Dieses Dokument steht unter einer CreativeCommons Lizenz by/4.0
DC ElementWertSprache
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_DE
dc.identifier.issn1422-0067de_DE
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_DE
dc.relation.ispartofInternational Journal of Molecular Sciencesde_DE
dc.rightsCC BY 4.0de_DE
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.subjectalkaline proteasede_DE
dc.subjectimmobilizationde_DE
dc.subjecthollow core-mesoporous shell silica nanospheresde_DE
dc.subjectnanotechnologyde_DE
dc.subjectalkaliphilesde_DE
dc.subjectdetergentsde_DE
dc.subject.ddc540: Chemiede_DE
dc.titleEnhancement of alkaline protease activity and stability via covalent immobilization onto hollow core-mesoporous shell silica nanospheresde_DE
dc.typeArticlede_DE
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_DE
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_DE
tuhh.relation.ispartofInternational Journal of Molecular Sciencesde
tuhh.publisher.doi10.3390/ijms17020184-
tuhh.publication.instituteTechnische Mikrobiologie V-7de_DE
tuhh.identifier.doi10.15480/882.1421-
tuhh.type.opus(wissenschaftlicher) Artikelde
tuhh.institute.germanTechnische Mikrobiologie V-7de
tuhh.institute.englishTechnische Mikrobiologie V-7de_DE
tuhh.gvk.hasppnfalse-
tuhh.hasurnfalse-
openaire.rightsinfo:eu-repo/semantics/openAccessde_DE
dc.type.driverarticle-
dc.rights.ccbyde_DE
dc.rights.ccversion4.0de_DE
dc.type.casraiJournal Articleen
dc.rights.nationallicensefalsede_DE
item.creatorOrcidIbrahim, Abdelnasser S. S.-
item.creatorOrcidAl-Salamah, Ali A.-
item.creatorOrcidEl-Toni, Ahmed Mohamed-
item.creatorOrcidAlmaary, Khalid S.-
item.creatorOrcidEl-Tayeb, Mohamed A.-
item.creatorOrcidElbadawi, Yahya B.-
item.creatorOrcidAntranikian, Garabed-
item.creatorGNDIbrahim, Abdelnasser S. S.-
item.creatorGNDAl-Salamah, Ali A.-
item.creatorGNDEl-Toni, Ahmed Mohamed-
item.creatorGNDAlmaary, Khalid S.-
item.creatorGNDEl-Tayeb, Mohamed A.-
item.creatorGNDElbadawi, Yahya B.-
item.creatorGNDAntranikian, Garabed-
item.grantfulltextopen-
item.fulltextWith Fulltext-
Enthalten in den Sammlungen:tub.dok
Dateien zu dieser Ressource:
Datei Beschreibung GrößeFormat 
ijms-17-00184.pdf3,9 MBAdobe PDFMiniaturbild
Öffnen/Anzeigen
Zur Kurzanzeige

Seitenansichten

119
Letzte Woche
0
Letzten Monat
1
checked on 18.08.2018

Download(s)

75
checked on 18.08.2018

Google ScholarTM

Prüfe


Alle Ressourcen in diesem Repository sind urheberrechtlich geschützt.