778 ◽  
pp. 1-8 ◽  
Author(s):  
Andreas Baum ◽  
Anne S. Meyer ◽  
Javier Lopez Garcia ◽  
Max Egebo ◽  
Per Waaben Hansen ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Activity Measurement ◽  
Spectral Evolution

Proteolytic Activity at Quantum Dot-Conjugates: Kinetic Analysis Reveals Enhanced Enzyme Activity and Localized Interfacial “Hopping”

Nano Letters ◽  
2012 ◽  
Vol 12 (7) ◽  
pp. 3793-3802 ◽  
Author(s):  
W. Russ Algar ◽  
Anthony Malonoski ◽  
Jeffrey R. Deschamps ◽  
Juan B. Blanco-Canosa ◽  
Kimihiro Susumu ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Quantum Dot ◽  
Kinetic Analysis ◽  
Proteolytic Activity

Quantum dot based enzyme activity sensors present deviations from Michaelis-Menten kinetic model

2016 ◽  
Author(s):  
Sebastián A. Díaz ◽  
Carl W. Brown ◽  
Anthony P. Malanoski ◽  
Eunkeu Oh ◽  
Kimihiro Susumu ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Kinetic Model ◽  
Quantum Dot ◽  
Activity Sensors ◽  
Menten Kinetic
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