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Catalase Assay Kit

Product code: K-CATAL
€212.00

100 / 200 assays per kit

Prices exclude VAT

Available for shipping

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Content: 100 / 200 assays per kit
Shipping Temperature: Ambient
Storage Temperature: Short term stability: 2-8oC,
Long term stability: See individual component labels
Stability: > 2 years under recommended storage conditions
Analyte: Catalase
Assay Format: Spectrophotometer
Detection Method: Absorbance
Wavelength (nm): 520
Signal Response: Increase
Limit of Detection: 0.5 U/mL
Total Assay Time: 20 min
Application examples: Various food, biological and bacterial samples.
Method recognition: Novel method

Megazyme’s catalase assay kit provides a simple colourimetric method for the measurement of catalase activity. The method is delivered in a fast and reliable format and may be used to detect catalase activity in various samples, including food, biological and bacterial samples. The calculation method included allows for significant variation in the concentration of the H2O2 substrate solution that is employed in the assay which translates into a reduction in the ‘hands on’ time required by the analyst in comparison to other commercial kits.

See our complete list of assay kits for the measurement enzyme activity.

Scheme-K-CATAL CATAL Megazyme

Advantages
  • Very cost effective 
  • Simple, convenient, rapid assay 
  • Standard included  
  • Mega-Calc™ software tool is available from our website for hassle-free raw data processing
Documents
Certificate of Analysis
Safety Data Sheet
Assay Protocol Data Calculator
Publications
Publication

Contrasting anther glucose‐6‐phosphate dehydrogenase activities between two bean varieties suggest an important role in reproductive heat tolerance.

Santiago, J. P., Soltani, A., Bresson, M. M., Preiser, A. L., Lowry, D. B. & Sharkey, T. D. (2021). Plant, Cell & Environment, 44(7), 2185-2199.

Common beans (Phaseolus vulgaris) are highly sensitive to elevated temperatures, and rising global temperatures threaten bean production. Plants at the reproductive stage are especially susceptible to heat stress due to damage to male (anthers) and female (ovary) reproductive tissues, with anthers being more sensitive to heat. Heat damage promotes early tapetal cell degradation, and in beans this was shown to cause male infertility. In this study, we focus on understanding how changes in leaf carbon export in response to elevated temperature stress contribute to heat-induced infertility. We hypothesize that anther glucose-6-phosphate dehydrogenase (G6PDH) activity plays an important role at elevated temperature and promotes thermotolerance. To test this hypothesis, we compared heat-tolerant and susceptible common bean genotypes using a combination of phenotypic, biochemical, and physiological approaches. Our results identified changes in leaf sucrose export, anther sugar accumulation and G6PDH activity and anther H2O2 levels and antioxidant-related enzymes between genotypes at elevated temperature. Further, anther respiration rate was found to be lower at high temperature in both bean varieties. Overall, our results support the hypothesis that enhanced male reproductive heat tolerance involves changes in the anther oxidative pentose phosphate pathway, which supplies reductants to critical H2O2 scavenging enzymes.

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Publication

Assessment of different Bacillus coagulans strains for L-lactic acid production from defined media and gardening hydrolysates: Effect of lignocellulosic inhibitors.

Cubas-Cano, E., Venus, J., González-Fernández, C. & Tomás-Pejó, E. (2020). Journal of Biotechnology, 323, 9-16.

Cellulose valorisation has been successfully addressed for years. However, the use of hemicellulosic hydrolysates is limited due to the presence of C5-sugars and inhibitors formed during pretreatment. Bacillus coagulans is one of the few bacteria able to utilize both C6- and C5-sugars to produce l-lactic acid, but its susceptibility to the lignocellulosic inhibitors needs further investigation. For such a purpose, the tolerance of different B. coagulans strains to increasing concentrations of inhibitors is studied. The isolated A162 strain reached the highest l-lactic acid productivity in all cases (up to 2.4 g L−1  h−1), even in presence of 5 g L−1 of furans and phenols. Remarkably, most of furans and phenolic aldehydes were removed from defined media and hemicellulosic gardening hydrolysate after fermentation with A162. Considering the high productivities and the biodetoxifying effect attained, A162 could be pointed out as a great candidate for valorisation of mixed sugars from hemicellulosic hydrolysates with high inhibitors concentration, promoting the implementation of lignocellulosic biorefineries.

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Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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