This review paper provides an overview regarding the main aspects of microbial lipases production. The most important microbial lipase-producing strains for submerged and solid-state fermentations are reviewed as well as the main substrates, including the use of agroindustrial residues. Current process techniques (batch, repeated-batch, fed-batch, and continuous mode) are discussed and the main bioreactors configurations are also presented. Furthermore, the present review paper shows a general overview about the development of mathematical models applied to lipase production. Finally, some future perspectives on lipase production are discussed with special emphasis on lipase engineering and the use of mathematical models as a useful tool for process improvement and control.

A Review on Microbial Lipases Production

Lipases and phospholipases are interfacial enzymes that hydrolyze hydrophobic ester linkages of triacylglycerols and phospholipids, respectively. In addition to their role as esterases, these enzymes catalyze a plethora of other reactions; indeed, lipases also catalyze esterification, transesterification and interesterification reactions, and phospholipases also show acyltransferase, transacylase and transphosphatidylation activities. Thus, lipases and phospholipases represent versatile biocatalysts that are widely used in various industrial applications, such as for biodiesels, food, nutraceuticals, oil degumming and detergents; minor applications also include bioremediation, agriculture, cosmetics, leather and paper industries. These enzymes are ubiquitous in most living organisms, across animals, plants, yeasts, fungi and bacteria. For their greater availability and their ease of production, microbial lipases and phospholipases are preferred to those derived from animals and plants. Nevertheless, traditional purification strategies from microbe cultures have a number of disadvantages, which include non-reproducibility and low yields. Moreover, native microbial enzymes are not always suitable for biocatalytic processes. The development of molecular techniques for the production of recombinant heterologous proteins in a host system has overcome these constraints, as this allows high-level protein expression and production of new redesigned enzymes with improved catalytic properties. These can meet the requirements of specific industrial process better than the native enzymes. The purpose of this review is to give an overview of the structural and functional features of lipases and phospholipases, to describe the recent advances in optimization of the production of recombinant lipases and phospholipases, and to summarize the information available relating to their major applications in industrial processes.

https://www.mdpi.com/1422-0067/16/9/20774/pdf

Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications

Organic solvent adaptation of Gram positive bacteria: applications and biotechnological potentials.

Thermostable bacterial lipases occupy a place of prominence among biocatalysts owing to their novel, multifold applications and resistance to high temperature and other operational conditions The capability of lipases to catalyze a variety of novel reactions in both aqueous and nonaqueous media presents a fascinating field for research, creating interest to isolate novel lipase producers and optimize lipase production The most important stages in a biological process are modeling and optimization to improve a system and increase the efficiency of the process without increasing the cost Different production media were tested for lipase production by a newly isolated thermophilic Geobacillus sp strain ARM (DSM 21496 = NCIMB 41583) The maximum production was obtained in the presence of peptone and yeast extract as organic nitrogen sources, olive oil as carbon source and lipase production inducer, sodium and calcium as metal ions, and gum arabic as emulsifier and lipase production inducer The best models for optimization of culture parameters were achieved by multilayer full feedforward incremental back propagation network and modified response surface model using backward elimination, where the optimum condition was: growth temperature (523°C), medium volume (50 ml), inoculum size (1%), agitation rate (static condition), incubation period (24 h) and initial pH (58) The experimental lipase activity was 047 Uml-1 at optimum condition (47-fold increase), which compared well to the maximum predicted values by ANN (047 Uml-1) and RSM (0476 Uml-1), whereas R2 and AAD were determined as 0989 and 0059% for ANN, and 095 and 0078% for RSM respectively Lipase production is the result of a synergistic combination of effective parameters interactions These parameters are in equilibrium and the change of one parameter can be compensated by changes of other parameters to give the same results Though both RSM and ANN models provided good quality predictions in this study, yet the ANN showed a clear superiority over RSM for both data fitting and estimation capabilities On the other hand, ANN has the disadvantage of requiring large amounts of training data in comparison with RSM This problem was solved by using statistical experimental design, to reduce the number of experiments

/pdf/a-modeling-study-by-response-surface-methodology-and-4ustgk6ion.pdf

A modeling study by response surface methodology and artificial neural network on culture parameters optimization for thermostable lipase production from a newly isolated thermophilic Geobacillus sp. strain ARM

Gupta Anshu

Papers

Lipase from solvent tolerant Pseudomonas aeruginosa strain: Production optimization by response surface methodology and application