Please use this identifier to cite or link to this item: https://doi.org/10.15480/882.1421
Publisher DOI: 10.3390/ijms17020184
Title: Enhancement of alkaline protease activity and stability via covalent immobilization onto hollow core-mesoporous shell silica nanospheres
Language: English
Authors: Ibrahim, Abdelnasser S. S. 
Al-Salamah, Ali A. 
El-Toni, Ahmed Mohamed 
Almaary, Khalid S. 
El-Tayeb, Mohamed A. 
Elbadawi, Yahya B. 
Antranikian, Garabed 
Keywords: alkaline protease;immobilization;hollow core-mesoporous shell silica nanospheres;nanotechnology;alkaliphiles;detergents
Issue Date: 29-Jan-2016
Publisher: Multidisciplinary Digital Publishing Institute
Source: International Journal of Molecular Sciences 17(2016), 2: 184
Journal or Series Name: International journal of molecular sciences 
Abstract (english): 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.
URI: http://hdl.handle.net/11420/1424
DOI: 10.15480/882.1421
ISSN: 1422-0067
Institute: Technische Mikrobiologie V-7 
Type: (wissenschaftlicher) Artikel
License: CC BY 4.0 (Attribution) CC BY 4.0 (Attribution)
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