performance improvement of ca-alginate bead cross- linked laccase from trametes versicolor ibl-04
Clicks: 236
ID: 218168
2015
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This
article has not been analysed, so there is no overall score —
reader engagement is measured and shown alongside.
Reader Engagement
Steady Performance
30.0
/100
236 views
38 readers
AI Quality Assessment
Not analyzed
Readership in this journal
SteadyRanked #110 of 185 articles by views in medical archives (sarajevo, bosnia and herzegovina)
Most read
Least read
Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 185 in total.
Mint this article as an NFT
Not yet mintedCreate a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.
5
SUSD
one-off · no wallet required
Abstract
Extracellular laccase was produced by Trametes versicolor IBL-04 using corn cobs as a substrate under pre-optimized culture conditions. A 64-kDa laccase enzyme was purified and immobilized on calcium alginate beads using glutaraldehyde as a cross-linking reagent. Maximum enzyme immobilization efficiency (89%) was observed with 2-mm calcium-alginate beads that were developed using 4% (w/v) sodium alginate in 2% (w/v) calcium chloride solution. Immobilization of laccase enhanced the optimum temperature but caused an acidic shift in the optimum pH of the enzyme. The immobilized enzyme showed optimum activity at pH 3.0 and 60 °C as compared to pH 4.5 and 45 °C for free laccase. The kinetic constants Km and Vmax of laccase were significantly altered by immobilization. The affinity of enzyme toward its substrate increased (Km decreased), leading to enhanced catalytic efficiency (Vmax increased). Scanning electron microscopy (SEM) was performed to characterize the free and enzyme-bound immobilization matrix. Free and immobilized enzymes also were used for decolorization of the Reactive T Blue dye (030905 GWF) for three days. The free and immobilized laccases decolorized the dye by 65% and 92%, respectively, in 72 h. The immobilized enzyme retained 68% of its original activity after three cycles of repeated reuse for dye decolorization, indicating the usefulness of immobilized laccase in repeated industrial batch operations.
| Reference Key |
noreen2015bioresourcesperformance
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
|---|---|
| Authors | ;Sadia Noreen;Muhammad Asgher;Fatma Hussain;Ahsan Iqbal |
| Journal | medical archives (sarajevo, bosnia and herzegovina) |
| Year | 2015 |
| DOI |
10.15376/biores.11.1.558-572
|
| URL | |
| Keywords |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.