Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions.

Autor: Miranda FC; Institute of Natural Resources, Federal University of Itajubá, Av. Benedito Pereira dos Santos, 1303, Itajubá, Minas Gerais 37500-903, Brazil., Oliveira KSGC; Department of Chemical Engineering, Federal University of São Carlos, Rod. Washington Luís, km 235, São Carlos, São Paulo 13565-905, Brazil., Tardioli PW; Department of Chemical Engineering, Federal Institute of Education, Science and Technology of the South of Minas Gerais, Av. Maria da Conceição Santos, 900, 37560-260 Pouso Alegre, Minas Gerais, Brazil., Fernandez-Lafuente R; Department of biocatalysis, Institute of Catalysis and Petrochemistry (ICP-CSIC), Campus UAM -CSIC, 28049 Madrid, Spain. Electronic address: rfl@icp.csic.es., Guimarães JR; Institute of Natural Resources, Federal University of Itajubá, Av. Benedito Pereira dos Santos, 1303, Itajubá, Minas Gerais 37500-903, Brazil. Electronic address: jrenatoguimaraes@unifei.edu.br.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Aug; Vol. 275 (Pt 1), pp. 133555. Date of Electronic Publication: 2024 Jul 01.
DOI: 10.1016/j.ijbiomac.2024.133555
Abstrakt: Here, we report a study of the effect of the blocking agent on the properties of the lipase from Thermomyces lanuginosus (TLL) immobilized on a heterofunctional support (Purolite C18-ethylnediamina (EDA)- vinyl sulfone (VS)-TLL-blocking agent) in different reactions. The performance of the biocatalysts was compared to those immobilized on standard hydrophobic support (Purolite C18-TLL) and the commercial one (TLL-IM). The nature of the blocking agent (Cys, Gly and Asp) altered the enzyme features. TLL-IM always gave a comparatively worse performance, with its specificity for the oil being very different to the Purolite biocatalysts. Under optimized conditions, Purolite C18-TLL yielded 97 % of hydrolysis conversion after 4 h using a water/waste cooking soybean oil (WCSO) mass ratio of 4.3, biocatalyst load of 6.5 wt% and a temperature of 44.2 °C (without buffer or emulsification agent). In esterification reactions of the purified free fatty acids (FFAs) obtained from WCSO, the best TLL biocatalysts depended on the utilized alcohol: linear amyl alcohol was preferred by Purolite C18-TLL and Purolite C18-EDA-VS-TLL-Gly, while higher activity was achieved utilizing isoamyl alcohol as nucleophile by Purolite C18-EDA-VS-TLL-Cys, Purolite C18-EDA-VS-TLL-Asp and IM-TLL as catalysts. All the results indicate the influence of the blocking step on the final biocatalyst features.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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