Microbial Lipases Research Articles

Comprehensive Insights into Microbial Lipases: Unveiling Structural Dynamics, Catalytic Mechanism, and Versatile Applications.

Microbial lipases (MLs) are pivotal biocatalysts in lipid biotechnology due to their diverse enzymatic properties and substrate specificity, garnering significant research attention. This comprehensive review explores the significance of MLs in biocatalysis, providing insights into their structure, catalytic domain, and oxyanion hole. The catalytic mechanism is elucidated, highlighting the molecular processes driving their efficiency. The review delves into ML sources, spanning fungi, yeasts, bacteria, and actinomycetes, followed by a discussion on classification and characterization. Emphasizing the scattered findings in the literature, the paper consolidates the latest information on ML applications across various industries, from food and pharmaceuticals to biofuel production and the paper and pulp industry. The review captures the dynamic landscape of ML research, emphasizing their structure-function relationships and practical implications across diverse sectors.

Microbial lipases: propitious biocatalysts for various biotechnological applications

The use of microbial lipases is very important because they have a broad spectrum of catalytic reactions. Lipases catalyze reactions in aqueous and non-aqueous media and have advantages when compared to chemical catalysts, due to their specificity, enantioselectivity and stability at pH and temperature. The interest in research for microbial lipases occurs because of their applicability in various sectors and industries, such as food and beverage production, cosmetics, pharmaceuticals, surfactants, dairy products, treatment of effluents containing oils and fats, biofuels, among others. Biocatalysts can be obtained by submerged fermentation (SF) or solid-state fermentation (SSF), which has advantages over SF, because it is possible to use agroindustrial waste as substrate or growth support for microorganisms, becoming an alternative to reduce production costs. SSF is a promising technology for enzyme production, because besides using low-cost substrates, the biocatalyst can be produced in a more concentrated form, facilitating its recovery from the culture medium when necessary. Thus, this paper intends to discuss and review studies on microbial lipases, with direct application of the fermented solid (SSF), focusing on the main microorganisms, substrates and supports used in SSF, applicability of lipases in several industrial sectors, besides presenting conversion results using different microorganisms or/and substrates.

Use of genomics & proteomics in studying lipase producing microorganisms & its application

In biotechnological applications, lipases are recognized as the most widely utilized and versatile enzymes, pivotal in biocatalytic processes, predominantly produced by various microbial species. Utilizing omics technology, natural sources can be meticulously screened to find microbial flora which are responsible for oil production. Lipases are versatile biocatalysts. They are used in a variety of bioconversion reactions and are receiving a lot of attention because of the quick development of enzyme technology and its usefulness in industrial operations. This article offers recent insights into microbial lipase sources, including fungi, bacteria, and yeast, alongside traditional and modern methods of purification such as precipitation, immunopurification and chromatographic separation. Additionally, it explores innovative methods like the reversed micellar system, aqueous two-phase system (ATPS), and aqueous two-phase flotation (ATPF). The article deals with the use of microbial lipases in a variety of sectors, including the food, textile, leather, cosmetics, paper, detergent, while also critically analyzing lipase-producing microbes. Moreover, it highlights the role of lipases in biosensors, biodiesel production, tea processing, bioremediation, and racemization. This review provides the concept of the use of omics technique in the mechanism of screening of microbial species those are capable of producing lipase and also find the potential applications.

Hydrophobic Residues Promote Interfacial Activation of Candida rugosa Lipase: A Study of Rotational Dynamics.

Microbial lipases constitute a class of biocatalysts with the ability to cleave ester linkages of long-chain triglycerides. This property makes them particularly attractive for industrial applications ranging from food processing to pharmaceutical preparation. Among such enzymes, Candida rugosa lipase (CRL) is one of the most frequently used in biotransformation. A notable feature of CRL, among many lipases, is its propensity for interfacial activation: these enzymes exhibit elevated catalytic rates when acting at the interface between aqueous and hydrophobic phases. Notably, this phenomenon can be attributed to the presence of a mobile lid domain, which in its closed state occludes the enzyme active site. To advance our understanding of interfacial activation, we explore the dynamics of CRL rotation at the octane-water interface in this work. To do so, we employ molecular dynamics and umbrella sampling to evaluate the free energy of rotation of the enzyme at the interface. We identify a global minimum in the rotational landscape that coincides with lid opening at the interface. Additionally, we investigate the role of surface residues outside the lid domain as they serve to instigate rotation of the lid toward the aqueous phase. In doing so, we identify a patch of leucine residues which when mutated to glycine impose a barrier to rotation that maintains the enzyme in the inactive (closed lid) state on the order of 1 μs. Importantly, this study presents a novel quantification of the rotational free energy corresponding to CRL lid opening at the octane-water interface. The accompanying mutagenesis study likewise clarifies the role of hydrophobic surface residues in the transition. As such, this work provides valuable insight into the phenomenon of interfacial activation that might open up new avenues for manipulating the microenvironment of industrially relevant lipases, affording enhanced control over the enzyme state.

