Enzymatic detection of As(III) in aqueous solution using alginate immobilized pumpkin urease: Optimization of process variables by response surface methodology
Bioresource Technology, ISSN: 0960-8524, Vol: 100, Issue: 19, Page: 4462-4467
2009
- 23Citations
- 31Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations23
- Citation Indexes23
- 23
- CrossRef15
- Captures31
- Readers31
- 31
Article Description
Urease immobilized on alginate was utilized to detect and quantify As 3+ in aqueous solution. Urease from the seeds of pumpkin (vegetable waste) was purified to apparent homogeneity by heat treatment and gel filtration (Sephadex G-200). Further enzyme was entrapped in 3.5% alginate beads. Urea hydrolysis by enzyme revealed a clear dependence on the concentration and interaction time of As 3+. The process variables effecting the quantitation of As 3+ was investigated using central composite design with Minitab ® 15 software. The predicted results were found in good agreement ( R 2 = 96.71%) with experimental results indicating the applicability of proposed model. The multiple regression analysis and ANOVA showed that enzyme activity decreased with increase of As 3+ concentration and interaction time. 3D plot and contour plot between As 3+ concentration and interaction time was helpful to predict residual activity of enzyme for a particular As 3+ at a particular time.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S096085240900368X; http://dx.doi.org/10.1016/j.biortech.2009.04.009; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=67349288049&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/19423339; https://linkinghub.elsevier.com/retrieve/pii/S096085240900368X; https://dx.doi.org/10.1016/j.biortech.2009.04.009
Elsevier BV
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