Practical Enzymology

Bisswanger, Hans

doi:10.1002/9783527659227

Cited by 70 publications

(77 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One unit of Catalase is defined as the amount of enzyme catalyzing the decomposition of 1 mol H 2 O 2 in a minute [20]. The substrate used for analysis was 10 mM H 2 O 2 solution which was made in 50 mM phosphate buffer, pH 7.0 [21].…”

Section: Spectrophotometric Analysis Of Catalase Activitymentioning

confidence: 99%

Purification and characterization of catalase from sprouted black gram (Vigna mungo) seeds

Kandukuri

Noor

Ranjini

et al. 2012

Journal of Chromatography B

View full text Add to dashboard Cite

Section: Spectrophotometric Analysis Of Catalase Activitymentioning

confidence: 99%

Purification and characterization of catalase from sprouted black gram (Vigna mungo) seeds

Kandukuri

Noor

Ranjini

et al. 2012

Journal of Chromatography B

View full text Add to dashboard Cite

“…Regarding the trans-cinnamic acid as inhibitor, the results obtained pointed to a concomitant increase in inhibition efficiency with increase in caffeic acid concentration. In fact, this statement could expose an uncompetitive inhibition behaviour, which works best when substrate concentration is high [44]. Herein, the trans-cinnamic acid only exhibited its inhibitory effect for caffeic acid concentrations equal to or higher than 0.…”

Section: Effect Of Inhibitors On the Diphenolase Activity Of Mushroommentioning

confidence: 96%

“…Similar results were found for the other caffeic acid solutions tested. Bearing in mind that zero-order conditions can only be achieved as long as the catalyst is limiting and that the reaction rate must be proportional to enzyme concentration to evaluate the Michaelis-Menten kinetics [44], a 54 U mL −1 enzyme concentration was chosen.…”

Section: Enzyme Concentrationmentioning

confidence: 99%

Automatic flow methodology for kinetic and inhibition studies of reactions with poorly water-soluble substrates in ionic liquid systems

Araújo¹,

Saraiva²,

Lima³

2011

Analytica Chimica Acta

View full text Add to dashboard Cite

“…During the first stage, WorleyParsons reviewed, commented and discussed with PNNL and Akermin the preliminary report [2] and the work sheet [3]. Subsequently, PNNL and Akermin provided an updated report [4] and worksheet [5], incorporating WorleyParsons preliminary comments.…”

Section: Summary Of the Work Performed By Worleyparsonsmentioning

confidence: 99%

Advanced Low Energy Enzyme Catalyzed Solvent for CO<sub>2</sub> Capture

Zaks¹,

Reardon²

2013

View full text Add to dashboard Cite

A proof-of-concept biocatalyst enhanced solvent process was developed and demonstrated in an integrated bench-scale system using coal post combustion flue gas. The biocatalyst was deployed as a coating on M500X structured packing. Rate enhancement was evaluated using a non-volatile and nontoxic 20 wt% potassium carbonate solution. Greater than 500-fold volumetric scale-up from laboratory to bench scale was demonstrated in this project. Key technical achievements included: 10-fold mass transfer enhancement demonstrated in laboratory testing relative to blank potassium carbonate at 45°C; ~ 7-fold enhancement over blank in bench-scale field testing at National Carbon Capture Center; aerosol emissions were below detection limits (< 0.8 ppm); 90% capture was demonstrated at ~19.5 Nm 3 /hr (dry basis); and ~ 80% CO 2 capture was demonstrated at ~ 30 Nm 3 /hr (dry basis) for more than 2800-hrs on flue gas with minimal detectible decline in activity. The regeneration energy requirement was 3.5 GJ/t CO 2 for this solvent, which was below the target of <2.1 GJ/t CO 2 . Bench unit testing revealed kinetic limitations in the un-catalyzed stripper at around 85°C, but process modeling based on bench unit data showed that equivalent work of less than 300 kWh/t CO 2 including all CO 2 compression can be achieved at lower temperature stripping conditions. Cost analysis showed that 20% potassium carbonate in a basic solvent flow sheet with biocatalyst coated packing has economic performance comparable to the reference NETL Case-12, 30% MEA. A detailed techno-economic analysis indicated that addition of catalyst in the stripper could reduce the cost of capture by ~6% and cost of avoided CO 2 by ~10% below reference NETL Case-12. Based on these results, a directional plan was identified to reduce the cost of CO 2 capture in future work.

show abstract

Practical Enzymology

Cited by 70 publications

References 0 publications

Purification and characterization of catalase from sprouted black gram (Vigna mungo) seeds

Purification and characterization of catalase from sprouted black gram (Vigna mungo) seeds

Automatic flow methodology for kinetic and inhibition studies of reactions with poorly water-soluble substrates in ionic liquid systems

Advanced Low Energy Enzyme Catalyzed Solvent for CO<sub>2</sub> Capture

Contact Info

Product

Resources

About