CCL

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001-es BibID:BIBFORM103963
035-os BibID:(WOS)000522021900002 (Scopus)85082415468
Első szerző:Todea, Anamaria
Cím:Thermal behavior of oligo[(epsilon-caprolactone)-co-delta-gluconolactone] enzymatically synthesized in reaction conditions optimized by experimental design / Anamaria Todea, Diana Aparaschivei, Ioan Bîtcan, Ionuț Valentin Ledeți, Geza Bandur, Francisc Péter, Lajos Nagy, Sándor Kéki, Emese Biró
Dátum:2020
ISSN:1388-6150 1588-2926
Megjegyzések:The thermal behavior of co-oligomers of epsilon-caprolactone (ECL) with gluconolactone, compared to the epsilon-caprolactone oligomer, has been assessed by thermogravimetric analysis, while differential scanning calorimetry was used to evaluate the melting comportment. As the insertion of more hydrophilic structural units can improve the properties and functionalities of the ECL oligoesters, the enzymatic in vitro oligomerization process was optimized by a 3-factorial/3-level experimental design, using the Box-Behnken method. The selected independent variables were the temperature, the enzyme amount, and the molar ratio of monomers, while the co-oligomerization degree and the mass average molecular mass (calculated from MALDI-TOF MS data) were the response variables. The results indicate that temperature has the most significant effect and is directly correlated with the formation of linear co-oligoesters. The overall effect of the other variables was also significant. The thermogravimetric analysis of the co-oligomer synthesized in the optimized conditions indicated a decrease of the thermal stability and compared to the ECL oligomer. Thermoanalytical techniques can consistently improve the utilization efficiency of polymer-based formulations in pharmaceutical and medical applications.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Biocatalysis
Enzymatic oligomerization
Thermal analysis
Lipaseepsilon-caprolactone
delta-gluconolactone
Megjelenés:Journal of Thermal Analysis and Calorimetry. - 141 : 3 (2020), p. 1017-1026. -
További szerzők:Aparaschivei, Diana Bîtcan, Ioan Ledeți, Ionuț Valentin Bandur, Geza Péter, Francisc Nagy Lajos (1979-) (vegyész) Kéki Sándor (1964-) (polimer kémikus) Biro, Emese
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001-es BibID:BIBFORM084756
Első szerző:Todea, Anamaria
Cím:Optimization of enzymatic ring-opening copolymerizations involving delta-gluconolactone as monomer by experimental design / Anamaria Todea, Emese Biro, Valentin Badea, Cristina Paul, Adinela Cimporescu, Lajos Nagy, Sándor Kéki, Geza Bandur, Carmen Boeriu, Francisc Péter
Dátum:2014
ISSN:0033-4545 1365-3075
Megjegyzések:Enzymatic incorporation of carbohydrate-derived monomer units into hydrophobic polyester backbones represents a promising alternative to obtain new biodegradable oligomers and polymers. Immobilized lipases are efficient biocatalysts for copolymerization of β-butyrolactone and delta-gluconolactone, but only a systematic optimization study was able to highlight the influence of the main reaction parameters on the polymerization degree and on the relative copolymer content of the product. Therefore, experimental design was employed for determination of the optimal ring-opening copolymerization conditions in solventless reaction systems, at temperatures up to 80 °C. The obtained products, cyclic and linear polyesters, have been characterized by FT-IR, MALDI-TOF MS, NMR, and TG analysis, demonstrating the incorporation of gluconolactone unit(s) into the hydrophobic backbone of the polyester and the formation of new bio-based products.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
biocatalysis
experimental design
lipase
modeling
POC-2014
polymerization
delta-gluconolactone
Megjelenés:Pure And Applied Chemistry. - 86 : 11 (2014), p. 1781-1792. -
További szerzők:Biro, Emese Badea, Valentin Paul, Cristina Cimporescu, Adinela Nagy Lajos (1979-) (vegyész) Kéki Sándor (1964-) (polimer kémikus) Bandur, Geza Boeriu, Carmen G. Péter, Francisc
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DOI
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