Substrate specificity of commercial lipases activated by a hydration–aggregation pretreatment in anhydrous esterification reactions

Substrate specificity in non-aqueous esterification catalyzed by commercial lipases activated by hydration–aggregation pretreatment was investigated. Four microbial lipases from Rhizopus japonicus, Burkholderia cepacia, Rhizomucor miehei, and Candida antarctica (fraction B) were used to study the effect of the carbon chain length of saturated fatty acid substrates on the esterification activity with methanol in n-hexane. Hydration–aggregation pretreatment had an activation effect on all lipases used, and different chain length dependencies of esterification activity for lipases from different origins were demonstrated. The effects of various acidic substrates with different degrees of unsaturation, aromatic rings, and alcohol substrates with different carbon chain lengths on esterification activity were examined using R. japonicus lipase, which demonstrated the most remarkable activity enhancement after hydration–aggregation pretreatment. Furthermore, in the esterification of myristic acid with methanol catalyzed by the hydrated–aggregated R. japonicus lipase, maximum reaction rate (5.43 × 10−5 mmol/(mg-biocat min)) and Michaelis constants for each substrate (48.5 mM for myristic acid, 24.7 mM for methanol) were determined by kinetic analysis based on the two-substrate Michaelis-Menten model.

Statistical approach for newly isolated and identified microbial lipases production

Statistical approach for newly isolated and identified microbial lipases production

Exploring microbial lipases: Screening and identification for biocatalyst potential in bioethanol synthesis from glycerol-based biodiesel waste

Lipases are hydrolytic enzymes that break triglycerides into free fatty acids and glycerol. Typically, these enzymes are produced by microorganisms and used as industrial biocatalysts. Microorganisms isolated from oil-based environmental samples were screened for their lipase-producing ability, collecting twenty bacteria and eighteen fungal strains. Through selective media and morphological identification, various microorganisms were identified, including Pseudomonas sp. (12 strains), Escherichia coli (4 strains), Serratia (2 strains), carotenoid-producing bacteria (1 strain), an unknown isolate bacterium, Aspergillus sp. (6 strains), Aspergillus niger (1 strain), Aspergillus flavus (1 strain), Penicillium sp. (3 strains), Saccharomyces sp. (2 strains), Filamentous Black Fungus (2 strains), Omphalina sp. (1 strain), Rhizopus sp. (1 strain), and Trichoderma sp. (1 strain). Based on lipolytic index results, six bacteria exhibited high lipolytic indices, with Pseudomonas sp. having the highest index. After multi-screening, three lipolytic bacteria belonging to the genera Pseudomonas sp., Serratia sp., and Escherichia coli, as well as three lipolytic fungi belonging to the genera Saccharomyces sp., Trichoderma sp., and Aspergillus flavus, respectively, demonstrated the highest lipolytic activity when screened on a lipase assay, reaching 6.3 and 5.01 mU/g at 72 h of incubation. Consequently, these selected microorganisms were chosen for further study on bioethanol synthesis from glycerol. The study has revealed that the isolated bacteria and fungi strains have the potential to be efficient lipase producers.

