Academic Journal
Optimization of process variables by central composite design for the immobilization of urease enzyme on functionalized gold nanoparticles for various applications.
| Τίτλος: | Optimization of process variables by central composite design for the immobilization of urease enzyme on functionalized gold nanoparticles for various applications. |
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| Συγγραφείς: | Talat M; Department of Physics, Nanoscience and Nanotechnology Unit, Banaras Hindu University, Varanasi, 221005, India., Singh AK, Srivastava ON |
| Πηγή: | Bioprocess and biosystems engineering [Bioprocess Biosyst Eng] 2011 Aug; Vol. 34 (6), pp. 647-57. Date of Electronic Publication: 2011 Jan 26. |
| Τύπος έκδοσης: | Journal Article; Research Support, Non-U.S. Gov't |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Springer-Verlag Country of Publication: Germany NLM ID: 101088505 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1615-7605 (Electronic) Linking ISSN: 16157591 NLM ISO Abbreviation: Bioprocess Biosyst Eng Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Berlin, Germany : Springer-Verlag, 2001- |
| Ιατρικοί όροι (MeSH): | Urease*/chemistry , Urease*/metabolism, Cucurbita/*enzymology , Enzymes, Immobilized/*metabolism , Nanoparticles/*chemistry , Research Design/*statistics & numerical data, Environmental Monitoring/methods ; Gold/chemistry ; Nanoparticles/ultrastructure ; Analysis of Variance ; Data Interpretation, Statistical ; Hydrogen-Ion Concentration ; Regression Analysis ; Spectroscopy, Fourier Transform Infrared ; Temperature |
| Περίληψη: | In the present study, enzyme urease has been immobilized on amine-functionalized gold nanoparticles (AuNPs). AuNPs were synthesized using natural precursor, i.e., clove extract and amine functionalized through 0.004 M L: -cysteine. Enzyme (urease) was extracted and purified from the vegetable waste, i.e., seeds of pumpkin to apparent homogeneity (sp. activity 353 U/mg protein). FTIR spectroscopy and transmission electron microscopy was used to characterize the immobilized enzyme. The immobilized enzyme exhibited enhanced activity as compared with the enzyme in the solution, especially, at lower enzyme concentration. Based on the evaluation of activity assay of the immobilized enzyme, it was found that the immobilized enzyme was quite stable for about a month and could successfully be used even after eight cycles having enzyme activity of about 47%. In addition to this central composite design (CCD) with the help of MINITAB version 15 Software was utilized to optimize the process variables viz., pH and temperature affecting the enzyme activity upon immobilization on AuNPs. The results predicted by the design were found in good agreement (R2 = 96.38%) with the experimental results indicating the applicability of proposed model. The multiple regression analysis and ANOVA showed the individual and cumulative effect of pH and temperature on enzyme activity indicating that the activity increased with the increase of pH up to 7.5 and temperature 75 °C. The effects of each variables represented by main effect plot, 3D surface plot, isoresponse contour plot and optimized plot were helpful in predicting results by performing a limited set of experiments. |
| Substance Nomenclature: | 0 (Enzymes, Immobilized) 7440-57-5 (Gold) EC 3.5.1.5 (Urease) |
| Entry Date(s): | Date Created: 20110127 Date Completed: 20120305 Latest Revision: 20110714 |
| Update Code: | 20260130 |
| DOI: | 10.1007/s00449-011-0514-2 |
| PMID: | 21267597 |
| Βάση Δεδομένων: | MEDLINE |
| ISSN: | 1615-7605 |
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| DOI: | 10.1007/s00449-011-0514-2 |