## 1 Introduction  
Lipases have a myriad of industrial and biotechnological applications that rely on the variety of reactions that they catalyze. Based on hydrolytic reactions these biocatalysts can be applied: in the food industry for lipid modification through complete or partial triacylglycerol degradation, resulting in food with improved sensorial properties [1; 2]; as a digestive auxiliary [3]; being incorporated in detergents, facilitating the removal of fat stains from fabrics. Through synthetic reactions, lipases can be applied to biodiesel production since they catalyze the transesterification of vegetable oils and simple alcohols [4]. On the other hand, one of the most relevant lipase applications is in the pharmaceutical industry where, through hydrolytic or esterification reactions, lipases can discriminate enantiomers from racemic substrates and produce specific enantiopure drugs, as in the case of profens and atenol [5]. Additionally, in several of these applications, lipases can be immobilized in inert supports to improve their properties, including stability and selectivity, and enable reuse [6]. Lipases (EC 3.1.1.3, triacylglycerglycerol lipase) are triacylglycerol hydrolases produced by various organisms with the natural function of hydrolyzing fats and lipids [7]. Although they hydrolyze triacylglycerol molecules into mono- and diacylglycerols, fatty acids and glycerol in aqueous solutions [8], lipolytic enzymes are the most used hydrolases in organic chemistry due to their capacity for catalyzing synthetic reactions in micro-aqueous conditions [9]. Among the different reactions they catalyze are hydrolysis, esterification, interestricification, aminolysis, transesterification, acidolysis and alcoholysis [10]. Lipases are ubiquitous enzymes produced by animals [11], plants [12] and microorganisms [13; 14; 15], with microorganisms being the most representative source of commercial lipases. Each lipase producing species has its own set of lipases with different levels of activity, stability and substrate selectivity, fitting its physiological and metabolic requirements. The challenge is to identify variants within the almost endless pool of natural lipases, which has the best potential as a catalyst in a desirable reaction. Elaborate and effective screening programs dedicated to searching for new lipases are constantly ongoing using microorganisms that can be cultured in the laboratory [16] or metagenomics libraries as a starting point [17]. Since new hits may be found in microorganisms that do not perform well in a production setup or just via a DNA sequence, heterologous production is key to exploiting lipase diversity. The predominant hosts used for recombinant lipase production are _Escherichia coli_ and _Komagataella phaffi_ (previously known as _Pichia pastoris_) [18; 19; 20; 21], but other species with a more powerful secretory capacity are increasingly used. In this context, known potent natural secretory organisms, such as filamentous fungi, can serve as excellent high-yielding hosts for heterologous production [22]. For example, _Aspergillus_ spp. and _Trichoderma reseei_ are eukaryotic hosts that have highly efficient secretory pathways, achieving more than 30 g of protein per liter of media [23; 24; 25]. In addition, different _Bacillus_ species are great alternatives for the recombinant production of prokaryotic enzymes, achieving levels of 20 g of protein per liter of media [26]. However, although some studies on the homologous or heterologous overproduction of lipases have been reported by these industrial workhorses [27; 28; 29], their ability to produce recombinant lipases is still a field that needs to be further explored. Unlike esterases that preferentially hydrolyze \"simple\" esters and triglycerides composed by short chain fatty acids (shorter than C6), lipases are mostly active against water-insoluble substrates, such as triglycerides composed by long-chain fatty acids [30; 31].