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dc.contributor.authorIbrahim, Abdelnasser S. S.-
dc.contributor.authorAl-Salamah, Ali A.-
dc.contributor.authorEl-Toni, Ahmed Mohamed-
dc.contributor.authorAlmaary, Khalid S.-
dc.contributor.authorEl-Tayeb, Mohamed A.-
dc.contributor.authorElbadawi, Yahya B.-
dc.contributor.authorAntranikian, Garabed-
dc.date.accessioned2017-08-29T11:52:20Z-
dc.date.available2017-08-29T11:52:20Z-
dc.date.issued2016-01-29-
dc.identifierdoi: 10.3390/ijms17020184-
dc.identifier.citationInternational Journal of Molecular Sciences 17(2016), 2: 184de
dc.identifier.issn1422-0067de
dc.identifier.urihttp://tubdok.tub.tuhh.de/handle/11420/1424-
dc.description.abstractThe stability and reusability of soluble enzymes are of major concerns, which limit their industrial applications. Herein, alkaline protease from <i>Bacillus</i> 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–NH<sub>2</sub> 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 <i>V<sub>max</sub></i>, <i>k<sub>cat</sub></i> and <i>k<sub>cat</sub></i>/<i>K<sub>m</sub></i>, 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.-
dc.description.abstractThe stability and reusability of soluble enzymes are of major concerns, which limit their industrial applications. Herein, alkaline protease from <i>Bacillus</i> 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–NH<sub>2</sub> 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 <i>V<sub>max</sub></i>, <i>k<sub>cat</sub></i> and <i>k<sub>cat</sub></i>/<i>K<sub>m</sub></i>, 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.en
dc.publisherMultidisciplinary Digital Publishing Institutede
dc.relation.ispartofInternational Journal of Molecular Sciencesde
dc.rightsCC BY 4.0de
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.subjectalkaline proteasede
dc.subjectimmobilizationde
dc.subjecthollow core-mesoporous shell silica nanospheresde
dc.subjectnanotechnologyde
dc.subjectalkaliphilesde
dc.subjectdetergentsde
dc.subject.ddc540: Chemiede
dc.titleEnhancement of alkaline protease activity and stability via covalent immobilization onto hollow core-mesoporous shell silica nanospheresde
dc.typeArticlede
dc.date.updated2017-08-24T09:55:08Z-
dc.identifier.urnurn:nbn:de:gbv:830-882w02212-
dc.identifier.doi10.15480/882.1421-
dc.type.diniarticle-
dc.subject.ddccode540-
dcterms.DCMITypeText-
tuhh.identifier.urnurn:nbn:de:gbv:830-882w02212de
tuhh.oai.showtrue-
dc.identifier.hdl11420/1424-
tuhh.abstract.englishThe stability and reusability of soluble enzymes are of major concerns, which limit their industrial applications. Herein, alkaline protease from <i>Bacillus</i> 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–NH<sub>2</sub> 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 <i>V<sub>max</sub></i>, <i>k<sub>cat</sub></i> and <i>k<sub>cat</sub></i>/<i>K<sub>m</sub></i>, 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.de
tuhh.relation.ispartofInternational Journal of Molecular Sciencesde
tuhh.publisher.doi10.3390/ijms17020184-
tuhh.publication.instituteTechnische Mikrobiologie V-7de
tuhh.identifier.doi10.15480/882.1421-
tuhh.type.opus(wissenschaftlicher) Artikelde
tuhh.institute.germanTechnische Mikrobiologie V-7de
tuhh.gvk.hasppnfalse-
tuhh.hasurnfalse-
openaire.rightsinfo:eu-repo/semantics/openAccessde
dc.type.driverarticle-
dc.rights.ccbyde
dc.rights.ccversion4.0de
dc.type.casraiJournal Articleen
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