Kinetics and mechanisms of reactions catalysed by immobilized lipases.

Production of exogenous lipases by bacteria, fungi, and actinomycetes

The lipases obtained from the genus Aspergillus present remarkable importance in biotechnological applications, and numerous studies have reported the importance of the fermentation parameters, such as nutrients, temperature and fermentation time. Moreover, many Aspergillus spp. lipases present several properties of immense industrial importance, such as their pH and temperature stability and excellent enantioselectivity. Different strategies have been used in order to immobilize crude or purified Aspergillus spp. lipases. Hence, Aspergillus spp. lipases have been studied for different industrial applications such as in the food and detergent industries, and also in the kinetic resolution of pharmaceuticals and chiral intermediates. This review highlights the production, purification, characterization, applications and immobilization of lipases from Aspergillus spp.

Aspergillus sp. lipase: Potential biocatalyst for industrial use

Applications of immobilized lipases to transesterification and esterification reactions in nonaqueous systems.

Lipases are water-soluble enzymes that act on insoluble substrates and catalyze the hydrolysis of long-chain triglycerides. Lipases play a vital role in the food, detergent, chemical, and pharmaceutical industries. In the past, fungal lipases gained significant attention in the industries due to their substrate specificity and stability under varied chemical and physical conditions. Fungal enzymes are extracellular in nature, and they can be extracted easily, which significantly reduces the cost and makes this source preferable over bacteria. Soil contaminated with spillage from the products of oil and dairy harbors fungal species, which have the potential to secrete lipases to degrade fats and oils. Herein, the strategies involved in the characterization of fungal lipases, capable of degrading fatty substances, are narrated with a focus on further applications.

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Strategies to Characterize Fungal Lipases for Applications in Medicine and Dairy Industry

A qualitative screening revealed the occurrence of lipase, esterase, protease, amylase, endo-1,4-β-D-glucanase, xylanase, pectinmethylesterase, polygalacturonase, catalase, β-D-glucosidase and β-D-galactosidase activities in the technical Aspergillus niger enzyme under study (Lipase 2212 D, Rohm). The isolation and purification of lipolytic activities were performed by combination of DEAE-Trisacryl M ion exchange chromatography, Sephadex G 50 gel filtration and hydrophobic chromatography using Phenylsepharose CL-4B. The individual purification steps were checked by specific enzyme visualization in ultrathin agar gels after ultrathin-layer isoelectric focusing (UIEF). Two UIEF homogeneous lipase isoenzymes (I and II) were isolated and characterized by the following parameters: isoelectric points (I: 4.0; II. 3.5); molecular weights (I: 31000 daltons; II: 19000 daltons); carbohydrate contents (I: 6%; II: 9%) and compositions; pH optima (I, II: 5-6); substrate specificities and various effectors.

A. Zink

Papers

Isolation, Purification, and Characterization of Lipase Isoenzymes from a Technical Aspergillus niger Enzyme