Catalytic Activation of Esterases by PEGylation for Polyester Synthesis

Noro, Jennifer; Castro, Tarsila G.; Gonçalves, Filipa; Ribeiro, Artur; Silva, Carla

doi:10.1002/cctc.201900451

Cited by 14 publications

(24 citation statements)

References 52 publications

(65 reference statements)

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“…Noro et al. [ 73 ] reported the PEGylation of three different enzymes, namely lipase from CALB, lipase from TL, and cutinase from Fusarium solani pisi , using a monofunctional PEG (5000 Da). The PEGylation resulted in the isolation of the enzymes with at least 50% of the lysines modified.…”

Section: Improvement Of Lipases’ Propertiesmentioning

confidence: 99%

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Chemical modification of lipases: A powerful tool for activity improvement

Noro

Cavaco‐Paulo

Silva

2022

Biotechnology Journal

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The demand for adequate and ecologically acceptable procedures to produce the most differentiated products has been growing in recent decades, with enzymes being excellent examples of the advances achieved so far. Lipases are astonishing catalysts with a vast range of applications including the synthesis of esters, flavors, biodiesel, and polymers. The broad specificity of the substrates, as well as the regio-, stereo-, and enantioselectivity, are the differentiating factors of these enzymes. Structural modification is a current approach to enhance the activity of lipases. Chemical modification of lipases to improve catalytic performance is of great interest considering the increasingly broad fields of application. Together with the physical immobilization onto solid supports, different strategies have been developed to produce catalysts with higher activity and stability. In this review, practical insights into the different strategies developed in recent years regarding the modification of lipases are described. For the first time, the impact of the modifications on the activity and stability of lipases, as well as on the biotechnological applications, is fully compiled.

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Section: Improvement Of Lipases’ Propertiesmentioning

confidence: 99%

“…This strategy showed the potential of the modified enzymes for the synthesis of polyesters with potential for application in differentiated fields like textiles or biomedical. [ 73 ]…”

Section: Improvement Of Lipases’ Propertiesmentioning

confidence: 99%

Chemical modification of lipases: A powerful tool for activity improvement

Noro

Cavaco‐Paulo

Silva

2022

Biotechnology Journal

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“…The data revealed a higher polymerase activity for the lipase TL and cutinase PEGylated forms. This may be due to a more open active site cavity for the PEGylated catalysts facilitating the catalysis [ 215 ].…”

Section: Biocatalysis Engineeringmentioning

confidence: 99%

Prospects of Using Biocatalysis for the Synthesis and Modification of Polymers

Nikulin

Švedas

2021

Molecules

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Trends in the dynamically developing application of biocatalysis for the synthesis and modification of polymers over the past 5 years are considered, with an emphasis on the production of biodegradable, biocompatible and functional polymeric materials oriented to medical applications. The possibilities of using enzymes not only as catalysts for polymerization but also for the preparation of monomers for polymerization or oligomers for block copolymerization are considered. Special attention is paid to the prospects and existing limitations of biocatalytic production of new synthetic biopolymers based on natural compounds and monomers from biomass, which can lead to a huge variety of functional biomaterials. The existing experience and perspectives for the integration of bio- and chemocatalysis in this area are discussed.

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“…Higher degree of polymerization and conversion yield were obtained in the biosynthesis of a polyester, poly(ethylene glutarate). [14] The chemical modification of lipase TL by grafting small hydrophobic aldehydes and isothiocyanates to the exposed lysine residues at the enzymes' surface, was recently reported by us. Besides higher thermostability, the modified enzyme revealed also improved activity for the hydrolysis of differentiated chain-length substrates.…”

Section: Introductionmentioning

confidence: 95%

Chemically Modified Lipase from Thermomyces lanuginosus with Enhanced Esterification and Transesterification Activities

2021

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Lipase from Thermomyces lanuginosus is one of the most explored enzymes for the esterification of several added-value industrial compounds, such as biodiesel, fragrances, and flavors. Its selectivity in these reactions is mostly related with its activity towards small alcohols. In this work, the impact of the chemical modification, with 4 dodecyl chains at its surface, was evaluated regarding its transesterification and esterification activities, comparing with the native form. Linear size-differentiated alcohols (from 1 to 20 carbons in the aliphatic chain) were used to explore for the first time the effect of the chain length in both transesterification and esterification reactions, using p-nitrophenyl palmitate and oleic acid as model compounds, respectively. The chemically modified lipase showed an outstanding improvement of its catalytic performance than the native enzyme, being this increase directly proportional to the size of the alcohols chain used as substrates. The enormous potential and remarkable versatility of this novel super catalyst was here demonstrated, where diverse types of esters, differing in their potential applications (biodiesel, cosmetics, fine chemistry), were efficiently synthesized. The produced esters were fully characterized by 1 H NMR, GC-MS, and FTIR.

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Catalytic Activation of Esterases by PEGylation for Polyester Synthesis

Cited by 14 publications

References 52 publications

Chemical modification of lipases: A powerful tool for activity improvement

Chemical modification of lipases: A powerful tool for activity improvement

Prospects of Using Biocatalysis for the Synthesis and Modification of Polymers

Chemically Modified Lipase from Thermomyces lanuginosus with Enhanced Esterification and Transesterification Activities

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