Esterification Process in Supercritical Carbon Dioxide Catalyzed by Geotrichum candidum Lipase Produced with Mozzarella Cheese Whey and Corn Steep Liquor

The valorization of industrial waste in the production of new products is a growing trend, with food waste showing significant promise as a raw material for various industries. Thus, this research aimed to investigate the production of Geotrichum candidum lipase using industrial waste, such as mozzarella cheese whey (MCW) and corn steep liquor (CSL), and to analyze how effectively it catalyzes the esterification of oleic acid with methanol. Lipase production was carried out in medium containing MCW and CSL, with fermentation conditions optimized using a fractional factorial experimental design and central composite experimental design. The highest activities (16.71 U/mL in 24 h and 17.80 U/mL in 48 h) were found in conditions of 13.6% (%w/v) CSL and 37.1% (%w/v) MCW, with corn oil fixed at 1% (%w/v) and pH fixed at 6,00. Esterification conditions were evaluated at atmospheric pressure, both in a solvent-free environment and using hexane, as well as under high pressures with supercritical carbon dioxide (SC-CO2). The produced lipase demonstrated high catalytic activity for the esterification reaction of oleic acid with methanol under SC-CO2 with an increase of 39.41% in the yield. The yields found confirm the feasibility of producing lipase from industrial waste, thus presenting it as a sustainable and efficient alternative for industrial processes, and show that there is no need to use toxic organic solvents in esterification reactions.

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Journal
Processes
Published
2024-09-26
DOI
https://doi.org/10.3390/pr12102086
Citations
2
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
0.47

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article

Esterification Process in Supercritical Carbon Dioxide Catalyzed by Geotrichum candidum Lipase Produced with Mozzarella Cheese Whey and Corn Steep Liquor

Alessandra Lopes de Oliveira, Paulo Rodolfo Ramos, Giselle Vallim Corrêa Ramos, Eliana Setsuko Kamimura
2 citations
Processes
Enzyme Catalysis and Immobilization
0.47
article

Esterification Process in Supercritical Carbon Dioxide Catalyzed by Geotrichum candidum Lipase Produced with Mozzarella Cheese Whey and Corn Steep Liquor

Alessandra Lopes de Oliveira, Paulo Rodolfo Ramos, Giselle Vallim Corrêa Ramos, Eliana Setsuko Kamimura
article en
2 citations

Abstract

The valorization of industrial waste in the production of new products is a growing trend, with food waste showing significant promise as a raw material for various industries. Thus, this research aimed to investigate the production of Geotrichum candidum lipase using industrial waste, such as mozzarella cheese whey (MCW) and corn steep liquor (CSL), and to analyze how effectively it catalyzes the esterification of oleic acid with methanol. Lipase production was carried out in medium containing MCW and CSL, with fermentation conditions optimized using a fractional factorial experimental design and central composite experimental design. The highest activities (16.71 U/mL in 24 h and 17.80 U/mL in 48 h) were found in conditions of 13.6% (%w/v) CSL and 37.1% (%w/v) MCW, with corn oil fixed at 1% (%w/v) and pH fixed at 6,00. Esterification conditions were evaluated at atmospheric pressure, both in a solvent-free environment and using hexane, as well as under high pressures with supercritical carbon dioxide (SC-CO2). The produced lipase demonstrated high catalytic activity for the esterification reaction of oleic acid with methanol under SC-CO2 with an increase of 39.41% in the yield. The yields found confirm the feasibility of producing lipase from industrial waste, thus presenting it as a sustainable and efficient alternative for industrial processes, and show that there is no need to use toxic organic solvents in esterification reactions.

ProcessesVol. 12(10)
Universidade de São Paulo (BR)
Fundação de Amparo à Pesquisa do Estado de São Paulo, Conselho Nacional de Desenvolvimento Científico e Tecnológico
Openalex Percentile: Top 35%
Enzyme Catalysis and Immobilization
0.47
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