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Immobilization of Alkaline Protease From Bacillus brevis Using Ca-Alginate Entrapment Strategy for Improved Catalytic Stability, Silver Recovery, and Dehairing Potentialities.
- Source :
-
Catalysis Letters . Dec2020, Vol. 150 Issue 12, p3572-3583. 12p. - Publication Year :
- 2020
-
Abstract
- Proteases are one of the most important biocatalysts with an industrial perspective due to their high production capability, cost-effective, and eco-friendly nature. In this study, an alkaline protease produced by Bacillus brevis (228.31 ± 6.2 U/mL) in liquid-state fermentation at pH 7.0 and 47 °C was further enhanced by optimizing various physical parameters. The maximum protease activity (631.09 ± 3.7 U/mL) was recorded at 45 °C, pH 8.0, and using 3 mL of inoculum size after 72 h. The optimally-produced alkaline protease was immobilized on Ca-alginate beads, and the process was optimized using a central composite design-based response surface methodology. The maximum immobilization yield (> 70%) was achieved using a 2–3.0% gelling agent (Na-alginate) and 2.5–3.0% binder (CaCl2), with 400–600 mg/L of protease concentration. Characterization revealed that immobilization improves the pH and thermal stability of protease, as the maximum activity was recorded at pH 10 and 65 °C. The kinetic studies of protease revealed higher Vmax (454.5 U/mL) and lower Km (0.09 μM) values after Ca-alginate immobilization as compared with the free enzyme (Vmax 333.3 U/mL and Km 0.16 μM). Ca-alginate immobilized protease also possessed good recyclability potential in several consecutive substrate hydrolysis experiments. By applying on goatskin and X-ray film, the immobilized biocatalyst showed improved activity than the free enzyme, revealing its potential biotechnological applications. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 1011372X
- Volume :
- 150
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Catalysis Letters
- Publication Type :
- Academic Journal
- Accession number :
- 146532000
- Full Text :
- https://doi.org/10.1007/s10562-020-03268-y