A lipase from Lacticaseibacillus rhamnosus IDCC 3201 with thermostability and pH resistance for use as a detergent additive

Lipases are important biocatalysts and ubiquitous in plants, animals, and microorganisms. The high growth rates of microorganisms with low production costs have enabled the wide application of microbial lipases in detergent, food, and cosmetic industries. Herein, a novel lipase from Lacticaseibacillus rhamnosus IDCC 3201 (Lac-Rh) was isolated and its activity analyzed under a range of reaction conditions to evaluate its potential industrial application. The isolated Lac-Rh showed a molecular weight of 24 kDa and a maximum activity of 3438.5 ± 1.8 U/mg protein at 60 °C and pH 8. Additionally, Lac-Rh retained activity in alkaline conditions and in 10% v/v concentrations of organic solvents, including glycerol and acetone. Interestingly, after pre-incubation in the presence of multiple commercial detergents, Lac-Rh maintained over 80% of its activity and the stains from cotton were successfully removed under a simulated laundry setting. Overall, the purified lipase from L. rhamnosus IDCC 3201 has potential for use as a detergent in industrial applications.Key points• A novel lipase (Lac-Rh) was isolated from Lacticaseibacillus rhamnosus IDCC 3201• Purified Lac-Rh exhibited its highest activity at a temperature of 60 °C and a pH of 8, respectively• Lac-Rh remains stable in commercial laundry detergent and enhances washing performance

Expression of microbial lipase in filamentous fungus Aspergillus niger: a review.

Lipase has high economic importance and is widely used in biodiesel, food, detergents, cosmetics, and pharmaceutical industries. The rapid development of synthetic biology and system biology has not only paved the way for comprehensively understanding the efficient operation mechanism of Aspergillus niger cell factories but also introduced a new technological system for creating and optimizing high-efficiency A. niger cell factories. In this review, all relevant data on microbial lipase enzyme sources and general properties are gathered and updated. The relationship between A. niger strain morphology and protein production is discussed. The safety of A. niger strain is investigated to ensure product safety. The biotechnologies and factors influencing lipase expression in A. niger are summarized. This review focuses on various strategies to improve lipase expression in A. niger. The summary of these methods and the application of the gene editing technology CRISPR/Cas9 system can further improve the efficiency of constructing the engineered lipase-producing A. niger.

Obtaining a biodegradable biocatalyst – study on lipase immobilization on spent coffee grounds as potential carriers

Coffee waste can be reused as matrices for enzyme immobilization, as it contains various organic compounds able to adsorb catalytic proteins. In this study, spent coffee grounds were used as a support in the immobilization process in their native form and after being pretreated with hexane, ethanol, and sulphuric acid solution, respectively. Microbial lipases from Aspergillus oryzae, Thermomyces lanuginosus, and Rhizomucor miehei were adsorbed on the carrier, and as a reference, the abovementioned lipases were also immobilized on a synthetic matrix - Lewatit VP OC 1600. The research investigated the impact of the purification step on the immobilization process and the full characteristics of the obtained biocatalysts. The hydrolytic and synthetic activities of the immobilized enzyme preparations were tested, as well as substrate specificity, recovery, and temperature and pH activity profiles. SEM and FTIR analyses were also performed. The results showed that the chemical composition of coffee waste influenced the activity of the obtained biocatalysts, and the lack of hemicellulose caused a reduction in lipolytic activity. The study reveals that spent coffee grounds can be a potential support for enzyme immobilization, and lipases adsorbed on them have improved properties such as hydrolytic or synthetic activity, and stability in pH.

Phenotypic and genetic characterization of a lipolytic Ralstonia mannitolilytica isolate from petroleum-contaminated soil in Iraq.

Lipases play a crucial role in various industrial applications, and microbial lipases, particularly those from bacteria, possess significant properties. With increasing concerns about the environmental and health impacts of hydrocarbons from pipelines and refineries, there is a growing need to mitigate the risks associated with these compounds. In this study, 40 bacterial isolates were recovered from contaminated soil samples collected from multiple refineries across Iraq. Using the Vitek system, bacterial isolates were identified up to the species level, revealing that only 12 isolates exhibited lipase-producing capabilities. Among the lipase-producing isolates, Ralstonia mannitolilytica demonstrated the highest extracellular lipase activity, as determined by an olive oil plate assay supplemented with rhodamine B. Confirmation of the species identity was achieved through 16S rRNA gene sequencing, with the obtained sequence deposited under accession number LC772176.1. Further sequence analysis revealed single nucleotide polymorphisms (SNPs) in the genome of Ralstonia mannitolilytica strain H230303-10_N19_7x_R2 (CP011257.1, positions 1,311,102 and 1,311,457). Additionally, the presence of the lipase gene was confirmed through amplification and sequencing using a thermocycler PCR. Sequence analysis of the gene, aligned using Geneious Prime software, identified SNPs (CP010799, CP049132, AY364601, CP011257, and CP023537), and a phylogenetic tree was constructed based on genetic characterization. Our findings highlight the potential of Ralstonia mannitolilytica as a promising candidate for lipase production and contribute to our understanding of its genetic diversity and biotechnological applications in hydrocarbon degradation and industrial processes.

