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Abstract

Lipase Enzyme for Biomass Valorization †

by
Madalina Tudorache
Faculty of Chemistry, University of Bucharest, 4–12 Regina Elisabeta Av., 030018 Bucharest, Romania
Presented at the 17th International Symposium “Priorities of Chemistry for a Sustainable Development” PRIOCHEM, Bucharest, Romania, 27–29 October 2021.
Chem. Proc. 2022, 7(1), 65; https://doi.org/10.3390/chemproc2022007065
Published: 20 April 2022
Lipase enzymes are part of the hydrolases family acting on carboxylic ester bonds. Physiologically, the lipase catalyzed the hydrolysis of triglyceride, leading to di-/mono-glycerides, fatty acids and glycerol. Additionally, lipases can assist the inter-/trans-esterification reactions in nonaqueous media [1,2,3,4,5,6,7,8,9,10]. This versatile behavior makes lipases one of the most useful enzymes in industrial areas. The most significant applications of lipases have been mainly developed in the food, detergent and pharmaceutical industries. Actual industrial applications rely on fossil resources for most of the industrial production. However, these natural sources are limited and their stock cannot be refilled in a short time. In addition, they are expensive and their exploitation has a negative impact on the environment. These are the main arguments taken under consideration to launch the new world strategy with biomass as a renewable carbon source. Thus far, the biomass composition used as feedstock imposed at least three general platforms, such as sugar, terpenes and combustibles. In this context, our research group explored lignocellulose, turpentine [8,9] and oil [1,2,3,4,5,6,7] as biomass samples with promising perspectives of renewable C sources. Lipase-based biocatalysis systems were adapted for biomass valorization, leading to added-value products with high impact on food, cosmetics and pharmaceutical areas. Limonene/α-pinene/menthol derivatives, grafted lignin, silybin esters, glycerol carbonate and glycidol are a few examples of the reaction products based on lipase biocatalysis developed in our lab. More details about these aspects demonstrating the high impact of lipase on the efficiency of the biocatalysis process, especially for biomass as raw materials, will be provided during the lecture.

Funding

This research was funded by the PNCDI III PED project (contract No. 376PED/2020) from UEFISCDI, Romania.

Institutional Review Board Statement

Not applicable.

Informed Consent Statement

Not applicable.

Data Availability Statement

Not applicable.

Conflicts of Interest

The authors declare no conflict of interest.

References

  1. Tudorache, M.; Protesescu, L.; Negoi, A.; Parvulescu, V.I. Recyclable biocatalytic composites of lipase-linked magnetic macro-/nano-particles for glycerol carbonate synthesis. Appl. Catal. A Gen. 2012, 437, 90–95. [Google Scholar] [CrossRef]
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  4. Tudorache, M.; Nae, A.; Coman, S.; Parvulescu, V.I. Strategy of cross-linked enzyme aggregates onto magnetic particles adapted to the green design of biocatalytic synthesis of glycerol carbonate. RSC Adv. 2013, 3, 4052–4058. [Google Scholar] [CrossRef]
  5. Tudorache, M.; Gherghe, G.; Nae, A.; Matei, E.; Mercioniu, I.; Kemnitz, E.; Ritter, B.; Coman, S.; Parvulescu, V.I. Biocatalytic designs for the conversion of renewable glycerol into glycerol carbonate as a value-added product. Cent. Eur. J. Chem. 2014, 12, 1262–1270. [Google Scholar] [CrossRef]
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  7. Tudorache, M.; Negoi, A.; Protesescu, L.; Parvulescu, V.I. Biocatalytic alternative for bio-glycerol conversion with alkyl carbonates via a lipase-linked magnetic nano-particles assisted process. Appl. Catal. B 2014, 145, 120–125. [Google Scholar] [CrossRef]
  8. Tudorache, M.; Gheorghe, A.; Vianu, A.S.; Parvulescu, V.I. Biocatalytic epoxidation of α-pinene to oxy-derivatives over cross-linked lipase aggregates. J. Mol. Catal. B Enzym. 2016, 134, 9–15. [Google Scholar] [CrossRef]
  9. Tudorache, M.; Gheorghe, A.; Negoi, A.; Rnache, M.; Maria, G.M.; Parvulescu, V.I. Bifunctional carbohydrate biopolymers entrapped lipase as catalyst for the two consecutive conversions of α-pinene to oxy-derivatives. Carbohydr. Polym. 2016, 152, 726–733. [Google Scholar] [CrossRef] [PubMed]
  10. Tudorache, M.; Negoi, A.; Parvulescu, V.I. Enhancement of the valorization of renewable glycerol: The effects of the surfactant-enzyme interaction on the biocatalytic synthesis of glycerol carbonate. Catal. Today 2017, 279, 71–76. [Google Scholar] [CrossRef]
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MDPI and ACS Style

Tudorache, M. Lipase Enzyme for Biomass Valorization. Chem. Proc. 2022, 7, 65. https://doi.org/10.3390/chemproc2022007065

AMA Style

Tudorache M. Lipase Enzyme for Biomass Valorization. Chemistry Proceedings. 2022; 7(1):65. https://doi.org/10.3390/chemproc2022007065

Chicago/Turabian Style

Tudorache, Madalina. 2022. "Lipase Enzyme for Biomass Valorization" Chemistry Proceedings 7, no. 1: 65. https://doi.org/10.3390/chemproc2022007065

APA Style

Tudorache, M. (2022). Lipase Enzyme for Biomass Valorization. Chemistry Proceedings, 7(1), 65. https://doi.org/10.3390/chemproc2022007065

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