期刊
CHEMSUSCHEM
卷 15, 期 9, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cssc.202102657
关键词
biocatalysis; carboxylic acids; lipases; oligoesters; polycondensation
资金
- European Union [101029444]
- Universita degli Studi di Trieste
- Regione Piemonte
- Marie Curie Actions (MSCA) [101029444] Funding Source: Marie Curie Actions (MSCA)
The lipase-catalyzed polycondensation of azelaic acid and glycerol was investigated using a Design-of-Experiment approach. The study provided rational guidelines for optimizing the reaction and successfully scaled it up for industrial use.
The lipase-catalyzed polycondensation of azelaic acid and glycerol is investigated according to a Design-of-Experiment approach that helps to elucidate the effect of experimental variables on monomer conversion, M-n and regioselectivity of acylation of glycerol. Chemometric analysis shows that after 24 h the reaction proceeds regardless of the presence of the enzyme. Accordingly, the biocatalyst was removed after a first step of synthesis and the chain elongation continued at 80 degrees C. That allowed the removal of the biocatalyst and the preservation of its activity: pre-requites for efficient applicability at industrial scale. The experimental study, combined with docking-based computational analysis, provides rational guidelines for the optimization of the regioselective acylation of glycerol. The process is scaled up to 73.5 g of monomer. The novelty of the present study is the rigorous control of the reaction conditions and of the integrity of the immobilized biocatalyst, which serve to avoiding any interference of free enzyme or fines released in the reaction mixture. The quantitative analysis of the effect of experimental conditions and the overcoming of some major technical bottlenecks for the scalability of enzymatic polycondensation opens new scenarios for industrial exploitation.
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