Effect of the degree of cross-linking on the properties of different CLEAs of penicillin acylase

Wilson, Lorena; Illanes, Andrés; Soler, Lorena; Henriquez, M

doi:10.1016/j.procbio.2008.11.010

Cited by 41 publications

(31 citation statements)

References 46 publications

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“…Pchelintsev et al (2009) found that variation in the duration of the precipitation step prior to cross-linking influenced the activity and microstructure of penicillin acylase CLEA. Wilson et al (2009) discovered that excess cross-linking agent reduced the enzyme conversion yield, productivity and stability, while Majumder et al (2008) also noted that the degree of crosslinking influenced enantioselectivity.…”

Section: Self-immobilisationmentioning

confidence: 99%

Advances in enzyme immobilisation

Brady

Jordaan²

2009

Biotechnol Lett

750

482

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Improvements in current strategies for carrier-based immobilisation have been developed using hetero-functionalised supports that enhance the binding efficacy and stability through multipoint attachment. New commercial resins (Sepabeads) exhibit improved protein binding capacity. Novel methods of enzyme self-immobilisation have been developed (CLEC, CLEA, Spherezyme), as well as carrier materials (Dendrispheres), encapsulation (PEI Microspheres), and entrapment. Apart from retention, recovery and stabilisation, other advantages to enzyme immobilisation have emerged, such as enhanced enzyme activity, modification of substrate selectivity and enantioselectivity, and multi-enzyme reactions. These advances promise to enhance the roles of immobilisation enzymes in industry, while opening the door for novel applications.

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Section: Self-immobilisationmentioning

confidence: 99%

Advances in enzyme immobilisation

Brady

Jordaan²

2009

Biotechnol Lett

750

482

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“…1). It is well known that the immobilization yield strongly depends on the incubation time of the cross-linking step as well as on the GA / protein ratio [26]. These parameters have, therefore, been optimized for the production of CLEAs of SPase (Fig.…”

Section: Production Of Spase Cleasmentioning

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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“…Initial reaction rates of penicillin G hydrolysis were determined, at different penicillin G concentrations in 100 mM sodium phosphate buffer pH 7.8 and 30ºC, using a pH stat (Mettler Toledo, DL50) to titrate the H + produced by the hydrolysis of penicillin G as it is converted into PAA; 50 mM NaOH was employed as titrant solution (Wilson et al 2009). The amount of H + produced can be easily converted into the amount of hydrolyzed penicillin G according to the stoichiometry of the reaction.…”

Section: Analysesmentioning

confidence: 99%

Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading

Illanes¹,

González²,

Gómez³

et al. 2010

Electro Journal of Biotech

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factors at different bulk substrate concentrations were determined for all biocatalysts, values ranging from 0.78 for small particle size at 25 mM penicillin G to 0.15 for large particle size at 2 mM penicillin G. Enzyme protein loading had a strong impact on the effectiveness factors of immobilized penicillin G acylase, being it more pronounced in the case of large particle size biocatalysts. At conditions in which 6-aminopenicillanic acid is industrially produced, all biocatalysts tested were mass-transfer limited, being this information valuable for reactor design and performance evaluation.

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Effect of the degree of cross-linking on the properties of different CLEAs of penicillin acylase

Cited by 41 publications

References 46 publications

Advances in enzyme immobilisation

Advances in enzyme immobilisation

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

Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading

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