Lipase-Catalyzed Polymerization of Glycerol and Dicarboxylic Acids in an Organic Medium

Pessagno, Romina C.; Baldessari, Alicia

doi:10.3390/50300372

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“…Reduced reaction temperatures and catalyst regioselectivity allows inclusion of thermally sensitive building blocks and creation of novel structures. [19][20][21] The above facts prompted us to investigate the synthesis of novel amphiphilic polymers based on glycerol as a synthon. Further, the other synthon poly[ethylene glycol bis(carboxymethyl) ether] dimethylester was chosen as PEG-based polymers are known to be non-toxic, biocompatible, and are approved for most medical and pharmaceutical applications.…”

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confidence: 99%

Biocatalytic Approach for the Synthesis of Glycerol‐Based Macroamphiphiles and their Self‐Assembly to Micellar Nanotransporters

Gupta

Pandey

Levón

et al. 2010

Macro Chemistry & Physics

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Glycerol is one of the most versatile and valuable chemical substances and is utilized in a variety of commercial products with no known adverse pharmacological or environmental effects. Moreover, it exhibits good chemical stability and inertness under biological conditions. We have designed and developed Candida antarctica lipase (CAL B) catalyzed biocatalytic method to synthesize novel polymeric systems using glycerol and poly[ethylene glycol bis(carboxymethyl) ether] dimethylester. Both synthons are biocompatible, non‐toxic, and are readily available. The polymerization occurs regioselectively through the primary hydroxyl groups of glycerol leaving the secondary hydroxyls for post‐polymerization chemical modifications and also for attaching drugs/bioactive molecules. We have utilized these sites for the synthesis of amphiphilic polymers by attaching alkyl chains at the secondary hydroxyl groups simply by acylation. The drug encapsulation abilities of the resulting polymers have been evaluated for potential biomedical applications.magnified image

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confidence: 99%

Biocatalytic Approach for the Synthesis of Glycerol‐Based Macroamphiphiles and their Self‐Assembly to Micellar Nanotransporters

Gupta

Pandey

Levón

et al. 2010

Macro Chemistry & Physics

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“…Studies have shown that Candida antarctica lipase B is an effective catalyst for polymerization, and is quickly gaining attention in the polymer production industry for being cost-effective and a more environmentally friendly alternative than the currently used chemical catalysts. (Pessagno and Baldessari 2000).…”

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confidence: 99%

Functional Expression and Characterization of a Truncated Candida antarctica Lipase B in Yeast

Robinson

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and their respective research groups at the USDA for their collaboration and insight on this project. And finally, I would like to thank my family, friends, and especially my partner, Michael, for giving me the continuous support and encouragement needed to complete this project. S.M.R. viii 22. Michaelis-Menten plot for the substrate p-NPB ranging from 40-1000 µM and the truncated CalB enzyme using the method of Blank et al. (2006). 23. Michaelis-Menten plot for the substrate p-NPB ranging from 40-6000 µM and the truncated CalB enzyme using the method of Blank et al. (2006). 24. Michaelis-Menten plot for the substrate p-NPB ranging from 40-20000 µM and the truncated CalB enzyme using the method of Martinelle et al. (1995). 25. Michaelis-Menten plot for the substrate p-NPB ranging from 40-20000 µM and the full-length CalB enzyme using the method of Martinelle et al. (1995).

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Lipase-Catalyzed Polymerization of Glycerol and Dicarboxylic Acids in an Organic Medium

Abstract: Abstract:Lipases from different sources catalyze the polyesterification of glycerol and several dicarboxylic acids in presence or organic solvents

Cited by 2 publications

References 2 publications

Biocatalytic Approach for the Synthesis of Glycerol‐Based Macroamphiphiles and their Self‐Assembly to Micellar Nanotransporters

Biocatalytic Approach for the Synthesis of Glycerol‐Based Macroamphiphiles and their Self‐Assembly to Micellar Nanotransporters

Functional Expression and Characterization of a Truncated Candida antarctica Lipase B in Yeast

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