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Int. J. Mol. Sci. 2016, 17(2), 184; doi:10.3390/ijms17020184

Enhancement of Alkaline Protease Activity and Stability via Covalent Immobilization onto Hollow Core-Mesoporous Shell Silica Nanospheres

1
Department of Botany and Microbiology, College of Science, King Saud University, Riyadh 11451, Saudi Arabia
2
Department of Chemistry of Natural and Microbial Products, Pharmaceutical Industries Research Division, National Research Center, El-Buhouth St., Dokki, Cairo 12311, Egypt
3
King Abdullah Institute for Nanotechnology, King Saud University, Riyadh 11451, Saudi Arabia
4
Central Metallurgical Research and Development Institute, Helwan, Cairo 11421, Egypt
5
Institute of Technical Microbiology, Hamburg University of Technology, Hamburg 21073, Germany
*
Author to whom correspondence should be addressed.
Academic Editor: Vladimír Křen
Received: 8 December 2015 / Revised: 21 January 2016 / Accepted: 25 January 2016 / Published: 29 January 2016
(This article belongs to the Special Issue Molecular Biocatalysis)
View Full-Text   |   Download PDF [3900 KB, uploaded 29 January 2016]   |  

Abstract

The stability and reusability of soluble enzymes are of major concerns, which limit their industrial applications. Herein, alkaline protease from Bacillus sp. NPST-AK15 was immobilized onto hollow core-mesoporous shell silica (HCMSS) nanospheres. Subsequently, the properties of immobilized proteases were evaluated. Non-, ethane- and amino-functionalized HCMSS nanospheres were synthesized and characterized. NPST-AK15 was immobilized onto the synthesized nano-supports by physical and covalent immobilization approaches. However, protease immobilization by covalent attachment onto the activated HCMSS–NH2 nanospheres showed highest immobilization yield (75.6%) and loading capacity (88.1 μg protein/mg carrier) and was applied in the further studies. In comparison to free enzyme, the covalently immobilized protease exhibited a slight shift in the optimal pH from 10.5 to 11.0, respectively. The optimum temperature for catalytic activity of both free and immobilized enzyme was seen at 60 °C. However, while the free enzyme was completely inactivated when treated at 60 °C for 1 h the immobilized enzyme still retained 63.6% of its initial activity. The immobilized protease showed higher Vmax, kcat and kcat/Km, than soluble enzyme by 1.6-, 1.6- and 2.4-fold, respectively. In addition, the immobilized protease affinity to the substrate increased by about 1.5-fold. Furthermore, the enzyme stability in various organic solvents was significantly enhanced upon immobilization. Interestingly, the immobilized enzyme exhibited much higher stability in several commercial detergents including OMO, Tide, Ariel, Bonux and Xra by up to 5.2-fold. Finally, the immobilized protease maintained significant catalytic efficiency for twelve consecutive reaction cycles. These results suggest the effectiveness of the developed nanobiocatalyst as a candidate for detergent formulation and peptide synthesis in non-aqueous media. View Full-Text
Keywords: alkaline protease; immobilization; hollow core-mesoporous shell silica nanospheres; nanotechnology; alkaliphiles; detergents alkaline protease; immobilization; hollow core-mesoporous shell silica nanospheres; nanotechnology; alkaliphiles; detergents
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MDPI and ACS Style

Ibrahim, A.S.S.; Al-Salamah, A.A.; El-Toni, A.M.; Almaary, K.S.; El-Tayeb, M.A.; Elbadawi, Y.B.; Antranikian, G. Enhancement of Alkaline Protease Activity and Stability via Covalent Immobilization onto Hollow Core-Mesoporous Shell Silica Nanospheres. Int. J. Mol. Sci. 2016, 17, 184.

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