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

Development of polyvinyl alcohol/β-cyclodextrin antimicrobial nanofibers for fresh mushroom packaging

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

Lipases (triacylglycerol acylhydrolases, (E.C. 3.1.1.3)) are a class of enzymes endowed with an ability to catalyze the hydrolysis of triglycerides to glycerol and free fatty acids. These are industrially significant, particularly microbial lipases. Among several diverse sources, lipases from fungal origin are much embraced owing to their high stability. These lipases are directly screened majorly by the plate assay technique involving various preferred and specific substrates and indirectly by appropriately growing the strains in liquid medium followed by analysing the activity of the filtrates. Production of fungal lipase is majorly by using solid state and submerged fermentation processes with considerable variation in their operational conditions, that are influenced by physico-chemical factors and which plays a major role in the optimum lipase production. Further, the immobilized fungal cells have also been employed for lipase production using various support materials. Keeping in view of all these aspects, this review focuses on the screening, production and utility of lipases obtained from prominent fungal organisms.

Screening and production of lipase from fungal organisms

Lipase immobilization on ceramic supports: An overview on techniques and materials.

Optimization of novel halophilic lipase production by Fusarium solani strain NFCCL 4084 using palm oil mill effluent.

Fungal lipases with an ability to catalyze both hydrolytic and synthetic activities are now becoming extremely useful for various industrial applications. However, identification and selection of fungus with this dual ability is challenging. In this direction, we attempted to screen and identify potential marine fungus to produce a novel extracellular lipase using multi-step screening approach. Initially, we qualitatively screened 10 strains isolated from sea water using tributyrin agar plate assay method and six potential producers (SW1 to SW6) were selected which showed halos greater than minimum threshold (3 mm). Further, we quantitatively screened for the hydrolytic activities of crude extracellular lipase and evaluated their synthetic activities (esterification and transesterification reactions) also. The result analysis showed that among the six potential strains, the extracellular lipase produced by SW4 strain exhibited the highest activity. Thus, the selected SW4 strain produced a novel extracellular lipase with a good correlation between hydrolytic and synthetic activities as compared to other strains. Further, the selected strain (SW4) was taxonomically identified as Fusarium solani and was deposited in NFCCI under accession No. 4048 and the nucleotide sequence was also deposited in GenBank under accession No. MF138865 .

Kiptoo Geoffry

Papers

Screening and production of lipase from fungal organisms

Optimization of novel halophilic lipase production by Fusarium solani strain NFCCL 4084 using palm oil mill effluent.

A novel halophilic extracellular lipase with both hydrolytic and synthetic activities