Study of Processing Conditions during Enzymatic Hydrolysis of Deer By-Product Tallow for Targeted Changes at the Molecular Level and Properties of Modified Fats.

In most cases, the unused by-products of venison, including deer tallow, are disposed of in rendering plants. Deer tallow contains essential fatty acids and can be used to prepare products for everyday food and advanced applications. This work aimed to process deer tallow into hydrolyzed products using microbial lipases. A Taguchi design with three process factors at three levels was used to optimize the processing: amount of water (8, 16, 24%), amount of enzyme (2, 4, 6%), and reaction time (2, 4, 6 h). The conversion of the tallow to hydrolyzed products was expressed by the degree of hydrolysis. The oxidative stability of the prepared products was determined by the peroxide value and the free fatty acids by the acid value; further, color change, textural properties (hardness, spreadability, stickiness, and adhesiveness), and changes at the molecular level were observed by Fourier transform infrared spectroscopy (FTIR). The degree of hydrolysis was 11.8-49.6%; the peroxide value ranged from 12.3 to 29.5 µval/g, and the color change of the samples expressed by the change in the total color difference (∆E*) was 1.9-13.5. The conditions of enzymatic hydrolysis strongly influenced the textural properties: hardness 25-50 N, spreadability 20-40 N/s, and stickiness < 0.06 N. FTIR showed that there are changes at the molecular level manifested by a decrease in ester bonds. Enzymatically hydrolyzed deer tallow is suitable for preparing cosmetics and pharmaceutical matrices.

Phylogenetic analyses reveal insights into interdomain horizontal gene transfer of microbial lipases

Microbial lipases play a pivotal role in a wide range of biotechnological processes and in the human skin microbiome. However, their evolution remains poorly understood. Accessing the evolutionary process of lipases could contribute to future applications in health and biotechnology. We investigated genetic events associated with the evolutionary trajectory of the microbial family LIP lipases. Using phylogenetic analysis, we identified two distinct horizontal gene transfer (HGT) events from Bacteria to Fungi. Further analysis of human cutaneous mycobiome members such as the lipophilic Malassezia yeasts and CUG-Ser-1 clade (including Candida sp. and other microorganisms associated with cutaneous mycobiota) revealed recent evolutionary processes, with multiple gene duplication events. The Lid region of fungal lipases, crucial for substrate interaction, exhibits varying degrees of conservation among different groups. Our findings suggest the adaptability of the fungal LIP family in various genetic and metabolic contexts and its potential role in niche exploration.

Effectiveness of &lt;i&gt;Pseudomonas Aeruginosa&lt;/i&gt; in Destruction of Harmful Lipids in Lipidemia Patients

Pseudomonas aeruginosa is a type of harmful microorganism that belongs to a large group of Gram-negative bacteria, these bacteria can secrete many extracellular enzymes such as microbial lipase and oxidase that act on certain lipids. This study aims to activate certain enzymes of P. aeruginosa like lipase and oxidase in order to decrease high plasma triglycerides and cholesterol in lipidemia patients. Serum can also be used due to the fact that lipids are found in both serum and plasma. Five ml. of blood were collected from 100 lipidemia patients at Baghdad Teaching Hospital laboratories in Medical city, P. aeruginosa was isolated from medical wastes; cultured on bacterial media, gram stained and biochemically tested in vitro. Methods depend on inoculation of bacterial broth containing colonies of P. aeruginosa adjusted to McFarland standard turbidity with 50% of blood plasma were added, then cultures were incubated at 37°C for 6 days, activation of bacterial lipase and oxidase were done during the incubation period by addition of certain activators to the broth like glycogen liquid. The results showed that 100% of patients had cholesterol &lt;200 mg/dl and 99% of patients had normal triglyceride level (&lt;200mg/dl) after bacterial inoculation and activation of microbial lipase and oxidase. As conclusion, the high plasma lipids level of patients was decreased four times by P. aeruginosa may be due to the activation of microbial lipase and oxidase which could needs to future research to extract them and used them as treatment for these cases.

