Lipases are very versatile enzymes, and produced the attention of the several industrial processes. Lipase can be achieved from several sources, animal, vegetable, and microbiological. The uses of microbial lipase market is estimated to be USD 425.0 Million in 2018 and it is projected to reach USD 590.2 Million by 2023, growing at a CAGR of 6.8% from 2018. Microbial lipases (EC 3.1.1.3) catalyze the hydrolysis of long chain triglycerides. The microbial origins of lipase enzymes are logically dynamic and proficient also have an extensive range of industrial uses with the manufacturing of altered molecules. The unique lipase (triacylglycerol acyl hydrolase) enzymes catalyzed the hydrolysis, esterification and alcoholysis reactions. Immobilization has made the use of microbial lipases accomplish its best performance and hence suitable for several reactions and need to enhance aroma to the immobilization processes. Immobilized enzymes depend on the immobilization technique and the carrier type. The choice of the carrier concerns usually the biocompatibility, chemical and thermal stability, and insolubility under reaction conditions, capability of easy rejuvenation and reusability, as well as cost proficiency. Bacillus spp., Achromobacter spp., Alcaligenes spp., Arthrobacter spp., Pseudomonos spp., of bacteria and Penicillium spp., Fusarium spp., Aspergillus spp., of fungi are screened large scale for lipase production. Lipases as multipurpose biological catalyst has given a favorable vision in meeting the needs for several industries such as biodiesel, foods and drinks, leather, textile, detergents, pharmaceuticals and medicals. This review represents a discussion on microbial sources of lipases, immobilization methods increased productivity at market profitability and reduce logistical liability on the environment and user.

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Microbial lipases and their industrial applications: a comprehensive review

Thermophiles and the applications of their enzymes as new biocatalysts.

Biomass-based biorefineries: An important architype towards a circular economy

Enzymes are natural catalysts highly specific to the substrate type and operate under mild conditions of temperature, pressure, and pH with high conversion rates, which makes them more efficient than conventional chemical catalysts. The enzymes can be obtained from various sources, animal, vegetable, and microbiological. Lipases are very versatile enzymes, and this has aroused the interest of the industries. However, the great problem of the use of soluble lipases is the high cost of acquisition, low operational stability, and difficulties of recovery, and reuse. Enzymatic immobilization has been suggested as an alternative to reduce the limitations of soluble enzymes, increasing their stability and facilitating recovery, and reuse, significantly reducing the cost of processes involving the use of enzymes. This review presents a discussion on the different immobilization methods for lipase, as well as the challenges of use lipases immobilized on the industrial scale.

Lipases: sources, immobilization methods, and industrial applications.

Lipases are industrially important biocatalyst, particularly microbial lipases and therefore, screening, production and purification of lipase enzyme from microbial strains are continuously emerging to fulfil the needs of pharmaceutical and food industries. More recently, various cost effective and efficient approaches are being attempted to increase the production of lipases in microbial strains. In this junction, this article attempt to connect production of lipases using various microbial strains such as bacteria, fungi and yeast has been highlighted and discussed, in order to enable researchers to choose an appropriate strains for lipase production. Then, screening of lipase producer and production of lipases under different fermentation system was discussed. Later, impact of various factors such as carbon sources, nitrogen sources, pH and temperature has been assessed, and presented in the perspective of increasing its production from microbial strains. Finally, purification techniques for lipase enzymes was summarized and recent literature pertaining to lipase purification from microbial stains are reviewed, and summarized.

Microbial lipases: An overview of screening, production and purification

Lipase (E.C.3.1.1.3) belongs to the hydrolases and is also known as fat splitting, glycerol ester hydrolase or triacylglycerol acylhydrolase. Lipase catalyzes the hydrolysis of triglycerides converting them to glycerol and fatty acids in an oil-water interface. These are widely used in food, dairy, flavor, pharmaceuticals, biofuels, leather, cosmetics, detergent, and chemical industries. Lipases are of plant, animal, and microbial origin, but microbial lipases are produced at industrial level and represent the most widely used class of enzymes in biotechnological applications and organic chemistry. Phylogenetic analysis and comparison of residues around GxSxG motif provided an insight to the diversity among bacterial lipases. A variety of para-Nitrophenyl (p-NP) esters having C2 to C16 (p-NP acetate to p-NP palmitate) in their fatty acid side chain can be hydrolyzed by bacterial lipases. Large heterogeneity has been observed in molecular and catalytic characteristics of lipases including molecular mass; 19–96 kDa, Km; 0.0064–16.58 mM, Kcat; 0.1665–1.0 × 104 s−1 and Kcat/Km; 26.02–7377 s-1/mM. Optimal conditions of their working temperature and pH have been stated 15–70 °C and 5.0–10.8, respectively and are strongly associated with the type and growth conditions of bacteria. Surface hydrophobicity, enzyme activity, stability in organic solvents and at high temperature, proteolytic resistance and substrate tolerance are the properties of bacterial lipases that have been improved by engineering. Bacterial lipases have been extensively studied during last decade. However, their wider applications demand a detailed review on purification, catalytic characterization and applications of lipases.

Ambreen Kouser

Papers

Bacterial lipases: A review on purification and characterization.