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Review

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

1
Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain
2
Departamento de Química Inorgánica e Instituto Universitario de Materiales, Universidad de Alicante, 03080 Alicante, Spain
3
Departamento de Química en Ciencias Farmacéuticas, Facultad de Farmacia, Universidad Complutense de Madrid, Plaza de Ramón y Cajal, s/n. 28040 Madrid, Spain
4
Biocatalysis and Enzyme Technology Lab, Institute of Food Science and Technology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, P.O. Box 15090, Porto Alegre 9500, Brazil
*
Authors to whom correspondence should be addressed.
Both authors have evenly contributed to this paper.
Catalysts 2020, 10(6), 605; https://doi.org/10.3390/catal10060605
Received: 12 May 2020 / Revised: 26 May 2020 / Accepted: 27 May 2020 / Published: 29 May 2020
(This article belongs to the Special Issue Multienzymatic Catalysis and/or Enzyme Co-immobilization)
Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes. View Full-Text
Keywords: lipases; combilipases; enzyme specificity; full modification; coimmobilization; cascade reaction lipases; combilipases; enzyme specificity; full modification; coimmobilization; cascade reaction
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MDPI and ACS Style

Arana-Peña, S.; Carballares, D.; Berenguer-Murcia, Á.; Alcántara, A.R.; Rodrigues, R.C.; Fernandez-Lafuente, R. One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates. Catalysts 2020, 10, 605. https://doi.org/10.3390/catal10060605

AMA Style

Arana-Peña S, Carballares D, Berenguer-Murcia Á, Alcántara AR, Rodrigues RC, Fernandez-Lafuente R. One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates. Catalysts. 2020; 10(6):605. https://doi.org/10.3390/catal10060605

Chicago/Turabian Style

Arana-Peña, Sara, Diego Carballares, Ángel Berenguer-Murcia, Andrés R. Alcántara, Rafael C. Rodrigues, and Roberto Fernandez-Lafuente. 2020. "One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates" Catalysts 10, no. 6: 605. https://doi.org/10.3390/catal10060605

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