title: A review on lipase-catalyzed reactions in ultrasound-assisted systems.
abstract: The named "green chemistry" has been receiving increasing prominence due to its environmentally friendly characteristics. The use of enzymes as catalysts in processes of synthesis to replace the traditional use of chemical catalysts present as main advantage the fact of following the principles of the green chemistry. However, processes of enzymatic nature generally provide lower yields when compared to the conventional chemical processes. Therefore, in the last years, the ultrasound has been extensively used in enzymatic processes, such as the production of esters with desirable characteristics for the pharmaceutical, cosmetics, and food industry, for the hydrolysis and glycerolysis of vegetable oils, production of biodiesel, etc. Several works found in the open literature suggest that the energy released by the ultrasound during the cavitation phenomena can be used to enhance mass transfer (substrate/enzyme), hence increasing the rate of products formation, and also contributing to enhance the enzyme catalytic activity. Furthermore, the ultrasound is considered a "green" technology due to its high efficiency, low instrumental requirement and significant reduction of the processing time in comparison to other techniques. The main goal of this review was to summarize studies available to date regarding the application of ultrasound in enzyme-catalyzed esterification, hydrolysis, glycerolysis and transesterification reactions.
authors.affiliation: Department of Chemical and Food Engineering, Federal University of Santa Catarina, UFSC, Campus Universitário, Bairro Trindade, Caixa Postal 476, Florianópolis, Santa Catarina, 88040-900, Brazil.
authors.forename: Lindomar A
authors.initials: LA
authors.lastname: Lerin
authors.forename: Raquel A
authors.initials: RA
authors.lastname: Loss
authors.forename: Daniela
authors.initials: D
authors.lastname: Remonatto
authors.forename: Mara Cristina
authors.initials: MC
authors.lastname: Zenevicz
authors.forename: Manuela
authors.initials: M
authors.lastname: Balen
authors.forename: Vendelino Oenning
authors.initials: VO
authors.lastname: Netto
authors.forename: Jorge L
authors.initials: JL
authors.lastname: Ninow
authors.forename: Cláudia M
authors.initials: CM
authors.lastname: Trentin
authors.forename: J Vladimir
authors.initials: JV
authors.lastname: Oliveira
authors.forename: Débora
authors.initials: D
authors.lastname: de Oliveira
mesh_terms: D000438:Alcohols; D056804:Biofuels; D016956:Burkholderia cepacia / Q000201:enzymology; D002384:Catalysis; D002861:Chromobacterium / Q000201:enzymology; D002942:Circular Dichroism; D004798:Enzymes / Q000737:chemistry*; D004800:Enzymes, Immobilized; D004952:Esters; D005230:Fatty Acids, Nonesterified / Q000737:chemistry; D005656:Fungal Proteins; D005990:Glycerol; D055772:Green Chemistry Technology; D006868:Hydrolysis; D008049:Lipase / Q000737:chemistry*; D008855:Microscopy, Electron, Scanning; D011108:Polymers / Q000737:chemistry; D012997:Solvents / Q000737:chemistry; D014465:Ultrasonics
chemical_list: D000438:Alcohols; D056804:Biofuels; D004798:Enzymes; D004800:Enzymes, Immobilized; D004952:Esters; D005230:Fatty Acids, Nonesterified; D005656:Fungal Proteins; D011108:Polymers; D012997:Solvents; C093667:Novozyme 435; D008049:Lipase; D005990:Glycerol