Enzyme immobilisation in biocatalysis : Why, what and how
Roger A. Sheldon,Sander van Pelt +1 more
TLDR
An overview of the why, what and how of enzyme immobilisation for use in biocatalysis is presented and emphasis is placed on relatively recent developments, such as the use of novel supports such as mesoporous silicas, hydrogels, and smart polymers, and cross-linked enzyme aggregates (CLEAs).Abstract:
In this tutorial review, an overview of the why, what and how of enzyme immobilisation for use in biocatalysis is presented. The importance of biocatalysis in the context of green and sustainable chemicals manufacture is discussed and the necessity for immobilisation of enzymes as a key enabling technology for practical and commercial viability is emphasised. The underlying reasons for immobilisation are the need to improve the stability and recyclability of the biocatalyst compared to the free enzyme. The lower risk of product contamination with enzyme residues and low or no allergenicity are further advantages of immobilised enzymes. Methods for immobilisation are divided into three categories: adsorption on a carrier (support), encapsulation in a carrier, and cross-linking (carrier-free). General considerations regarding immobilisation, regardless of the method used, are immobilisation yield, immobilisation efficiency, activity recovery, enzyme loading (wt% in the biocatalyst) and the physical properties, e.g. particle size and density, hydrophobicity and mechanical robustness of the immobilisate, i.e. the immobilised enzyme as a whole (enzyme + support). The choice of immobilisate is also strongly dependent on the reactor configuration used, e.g. stirred tank, fixed bed, fluidised bed, and the mode of downstream processing. Emphasis is placed on relatively recent developments, such as the use of novel supports such as mesoporous silicas, hydrogels, and smart polymers, and cross-linked enzyme aggregates (CLEAs).read more
Citations
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Make proper surfaces for immobilization of enzymes: Immobilization of lipase and α-amylase on modified Na-sepiolite.
Shiva Mortazavi,Hamidreza Aghaei +1 more
TL;DR: This paper has focused on making suitable carriers for the immobilization of α-amylase from Bacillus subtilis and lipase from Candida rugosa via adsorption on modified Na-sepiolite (SEP).
Journal ArticleDOI
Rapid In Situ Immobilization of Enzymes in Metal–Organic Framework Supports under Mild Conditions
Victoria Gascón,Cristina Carucci,Mayra B. Jiménez,Rosa M. Blanco,Manuel Sánchez-Sánchez,Edmond Magner +5 more
TL;DR: In this paper, the use of a metal organic framework (MOF) as a support for the in-situ immobilisation of enzymes is described, and the MOF support, a Basolite F300-like material, was prepared from FeCl3 and the tridentate linker trimesic acid.
Journal ArticleDOI
Tuneable 3D printed bioreactors for transaminations under continuous-flow
Edgar Peris,Obinna Okafor,Evelina Kulcinskaja,Ruth D. Goodridge,Santiago V. Luis,Eduardo García-Verdugo,Elaine O'Reilly,Victor Sans +7 more
TL;DR: A method to efficiently immobilize enzymes on 3D printed continuous-flow devices enables rapid screening of immobilization mechanisms and reaction conditions, simple transfer of optimised conditions into tailored printed microfluidic reactors and development of continuous- flow biocatalytic processes.
ComponentDOI
Development of an Engineered Ketoreductase with Simultaneously Improved Thermostability and Activity for Making a Bulky Atorvastatin Precursor
TL;DR: Using native ketoreductase LbCR, thermostability and activity were evolved separately by directed evolution, generating mutations V198I and M154I/A155D with increased thermostable and mutations A201D/A202L with increased enzymatic activity.
Journal ArticleDOI
Immobilized laccase in the form of (magnetic) cross-linked enzyme aggregates for sustainable diclofenac (bio)degradation
TL;DR: The promising results of DCF removal using CLEAs laccase and mCLEAs lAccase show that both immobilized forms of lacc enzyme have the potential to be used in cleaner industrial technologies, e.g. wastewater treatment.
References
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Engineering the third wave of biocatalysis
Uwe T. Bornscheuer,Gjalt W. Huisman,Romas J. Kazlauskas,Romas J. Kazlauskas,Stefan Lutz,Jeffrey C. Moore,Karen Robins +6 more
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Enzyme immobilization: The quest for optimum performance
TL;DR: Different methods for the immobilization of enzymes are critically reviewed, with emphasis on relatively recent developments, such as the use of novel supports, e.g., mesoporous silicas, hydrogels, and smart polymers, novel entrapment methods and cross-linked enzyme aggregates (CLEAs).
Journal ArticleDOI
Chemistry of Aerogels and Their Applications
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TL;DR: Aerogels form a new class of solids showing sophisticated potentialities for a range of applications, and can develop very attractive physical and chemical properties not achievable by other means of low temperature soft chemical synthesis.
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Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance
TL;DR: The advantages and disadvantages of the different existing immobilization strategies to solve the different aforementioned enzyme limitations are given and some advice to select the optimal strategy for each particular enzyme and process is given.
Journal ArticleDOI
Application of chitin- and chitosan-based materials for enzyme immobilizations: a review
TL;DR: A review of the literature on enzymes immobilized on chitin- and chitosan-based materials, covering the last decade, is presented in this paper, where one hundred fifty-eight papers on 63 immobilized enzymes for multiplicity of applications ranging from wine, sugar and fish industry, through organic compounds removal from wastewaters to sophisticated biosensors for both in situ measurements of environmental pollutants and metabolite control in artificial organs, are reviewed.