Chaperonin-Inspired pH Protection by Mesoporous Silica SBA-15 on Myoglobin and Lysozyme

While enzymes are valuable tools in many fields of biotechnology, they are fragile and must be protected against denaturing conditions such as unfavorable solution pH. Within living organisms, chaperonins help enzymes fold into their native shape and protect them from damage. Inspired by this natura...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1999. - 32(2016), 37 vom: 20. Sept., Seite 9604-10
1. Verfasser: Lynch, Michele M (VerfasserIn)
Weitere Verfasser: Liu, Jichuan, Nigra, Michael, Coppens, Marc-Olivier
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Enzymes, Immobilized Myoglobin SBA-15 Silicon Dioxide 7631-86-9 Muramidase EC 3.2.1.17 Chaperonins EC 3.6.1.-
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520 |a While enzymes are valuable tools in many fields of biotechnology, they are fragile and must be protected against denaturing conditions such as unfavorable solution pH. Within living organisms, chaperonins help enzymes fold into their native shape and protect them from damage. Inspired by this natural solution, mesoporous silica SBA-15 with different pore diameters is synthesized as a support material for immobilizing and protecting enzymes. In separate experiments, the model enzymes myoglobin and lysozyme are physically adsorbed to SBA-15 and exposed to a range of buffered pH conditions. The immobilized enzymes' biocatalytic activities are quantified and compared to the activities of nonimmobilized enzymes in the same solution conditions. It has been observed that myoglobin immobilized on SBA-15 is protected from acidic denaturation from pH 3.6 to 5.1, exhibiting relative activity of up to 350%. Immobilized lysozyme is protected from unfavorable conditions from pH 6.6 to 7.6, with relative activity of up to 200%. These results indicate that the protective effects conferred to enzymes immobilized by physical adsorption to SBA-15 are driven by the enzymes' electrostatic attraction to the material's surface. The pore diameter of SBA-15 affects the quality of protection given to immobilized enzymes, but the contribution of this effect at different pH values remains unclear 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Enzymes, Immobilized  |2 NLM 
650 7 |a Myoglobin  |2 NLM 
650 7 |a SBA-15  |2 NLM 
650 7 |a Silicon Dioxide  |2 NLM 
650 7 |a 7631-86-9  |2 NLM 
650 7 |a Muramidase  |2 NLM 
650 7 |a EC 3.2.1.17  |2 NLM 
650 7 |a Chaperonins  |2 NLM 
650 7 |a EC 3.6.1.-  |2 NLM 
700 1 |a Liu, Jichuan  |e verfasserin  |4 aut 
700 1 |a Nigra, Michael  |e verfasserin  |4 aut 
700 1 |a Coppens, Marc-Olivier  |e verfasserin  |4 aut 
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773 1 8 |g volume:32  |g year:2016  |g number:37  |g day:20  |g month:09  |g pages:9604-10 
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