Advances in enzyme immobilisation

Brady, Dean; Jordaan, Justin

doi:10.1007/s10529-009-0076-4

Cited by 747 publications

(510 citation statements)

References 81 publications

(99 reference statements)

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“…However, the enormous catalytic potential offered by the enzymes for innumerable transformations, has stimulated intense studies aimed at the improvement of their properties (Mateo et al 2007;Brady and Jordon 2009;FernandezLafuente 2009;Garcia-Galan et al 2011;Cowan and Fernandez-Lafuente 2011;Rodrigues et al 2013). Among several methods of this improvement that have been proposed, an immobilization of the enzymes is apparently most widely applied (Zhao 2010;Rodrigues et al 2011;Hanefeld et al 2013).…”

Section: General Overviewmentioning

confidence: 99%

Enzyme immobilization by adsorption: a review

2014

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Endowed with unparalleled high catalytic activity and selectivity, enzymes offer enormous potential as catalysts in practical applications. These applications, however, are seriously hampered by enzymes' low thermal and chemical stabilities. One way to improve these stabilities is the enzyme immobilization. Among various tested methods of this process that make use of different enzyme-carrier interactions, immobilization by adsorption on solid carriers has appeared most common. According to these findings, in this review we present a comparative analysis of the literature reports on the recent trends in the immobilization of the enzymes by adsorption. This thorough study was prepared in order to provide a deeper understanding of the process. Both carriers, carrier modifiers and procedures developed for effective adsorption of the enzymes are discussed. The review may thus be helpful in choosing the right adsorption scheme for a given enzyme to achieve the improvement of its stability and activity for a specific application.

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Section: General Overviewmentioning

confidence: 99%

Enzyme immobilization by adsorption: a review

2014

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“…Immobilized enzyme has a lot of advantages over free enzyme including improved storage stability and easy retrieval for re-use (Brady et al, 2009;Sheldon et al, 2013). Also, immobilization enhances enzyme specificity and activity (Pollard et al, 2007;Woodley, 2008;Garcia-Galan et al, 2011), reduces the possibility of contamination by microbes (Singh, 2008), decreases the cost of continuous production, and improves purity of the final products (D'Souza, 1999).…”

Section: Brazilian Journal Of Chemical Engineeringmentioning

confidence: 99%

Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Liu

Sun

et al. 2014

Braz. J. Chem. Eng.

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-For immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 on DEAE-52 cellulose, the optimal amount of enzyme protein was 12 mg protein: 1 g DEAE-52 cellulose; the optimal pH was 6.5; and the optimal immobilization time was 6 hr. The specific activity of immobilized enzyme was 36.67 mU.g -1 carrier with an immobilization yield of 98.87% and an enzyme recovery yield of 92.43%. The molar transformation rates of puerarin by immobilized enzyme and by the relative bacterial cell amount equal to the same amount of enzyme were 53.3% and 2.2%, respectively, after 1 hr of transformation. The former molar transformation rate, which was similar to that for free enzyme, was more than 24-fold greater than the latter. The immobilized puerarin glycosidase showed improved enzymatic properties and stability. The immobilized puerarin glycosidase retained 88% of its initial activity after being reused 10 times.

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“…Unfortunately, natural enzymes are often not optimally suited for industrial applications, which can be hampered by their lack of long-term stability under process conditions and by their difficult recovery and recycling. These drawbacks can, however, be overcome by immobilization of the enzymes [1][2][3][4].…”

Section: Introductionmentioning

confidence: 99%

Sucrose phosphorylase as cross‐linked enzyme aggregate: Improved thermal stability for industrial applications

Cerdobbel

Winter

Desmet

et al. 2010

Biotechnology Journal

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Sucrose phosphorylase is an interesting biocatalyst that can glycosylate a variety of small molecules using sucrose as a cheap but efficient donor substrate. The low thermostability of the enzyme, however, limits its industrial applications, as these are preferably performed at 60°C to avoid microbial contamination. Cross‐linked enzyme aggregates (CLEAs) of the sucrose phosphorylase from Bifidobacterium adolescentis were found to have a temperature optimum that is 17°C higher than that of the soluble enzyme. Furthermore, the immobilized enzyme displays an exceptional thermostability, retaining all of its activity after 1 week incubation at 60°C. Recycling of the biocatalyst allows its use in at least ten consecutive reactions, which should dramatically increase the commercial potential of its glycosylating activity.

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Advances in enzyme immobilisation

Cited by 747 publications

References 81 publications

Enzyme immobilization by adsorption: a review

Enzyme immobilization by adsorption: a review

Immobilization of puerarin glycosidase from Microbacterium oxydans CGMCC 1788 increases puerarin transformation efficiency

Sucrose phosphorylase as cross‐linked enzyme aggregate: Improved thermal stability for industrial applications

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