Lipases (triacylglycerolacyl hydrolases, EC3.1.1.3) are class of enzymes which catalyze the hydrolysis of long-chain triglycerides. In this review paper, an overview regarding the fungal lipase production, purification, and application is discussed. The review describes various industrial applications of lipase in pulp and paper, food, detergent, and textile industries. Some important lipase-producing fungal genera include Aspergillus, Penicillium, Rhizopus, Candida, etc. Current fermentation process techniques such as batch, fed-batch, and continuous mode of lipase production in submerged and solid-state fermentations are discussed in details. The purification of lipase by hydrophobic interaction chromatography is also discussed. The development of mathematical models applied to lipase production is discussed with special emphasis on lipase engineering.

Overview of fungal lipase: a review.

The lipase from Rhizomucor miehei (RML), formerly Mucor miehei, is a commercially available enzyme in both soluble and immobilized forms with very high activity and good stability under diverse experimental conditions (anhydrous organic solvents, supercritical fluids, etc.). The uses of the enzyme were initially oriented towards food industry, that way the enzyme has found a broad application in this area. This review intends to show the enzyme features and some of the most relevant aspects of the use of this interesting enzyme in oils and fats modification. The enzyme has been the first lipase whose structure was reported and its interfacial activation is very well known, making this enzyme a good template for modeling studies. Finally, the main uses of the enzyme in fatty acids, oils and fats modification will be revised (hydrolysis of glycerides, transesterification, esterification, acidolysis and interesterification). This lipase seems to be advantageous when compared to other lipases mainly in esterificaton reactions in anhydrous media, while other lipases can be preferred in transesterification reactions.

Lipase from Rhizomucor miehei as a biocatalyst in fats and oils modification

Lipases are a broad family of enzymes that catalyze the hydrolysis of ester bonds in substrates such as triglycerides, phospholipids, cholesteryl esters, and vitamin esters. Lipases are receiving increasing interest due to their effects on the quality of food products (e.g., the quality of post-harvest seafoods), and their actual and potential applications in modified foods and industrial processes. Lipases that catalyze specific reactions and that are active at particular conditions of pH and temperature to suit the requirements of industrial processes are of particular interest. This review focuses on lipases that display predominantly triacylglycerol hydrolase activity. Section 1 presents an overview of lipases from terrestrial organisms and the lipase gene family members. Due to their unique physiology, diet, and habitat, fish lipases may demonstrate novel activities that have potential applications for bioindustrial catalysis. Section 2 discusses lipases from fish and compares them with lipases from ...

Lipases from Mammals and Fishes

Summary Screening of lipolytic strains using Rhodamine-B/olive oil plate technique allowed the selection of Aspergillus niger MYA 135. Lipase production in submerged culture containing 2 % olive oil was enhanced by more than 50 % compared to basal cultural conditions. Optimal catalytic conditions for olive oil-induced lipase were pH=6.5 and 30–35 °C. These values were shifted to the acid region (4.0–6.5) and 35–37 °C when lipase extract was produced under basal conditions. Slight changes of the residual lipase activity against the pH were found. However, preincubation at either 37 or 40 °C caused an increase in the olive oil-inducible lipolytic activity. On the contrary, lipase residual activity decreases in the 30–55 °C range when it was produced in basal medium. Lipolytic extracts were almost not deactivated in presence of 50 % water-miscible organic solvents. However, water-immiscible aliphatic solvents reduced the lipase activity between 20 and 80 %.

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Kataliticka svojstva ekstrakta lipaze iz plijesni Aspergillus niger

Thirty-eight filamentous fungi cultivated under solid state fermentation (SSF) conditions were screened for lipase activity and enantioselectivity in kinetic resolutions of racemic secondary alcohols ( rac - 1a – c ) by acetylation with vinyl acetate performed in organic solvents. Many of the target fungi have not been studied previously for lipase/esterase activity and enantioselectivity. Without special enzyme isolation processes, the room temperature (25 °C) dried SSF cultures as such were tested in the enantiomer selective biotransformations. The majority of these SSF preparations proved to be effective as enantiomer selective biocatalysts exhibiting high but usual enantioselectivities according to the Kazlauskas rule. However, the SSF preparation of Mucor hiemalis origin acted as a selective anti-Kazlauskas catalyst. The best SSF products were successfully applied in preparative scale resolutions.

Kinetic resolutions with novel, highly enantioselective fungal lipases produced by solid state fermentation

Lipases produced extracellularly by bacteria and fungi are being widely used in the food industry for flavour development. During tea processing, the possibility of enhancing the flavour of tea by the exogenous addition of lipase has not been reported. It was therefore considered worthwhile to amend tea leaves with microbial lipases and observe the changes in the flavour profile of the finished product. Among a few fungal lipases screened, the enzyme secreted by Rhizomucor miehei increased the formation of desired flavour compounds. Hence, studies were initiated to achieve enhanced production of this industrially useful enzyme. Under solid-state fermentation R.M. miehei produces an extracellular lipase in copious amounts on a simple solid substrate within 96 h, which is active at lower temperatures and at near-neutral pH. These attributes make this enzyme suitable for use during the manufacturing of tea, where reactions are carried out at temperatures of 15 to 20 ̊C and pH range of 5 to 7. In the present study, exogenous addition of lipase resulted in an increase in flavour volatiles, which contribute to the aroma of tea.

S. Ramarethinam

Papers

Use of a Fungal Lipase for Enhancement of Aroma in Black Tea