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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Self-assembled organic-inorganic hybrid glucoamylase nanoflowers with enhanced activity and stability.
TL;DR: The hybrid nanoflowers exhibited 204% enhanced activity recovery and two folds improvement in thermal stability in terms of half-life (in the range of 50-70°C) with respect to the free form and retained 70% residual activity after eight successive cycles indicating their excellent durability.
Journal ArticleDOI
Agro-industrial wastes as potential carriers for enzyme immobilization: A review.
TL;DR: This review provides a general overview of the suitability of different agro-industrial wastes for enzyme immobilization and the development of economic biocatalysts more sustainable to reduce environmental impacts, improve the application of enzymatic technology in industry.
Journal ArticleDOI
Development of simple protocols to solve the problems of enzyme coimmobilization. Application to coimmobilize a lipase and a β-galactosidase
Sara Peirce,Sara Peirce,Jose J. Virgen-Ortíz,Veymar G. Tacias-Pascacio,Nazzoly Rueda,Nazzoly Rueda,Rocio Bartolome-Cabrero,Laura Fernandez-Lopez,Maria Russo,Antonio Marzocchella,Roberto Fernandez-Lafuente +10 more
TL;DR: The proposed protocol permitted the reuse of the most stable enzyme after inactivation of the least stable one, and is compatible with any immobilization protocol of the first enzyme that does not involve ion exchange as only reason for enzyme immobilization.
Journal ArticleDOI
Engineering a more sustainable world through catalysis and green chemistry.
TL;DR: The bio-based economy involves cross-disciplinary research at the interface of biotechnology and chemical engineering, focusing on the development of green, chemo- and biocatalytic technologies for waste biomass conversion to biofuels, chemicals and bio- based materials.
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
TL;DR: Applications of protein-engineered biocatalysts ranging from commodity chemicals to advanced pharmaceutical intermediates that use enzyme catalysis as a key step are discussed.
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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
Alain Pierre,Gerard Pajonk +1 more
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.
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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.