Industrial applications of microbial lipases

https://www.massey.ac.nz/%7Eychisti/Lipases.pdf

Production, purification, characterization, and applications of lipases.

Knowledge of bacterial lipolytic enzymes is increasing at a rapid and exciting rate. To obtain an overview of this industrially very important class of enzymes and their characteristics, we have collected and classified the information available from protein and nucleotide databases. Here we propose an updated and extensive classification of bacterial esterases and lipases based mainly on a comparison of their amino acid sequences and some fundamental biological properties. These new insights result in the identification of eight different families with the largest being further divided into six subfamilies. Moreover, the classification enables us to predict (1) important structural features such as residues forming the catalytic site or the presence of disulphide bonds, (2) types of secretion mechanism and requirement for lipase-specific foldases, and (3) the potential relationship to other enzyme families. This work will therefore contribute to a faster identification and to an easier characterization of novel bacterial lipolytic enzymes.

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Bacterial lipolytic enzymes: classification and properties

Lipases, triacylglycerol hydrolases, are an important group of biotechnologically relevant enzymes and they find immense applications in food, dairy, detergent and pharmaceutical industries. Lipases are by and large produced from microbes and specifically bacterial lipases play a vital role in commercial ventures. Some important lipase-producing bacterial genera include Bacillus, Pseudomonas and Burkholderia. Lipases are generally produced on lipidic carbon, such as oils, fatty acids, glycerol or tweens in the presence of an organic nitrogen source. Bacterial lipases are mostly extracellular and are produced by submerged fermentation. The enzyme is most commonly purified by hydrophobic interaction chromatography, in addition to some modern approaches such as reverse micellar and aqueous two-phase systems. Most lipases can act in a wide range of pH and temperature, though alkaline bacterial lipases are more common. Lipases are serine hydrolases and have high stability in organic solvents. Besides these, some lipases exhibit chemo-, regio- and enantioselectivity. The latest trend in lipase research is the development of novel and improved lipases through molecular approaches such as directed evolution and exploring natural communities by the metagenomic approach.

Bacterial lipases: an overview of production, purification and biochemical properties.

Developments in industrially important thermostable enzymes: a review.

Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. Molecular cloning, nucleotide sequence, purification and some properties

Thermoalkalophilic lipase of Bacillus thermocatenulatus large-scale production, purification and properties: aggregation behaviour and its effect on activity.

Publisher Summary This chapter describes the screening process for a thermophilic microbial lipase producer and the purification and characterization of the lipase BTL-1. It deals with the cloning and overexpression of an additional lipase of Bacillus thermocatenulatus , BTL-2. The large-scale production, purification, and characterization of this recombinant lipase BTL-2 are also described. The chapter develops an efficient expression system and simple purification procedure that allows the production of the large amounts of pure enzyme needed for crystallization. Crystallization and X-ray diffraction analysis of the lipase BTL-2 are in progress. Lipase BTL-2 proved to be a stable enzyme, with optimal activity at elevated temperatures and at alkaline pH, which are promising properties for biotechnological applications. The discovery of two different lipases in B. thermocatenulatus prompted to ask why this strain needs two lipolytic enzymes, what their physiological function is, and why only BTL-1 was detected in the culture broth of B. thermocatenulatus on induction with olive oil.

M. Luisa Rúa

Papers

Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. Molecular cloning, nucleotide sequence, purification and some properties

Thermoalkalophilic lipase of Bacillus thermocatenulatus large-scale production, purification and properties: aggregation behaviour and its effect on activity.

Two novel lipases from thermophile Bacillus thermocatenulatus: screening, purification, cloning, overexpression, and properties.