Enzymes immobilized in mesoporous silica: A physical–chemical perspective
Mesoporous materials as support for immobilized enzymes have been explored extensively during the last two decades, primarily not only for biocatalysis applications, but also for biosensing, biofuels and enzyme-controlled drug delivery. The activity of the immobilized enzymes inside the pores is oft...
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| Published in | Advances in colloid and interface science Vol. 205; pp. 339 - 360 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Amsterdam
Elsevier B.V
01.03.2014
Elsevier |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Mesoporous materials as support for immobilized enzymes have been explored extensively during the last two decades, primarily not only for biocatalysis applications, but also for biosensing, biofuels and enzyme-controlled drug delivery. The activity of the immobilized enzymes inside the pores is often different compared to that of the free enzymes, and an important challenge is to understand how the immobilization affects the enzymes in order to design immobilization conditions that lead to optimal enzyme activity. This review summarizes methods that can be used to understand how material properties can be linked to changes in enzyme activity. Real-time monitoring of the immobilization process and techniques that demonstrate that the enzymes are located inside the pores is discussed by contrasting them to the common practice of indirectly measuring the depletion of the protein concentration or enzyme activity in the surrounding bulk phase. We propose that pore filling (pore volume fraction occupied by proteins) is the best standard for comparing the amount of immobilized enzymes at the molecular level, and present equations to calculate pore filling from the more commonly reported immobilized mass. Methods to detect changes in enzyme structure upon immobilization and to study the microenvironment inside the pores are discussed in detail. Combining the knowledge generated from these methodologies should aid in rationally designing biocatalyst based on enzymes immobilized in mesoporous materials.
[Display omitted]
•Calculating pore filling as standard for comparing different mesoporous particles•Techniques for real time study of the immobilization process•Visualization of enzymes in the pores by microscopy•Methods for studying conformational changes of enzymes•Study of the microenvironment inside the pores as a function of material properties |
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| AbstractList | Mesoporous materials as support for immobilized enzymes have been explored extensively during the last two decades, primarily not only for biocatalysis applications, but also for biosensing, biofuels and enzyme-controlled drug delivery. The activity of the immobilized enzymes inside the pores is often different compared to that of the free enzymes, and an important challenge is to understand how the immobilization affects the enzymes in order to design immobilization conditions that lead to optimal enzyme activity. This review summarizes methods that can be used to understand how material properties can be linked to changes in enzyme activity. Real-time monitoring of the immobilization process and techniques that demonstrate that the enzymes are located inside the pores is discussed by contrasting them to the common practice of indirectly measuring the depletion of the protein concentration or enzyme activity in the surrounding bulk phase. We propose that pore filling (pore volume fraction occupied by proteins) is the best standard for comparing the amount of immobilized enzymes at the molecular level, and present equations to calculate pore filling from the more commonly reported immobilized mass. Methods to detect changes in enzyme structure upon immobilization and to study the microenvironment inside the pores are discussed in detail. Combining the knowledge generated from these methodologies should aid in rationally designing biocatalyst based on enzymes immobilized in mesoporous materials.
[Display omitted]
•Calculating pore filling as standard for comparing different mesoporous particles•Techniques for real time study of the immobilization process•Visualization of enzymes in the pores by microscopy•Methods for studying conformational changes of enzymes•Study of the microenvironment inside the pores as a function of material properties Mesoporous materials as support for immobilized enzymes have been explored extensively during the last two decades, primarily not only for biocatalysis applications, but also for biosensing, biofuels and enzyme-controlled drug delivery. The activity of the immobilized enzymes inside the pores is often different compared to that of the free enzymes, and an important challenge is to understand how the immobilization affects the enzymes in order to design immobilization conditions that lead to optimal enzyme activity. This review summarizes methods that can be used to understand how material properties can be linked to changes in enzyme activity. Real-time monitoring of the immobilization process and techniques that demonstrate that the enzymes are located inside the pores is discussed by contrasting them to the common practice of indirectly measuring the depletion of the protein concentration or enzyme activity in the surrounding bulk phase. We propose that pore filling (pore volume fraction occupied by proteins) is the best standard for comparing the amount of immobilized enzymes at the molecular level, and present equations to calculate pore filling from the more commonly reported immobilized mass. Methods to detect changes in enzyme structure upon immobilization and to study the microenvironment inside the pores are discussed in detail. Combining the knowledge generated from these methodologies should aid in rationally designing biocatalyst based on enzymes immobilized in mesoporous materials. Mesoporous materials as support for immobilized enzymes have been explored extensively during the last two decades, primarily not only for biocatalysis applications, but also for biosensing, biofuels and enzyme-controlled drug delivery. The activity of the immobilized enzymes inside the pores is often different compared to that of the free enzymes, and an important challenge is to understand how the immobilization affects the enzymes in order to design immobilization conditions that lead to optimal enzyme activity. This review summarizes methods that can be used to understand how material properties can be linked to changes in enzyme activity. Real-time monitoring