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Abstract
The ring-opening polymerization of δ-valerolactone catalyzed by a thermophilic esterase from the archaeon Archaeoglobus fulgidus was successfully conducted in organic solvents. The effects of enzyme concentration, temperature, reaction time and reaction medium on monomer conversion and product molecular weight were systematically evaluated. Through the optimization of reaction conditions, poly(δ-valerolactone) was produced in 97% monomer conversion, with a number-average molecular weight of 2225 g/mol, in toluene at 70 °C for 72 h. This paper has produced a new biocatalyst for the synthesis of poly(δ-valerolactone), and also deeper insight has been gained into the mechanism of thermophilic esterase-catalyzed ring-opening polymerization.
Highlights
Poly(δ-valerolactone) (PVL) is an important aliphatic polyester due to its good biodegradability, biocompatibility, and permeability characteristics
Previous work in our laboratory showed that a recombinant Escherichia coli whole-cell biocatalyst harboring the thermophilic lipase gene FN1333 could efficiently catalyze the ring-opening polymerization of δ-valerolactone, with monomer conversion of 97% and product Mn value of 1020 g/mol at 70 °C in toluene [12]
The SDS-PAGE analysis showed a major band at 35.5 kDa, which corresponded to the enzyme AFEST, and the purity was more than 92% (Figure 1)
Summary
Poly(δ-valerolactone) (PVL) is an important aliphatic polyester due to its good biodegradability, biocompatibility, and permeability characteristics. Through the optimization of reaction conditions (enzyme origin, temperature, reaction medium and time), PVL was successfully synthesized in a biocatalytic route, with the highest monomer conversion and number-average molecular weight (Mn) of 98% and 3200 g/mol, respectively [10]. Candida antarctica lipase B (CALB) could be realized, producing a product with a degree of polymerization of only 25 [11] Similar to these results, previous work in our laboratory showed that a recombinant Escherichia coli whole-cell biocatalyst harboring the thermophilic lipase gene FN1333 could efficiently catalyze the ring-opening polymerization of δ-valerolactone, with monomer conversion of 97% and product Mn value of 1020 g/mol at 70 °C in toluene [12]. Systematical optimization of the reaction conditions was performed to obtain high monomer conversion and product molecular weight, and was helpful for gaining deeper insight into the mechanism underlying the effects of the reaction conditions
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