Recent insight into the advances and prospects of microbial lipases and their potential applications in industry.

Enzymes play a crucial role in various industrial sectors. These biocatalysts not only ensure sustainability and safety but also enhance process efficiency through their unique specificity. Lipases possess versatility as biocatalysts and find utilization in diverse bioconversion reactions. Presently, microbial lipases are gaining significant focus owing to the rapid progress in enzyme technology and their widespread implementation in multiple industrial procedures. This updated review presents new knowledge about various origins of microbial lipases, such as fungi, bacteria, and yeast. It highlights both the traditional and modern purification methods, including precipitation and chromatographic separation, the immunopurification technique, the reversed micellar system, the aqueous two-phase system (ATPS), and aqueous two-phase flotation (ATPF), moreover, delves into the diverse applications of microbial lipases across several industries, such as food, vitamin esters, textile, detergent, biodiesel, and bioremediation. Furthermore, the present research unveils the obstacles encountered in employing lipase, the patterns observed in lipase engineering, and the application of CRISPR/Cas genome editing technology for altering the genes responsible for lipase production. Additionally, the immobilization of microorganisms' lipases onto various carriers also contributes to enhancing the effectiveness and efficiencies of lipases in terms of their catalytic activities. This is achieved by boosting their resilience to heat and ionic conditions (such as inorganic solvents, high-level pH, and temperature). The process also facilitates the ease of recycling them and enables a more concentrated deposition of the enzyme onto the supporting material. Consequently, these characteristics have demonstrated their suitability for application as biocatalysts in diverse industries.

Isolation of Lactiplantibacillus plantarum producing Extracellular Lipase from Dairy Products and Optimization of the Enzyme Production

Recently, microbial lipases isolated from probiotic bacteria have attracted the attention of many scientists because they have significantly beneficial properties for human health. As a highly nutritious substrate, dairy products possess great potential for probiotic bacteria isolation. The main purpose of this study was to isolate probiotic bacteria in order to search for lipase producing bacteria. The bacteria were isolated from dairy products and purified by repeated sub-culturing on MRS medium at 37°C. The isolates were subjected to primary and secondary screening via fluorometric and colorimetric methods respectively. The isolates showing orange fluorescence under UV light at 350 nm around their colonies were selected for the colorimetric method. In this method, lipase activity was investigated by p-nitrophenyl palmitate. Probiotic characterizations of lipase-producing isolates were performed by acid resistance test, cell surface hydrophobicity assay, auto-aggregation and co-aggregation. The optimization of lipase production was performed by Central Composite Design (CCD). In the present study, 92 isolates were recovered from 71 samples. The results showed that 41 isolates were positive for fluorometric assay. According to the amount of enzyme production, seven strains were selected for probiotic characterizations. Finally, a potential probiotic strain of genus Lactobacillus showed the highest enzyme activity with 3.4 U.ml-1 compared to other isolates. This strain showed 100% similarity to Lactiplantibacillus plantarum. This research indicated that the lipase of Lactiplantibacillus plantarum can be used as a promising enzyme in the food and medicine industries.

Cloning and characterization of an acidic lipase from a lipolytic bacterium in tempeh

BackgroundLipases have emerged as essential biocatalysts, having the ability to contribute to a wide range of industrial applications. Microbial lipases have garnered significant industrial attention due to their stability, selectivity, and broad substrate specificity. In the previous study, a unique lipolytic bacterium (Micrococcus luteus EMP48-D) was isolated from tempeh. It turns out the bacteria produce an acidic lipase, which is important in biodiesel production. Our main objectives were to clone the acidic lipase and investigate its potential in biodiesel production. ResultIn this study, the gene encoding a lipase from M. luteus EMP48-D was cloned and expressed heterologously in Escherichia coli. To our knowledge, this is the first attempt at the cloning and expression of the lipase gene from Micrococcus luteus. The amino acid sequence was deduced from the nucleotide sequence (1356 bp) corresponded to a protein of 451 amino acid residues with a molecular weight of about 40 kDa. The presence of a signal peptide suggested that the protein was extracellular. A sequence analysis revealed that the protein had a lipase-specific Gly-X-Ser-X-Gly motif. The enzyme was identified as an acidic lipase with a pH preference of 5.0. Fatty acid preferences for enzyme activities were C8 and C12 (p-nitrophenyl esters), with optimum temperatures at 30–40 °C and still remaining active at 80°C. The enzyme was also shown to convert up to 70% of the substrate into fatty acid methyl ester. ConclusionThe enzyme was a novel acidic lipase that demonstrated both hydrolytic and transesterification reactions. It appeared particularly promising for the synthesis of biodiesel as this enzyme’s catalytic reaction was optimum at low temperatures and was still active at high temperatures.