of the immobilization process and techniques that demonstrate that the enzymes are located inside the pores is discussed by contrasting them to the common practice of indirectly measuring the depletion of the protein concentration or enzyme activity in the surrounding bulk phase. We propose that pore filling (pore volume fraction occupied by proteins) is the best standard for comparing the amount of immobilized enzymes at the molecular level, and present equations to calculate pore filling from the more commonly reported immobilized mass. Methods to detect changes in enzyme structure upon immobilization and to study the microenvironment inside the pores are discussed in detail. Combining the knowledge generated from these methodologies should aid in rationally designing biocatalyst based on enzymes immobilized in mesoporous materials.Mesoporous materials as support for immobilized enzymes have been explored extensively during the last two decades, primarily not only for biocatalysis applications, but also for biosensing, biofuels and enzyme-controlled drug delivery. The activity of the immobilized enzymes inside the pores is often different compared to that of the free enzymes, and an important challenge is to understand how the immobilization affects the enzymes in order to design immobilization conditions that lead to optimal enzyme activity. This review summarizes methods that can be used to understand how material properties can be linked to changes in enzyme activity. Real-time monitoring of the immobilization process and techniques that demonstrate that the enzymes are located inside the pores is discussed by contrasting them to the common practice of indirectly measuring the depletion of the protein concentration or enzyme activity in the surrounding bulk phase. We propose that pore filling (pore volume fraction occupied by proteins) is the best standard for comparing the amount of immobilized enzymes at the molecular level, and present equations to calculate pore filling from the more commonly reported immobilized mass. Methods to detect changes in enzyme structure upon immobilization and to study the microenvironment inside the pores are discussed in detail. Combining the knowledge generated from these methodologies should aid in rationally designing biocatalyst based on enzymes immobilized in mesoporous materials. Mesoporous materials as support for immobilized enzymes have been explored extensively during the last two decades, primarily not only for biocatalysis applications, but also for biosensing, biofuels and enzyme-controlled drug delivery. The activity of the immobilized enzymes inside the pores is often different compared to that of the free enzymes, and an important challenge is to understand how the immobilization affects the enzymes in order to design immobilization conditions that lead to optimal enzyme activity. This review summarizes methods that can be used to understand how material properties can be linked to changes in enzyme activity. Real-time monitoring of the immobilization process and techniques that demonstrate that the enzymes are located inside the pores is discussed by contrasting them to the common practice of indirectly measuring the depletion of the protein concentration or enzyme activity in the surrounding bulk phase. We propose that pore filling (pore volume fraction occupied by proteins) is the best standard for comparing the amount of immobilized enzymes at themolecular level, and present equations to calculate pore filling from the more commonly reported immobilized mass. Methods to detect changes in enzyme structure upon immobilization and to study the microenvironment inside the pores are discussed in detail. Combining the knowledge generated from these methodologies should aid in rationally designing biocatalyst based on enzymes immobilized in mesoporous materials. |
| Author | Åkerman, Björn Olsson, Lisbeth Carlsson, Nils Gustafsson, Hanna Thörn, Christian Holmberg, Krister |
| Author_xml | – sequence: 1 givenname: Nils surname: Carlsson fullname: Carlsson, Nils organization: Chalmers University of Technology, Department of Chemical and Biological Engineering, Physical Chemistry, 412 96 Gothenburg, Sweden – sequence: 2 givenname: Hanna surname: Gustafsson fullname: Gustafsson, Hanna organization: Chalmers University of Technology, Department of Chemical and Biological Engineering, Applied Surface Chemistry, 412 96 Gothenburg, Sweden – sequence: 3 givenname: Christian surname: Thörn fullname: Thörn, Christian organization: Chalmers University of Technology, Department of Chemical and Biological Engineering, Industrial Biotechnology, 412 96 Gothenburg, Sweden – sequence: 4 givenname: Lisbeth surname: Olsson fullname: Olsson, Lisbeth organization: Chalmers University of Technology, Department of Chemical and Biological Engineering, Industrial Biotechnology, 412 96 Gothenburg, Sweden – sequence: 5 givenname: Krister surname: Holmberg fullname: Holmberg, Krister email: kh@chalmers.se organization: Chalmers University of Technology, Department of Chemical and Biological Engineering, Applied Surface Chemistry, 412 96 Gothenburg, Sweden – sequence: 6 givenname: Björn surname: Åkerman fullname: Åkerman, Björn organization: Chalmers University of Technology, Department of Chemical and Biological Engineering, Physical Chemistry, 412 96 Gothenburg, Sweden |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28759962$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/24112562$$D View this record in MEDLINE/PubMed https://research.chalmers.se/publication/196308$$DView record from Swedish Publication Index |
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| CODEN | ACISB9 |
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| Snippet | Mesoporous materials as support for immobilized enzymes have been explored extensively during the last two decades, primarily not only for biocatalysis... |
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| SubjectTerms | Adsorption Biocatalysis Chemistry Chemistry, Physical Colloidal state and disperse state Enzyme Activation Enzyme immobilization Enzymes Enzymes - chemistry Enzymes - metabolism Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Exact sciences and technology General and physical chemistry Immobilization Mathematical analysis Mesoporous silica Microenvironment Models, Molecular Monitoring Optimization Particle Size Pore filling Porosity Porous materials Proteins Silicon Dioxide - chemistry Surface Properties |
| Title | Enzymes immobilized in mesoporous silica: A physical–chemical perspective |
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