Industrial applications of fungal lipases: a review

Abstract

Fungal lipases (triacylglycerol acyl hydrolases EC 3.1.1.3) are significant industrial enzymes and have several applications in a number of industries and fields. Fungal lipases are found in several species of fungi and yeast. These enzymes are carboxylic acid esterases, categorized under the serine hydrolase family, and do not require any cofactor during the catalyzing of the reactions. It was also noticed that processes including the extraction and purification of lipases from fungi are comparatively easier and cheaper than other sources of lipases. In addition, fungal lipases have been classified into three chief classes, namely, GX, GGGX, and Y. Fungal lipases have applications not only in the hydrolysis of fats and oils (triglycerides) but are also involved in synthetic reactions such as esterification, acidolysis, alcoholysis, interesterification, and aminolysis. The production and activity of fungal lipases are highly affected by the carbon source, nitrogen source, temperature, pH, metal ions, surfactants, and moisture content. Therefore, fungal lipases have several industrial and biotechnological applications in many fields such as biodiesel production, ester synthesis, production of biodegradable biopolymers, formulations of cosmetics and personal care products, detergent manufacturing, degreasing of leather, pulp and paper production, textile industry, biosensor development, and drug formulations and as a diagnostic tool in the medical sector, biodegradation of esters, and bioremediation of wastewater. The immobilization of fungal lipases onto different carriers also helps in improving the catalytic activities and efficiencies of lipases by increasing thermal and ionic stability (in organic solvents, high pH, and temperature), being easy to recycle, and inducing the volume-specific loading of the enzyme onto the support, and thus, these features have proved to be appropriate for use as biocatalysts in different sectors.

UV Light Degradation of Polylactic Acid Kickstarts Enzymatic Hydrolysis

“…Our experimentation above used an ideal system for the biotic degradation of PLLA as proteinase K is the leading enzyme for the catalysis of PLLA enzymatic hydrolysis. , To determine if the trends demonstrated are more generalizable, the biodegradability experiments were repeated utilizing another esterase, triacylglycerol lipase. Lipases are present in a high majority of living organisms, with a large number of fungi also producing lipases . Tokiwa et al, demonstrated the ability of lipase to degrade synthetic polyesters, and Alejandra et al, confirmed lipase’s degradation capabilities in poly­(3-hydroxybutyrate- co -4-hydroxybutyrate). , Ultimately, lipase is a readily available enzyme and shown to degrade polyesters. , Figure shows that lipase induces a trend in enzymatic hydrolysis near identical to that of proteinase K. The presence of the identical catalytic triad in both lipase and proteinase K may be the cause for the similar response, with both proteinase K and lipase exhibit the ‘catalytic triad of aspartic acid (Asp), histidine (His), and serine (Ser) .…”

“…Lipases are present in a high majority of living organisms, with a large number of fungi also producing lipases. 34 Tokiwa et al, demonstrated the ability of lipase to degrade synthetic polyesters, and Alejandra et al, confirmed lipase's degradation capabilities in poly(3-hydroxybutyrate-co-4-hydroxybutyrate). 35,36 Ultimately, lipase is a readily available enzyme and shown to degrade polyesters.…”

A Review on Endophytic Fungi: A Natural Source of Industrial Enzymes

“…Lipases are considered a group of potential industrial enzymes that can catalyze the hydrolysis of triglycerides [soluble fats], liberating monoglycerides. Diglycerides, glycerol and free fatty acids across the oil-water interface [69]. Lipases are valuable enzymes as they accept a wide range of substrates, they are stable and active in organic solvents, and are available from several microbes.…”

Hydrophobic Clusters Regulate Surface Hydration Dynamics of Bacillus subtilis Lipase A

“…Lipases have several biotechnologically interesting characteristics. − The extracellular lipolytic activity of Bacillus subtilis was first observed in 1979 by Kennedy and Lennarz . However, intensive molecular research did not start over a decade later in 1992, with the cloning and sequencing of a lipase gene, lipA (lipaseA), followed by recombinant expression, purification, and functional and structural characterizations …”