Application of Bacterial Thermostable Lipolytic Enzymes in the Modern Biotechnological Processes: A Review

Samoylova, Yu. V.; Sorokina, K. N.; Piligaev, A. V.; Parmon, Valentin N.

doi:10.1134/s2070050419020107

Cited by 12 publications

(8 citation statements)

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“…Compared to animal sources, including pancreatic lipases, and plant lipases, for instance from Carica papaya and seeds, microbial lipases have been more exploited due to the necessity of simple and inexpensive culture media, practical handling, possibility of scale-up cultivations, and availability of various tools for genetic and protein engineering. The existence of profound knowledge regarding their genetics and physiology (especially for model organisms such as E. coli, K. phaffii and Saccharomyces cerevisiae) makes them important candidates for lipase production [40,41].…”

Section: Microbial Sources Of Lipasesmentioning

confidence: 99%

“…Most lipases investigated are from bacterial sources, such as enzymes from the genera Bacillus, