## 1 Introduction  
The global flavors and fragrances market was $25.89 billion in 2021 and it is expected to reach $36.49 billion in 2029, with a projected annual growth rate of 4.7% during the forecast period [1]. The compounds used in this market can be obtained from natural sources such as animal and plant materials (herbs, honey, fruits, flowers, and spices) or via chemical synthesis. These compounds comprise lactones, carboxylic acids, alcohols, esters, ketones, aldehydes, and terpenes [1, 2]. Synthetic flavors and fragrances, such as a wide variety of esters, are currently used in several products, including food and beverages, pharmaceuticals, fine fragrances, cosmetics, personal care products, and home and floor care products [1; 2; 3]. They have been preferentially produced using a variety of homogeneous or heterogeneous chemical catalysts or biocatalysts. Among the latter, we can remark whole-cells from several microorganisms or isolated enzymes--lipases, cutinases, acyltransferases, lipoxygenases, hydroperoxide lyases, alcohol dehydrogenases or even multi-enzymatic systems [4]. Recently, increasing environmental and health awareness among the general public and in legislation have driven the need to seek eco-friendly and sustainable processes for producing valuable industrial esters, including flavors and fragrances. In this context, the use of environmentally friendly catalysts (biocatalysts) in industrial processes has been considered crucial to meet the requirements of some sectors, including food, cosmetics and personal care industries, that require high-quality products [3; 4]. Moreover, esters produced via biocatalytic routes can be labeled as green products, with the advantages that this has in their commercialization and possible price [2; 3; 5]. Lipases (triacylglycered acylhydrolases, EC 3.1.1.3) stand among the most important industrial enzymes. In nature, these enzymes catalyze the hydrolysis of triacylglycereds into diacylglycerols, monoacylglycerols, free fatty acids and glycerol at the water/oil interface [6; 7]. In vitro, they can be utilized for producing food-grade flavor and fragrance compounds, mainly via esterification reactions conducted in the presence or absence of organic solvents [3; 4; 6; 7; 8]. In general, the application of lipases in their free forms (soluble or powder crude extracts) in non-aqueous systems is not attractive, due to their difficult recovery from the reaction systems and their inactivation involving several phenomena such as possible distorting effects caused by the use of high temperature, organic solvents or by the effects of raw materials, such as short-chain carboxylic acids and alcohols commonly used for producing flavor and fragrance esters [9; 10; 11; 12]. Moreover, enzyme aggregation can also drastically reduce their catalytic performances due to the generation of substrate diffusional problems [3; 6; 7; 13]. To overcome such problems, immobilization of lipases has been an important tool in industrial processes for their application. Immobilization of lipases allows easy separation of the biocatalysts from the reaction mixtures at the end of the process, reuse for repeated reactions in batch or continuous modes (as long as the enzyme remains active). Moreover, it has been shown that immobilization may be a potent tool to improve many other enzyme features, such as stability (following different mechanisms) [10]. Immobilization can also improve enzyme selectivity, specificity or reduced inhibitions [14; 15; 16; 17], being coupled to enzyme purification [18]. However, only a properly designed and controlled immobilization protocol can really fully benefit from the potential of these techniques, as many points that influence the final effects on the enzyme features are still under investigation [12]. Physical adsorption of lipases on hydrophobic support surfaces allows their immobilization via the mechanism of interfacial activation, enabling the immobilization of the open form of the lipase.