Enzyme stabilization by nano/microsized hybrid materials. Issue 1 (28th August 2012)
- Record Type:
- Journal Article
- Title:
- Enzyme stabilization by nano/microsized hybrid materials. Issue 1 (28th August 2012)
- Main Title:
- Enzyme stabilization by nano/microsized hybrid materials
- Authors:
- Hwang, Ee Taek
Gu, Man Bock - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Immobilization is a key technology for successful realization of enzyme‐based industrial processes, particularly for production of green and sustainable energy or chemicals from biomass‐derived catalytic conversion. Different methods to immobilize enzymes are critically reviewed. In principle, enzymes are immobilized via three major routes (i) binding to a support, (ii) encapsulation or entrapment, or (iii) cross‐linking (carrier free). As a result, immobilizing enzymes on certain supports can enhance storage and operational stability. In addition, recent breakthroughs in nano and hybrid technology have made various materials more affordable hosts for enzyme immobilization. This review discusses different approaches to improve enzyme stability in various materials such as nanoparticles, nanofibers, mesoporous materials, sol–gel silica, and alginate‐based microspheres. The advantages of stabilized enzyme systems are from its simple separation and ease recovery for reuse, while maintaining activity and selectivity. This review also considers the latest studies conducted on different enzymes immobilized on various support materials with immense potential for biosensor, antibiotic production, food industry, biodiesel production, and bioremediation, because stabilized enzyme systems are expected to be environmental friendly, inexpensive, and easy to use for enzyme‐based industrial<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Immobilization is a key technology for successful realization of enzyme‐based industrial processes, particularly for production of green and sustainable energy or chemicals from biomass‐derived catalytic conversion. Different methods to immobilize enzymes are critically reviewed. In principle, enzymes are immobilized via three major routes (i) binding to a support, (ii) encapsulation or entrapment, or (iii) cross‐linking (carrier free). As a result, immobilizing enzymes on certain supports can enhance storage and operational stability. In addition, recent breakthroughs in nano and hybrid technology have made various materials more affordable hosts for enzyme immobilization. This review discusses different approaches to improve enzyme stability in various materials such as nanoparticles, nanofibers, mesoporous materials, sol–gel silica, and alginate‐based microspheres. The advantages of stabilized enzyme systems are from its simple separation and ease recovery for reuse, while maintaining activity and selectivity. This review also considers the latest studies conducted on different enzymes immobilized on various support materials with immense potential for biosensor, antibiotic production, food industry, biodiesel production, and bioremediation, because stabilized enzyme systems are expected to be environmental friendly, inexpensive, and easy to use for enzyme‐based industrial applications.</p> </abstract> … (more)
- Is Part Of:
- Engineering in life sciences. Volume 13:Issue 1(2013:Jan.)
- Journal:
- Engineering in life sciences
- Issue:
- Volume 13:Issue 1(2013:Jan.)
- Issue Display:
- Volume 13, Issue 1 (2013)
- Year:
- 2013
- Volume:
- 13
- Issue:
- 1
- Issue Sort Value:
- 2013-0013-0001-0000
- Page Start:
- 49
- Page End:
- 61
- Publication Date:
- 2012-08-28
- Subjects:
- Bioengineering -- Periodicals
660.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1618-2863 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/elsc.201100225 ↗
- Languages:
- English
- ISSNs:
- 1618-0240
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3764.680000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3417.xml