In-silico identification and characterization of lipase gene sequences present in hexaploid wheat

Lipases (EC number 3.1.1.3), capable of hydrolyzing triacylglycerols (TAGs) into glycerol and fatty acids, gained attention due to diverse biotechnological applications and are extensively used in industries like dairy, pharmaceutical, cosmetic, food etc. Industrial use of microbial lipases is very costly, so an alternative seed lipase is used due to its low cost, specificity and ease of purification. Lipolytic activities in wheat (genus Triticum) are shown by embryo and aleurone lipids. The present study was undertaken to characterize the identified wheat lipase sequences with the help of bioinformatics tools. 63 wheat lipase genes were identified of which two genes matched common clusters with known lipase sequences of Arabidopsis, Oryza, and Zea mays through phylogenetic tree analysis. From STRING database (v11.0) analysis only one gene (ID: 000056_1AL) showed perfect 1st interaction networking. It depicted 8 functionally transcript partners with 9 nodes and 17 edges of which only 6 nodes have shown 2nd interaction. On further analysis, sequence 000056_1AL showed optimum physico-chemical characters with catalytic activity in lipid metabolism and a better network with 8 functionally associated transcript proteins. Domains present in the sequence 000056_1AL are TAG lipase, lipase class - 3, and phospholipase A1, which show broad substrate specificity of the particular protein.

Bioconversion of Black Soldier Fly (BSF) from Organic Waste Composting into Biodiesel Assisted by Whole Cell Microbial Lipase Biocatalyst through Direct Transesterification Process

Black Soldier Fly or Hermetia Illucens (BSF) is known for its potential as a biological agent that helps in the process of natural conversion of organic waste. Resulting compost and a large number of BSF colonies, potentially to be use as a non-food raw material in bioenergy production. The Method is BSF conversion experiment by direct transesterification reaction using Lab-scale bioreactor in 100ml three bottle neck flasks, the solution mixture consists of BSF powder, immobilized whole cell biocatalyst, and solvent. The Result is although in appearance the structure of the test mixture solution did not show an oily character, but based on the viscosity and density test, the test solution had density value 0.81 g/cm3 and viscosity value 1,024 mm2 /s which are above the value of the viscosity and density of methanol but still below the value of the viscosity and density of both SNI and EN14214 biodiesel standard, this could be due to insufficient separation or reaction, imperfect condition, and impurities that are still present in biodiesel products. It can be concluded that a transesterification reaction has occurred in this trial, however further analysis and more experiments are required to definitely conclude the changes in biodiesel production.

Study of Hydrolytic Enzymes Activity and Stability of the Isolated Yeast Close to Zygoascus hellenicus

Background: Lipase is one of the most well-known and essential biocatalysts in the de-tergent, food, and pharmaceutical industries. Microbial lipase sources such as yeasts are applicable due to their stability in harsh conditions. Objective: In this study, the effect of temperature, initial pH, and incubation time were investigated to improve the extracellular lipase production by yeast, named Zygoascus hellenicus strain MZ_574439 T. Methods: Strain MZ_574439 T has already been isolated and registered from Iran. In the current project, strain MZ_574439 T with 99% similarity to Z. hellenicus was isolated from water samples. Results: Our findings showed that the isolated strain has a remarkable difference from its close phy-logenetic species in the production of lipase and can produce extracellular lipase up to 7.2 U/ml while the Z. hellenicus has no ability of lipase production. The isolated strain was not able to pro-duce other hydrolytic enzymes. The enzyme activity results showed that the best activity for the iso-lated lipase is pH= 7 and 37°C. The best stability condition for the enzyme occurs at 50°C and pH =7. Conclusion: From the current study, it can be concluded that Z. hellenicus produces lipase. The li-pase enzyme production was optimized with different physiological conditions. Yeast extract could be a better source for maximum lipase production.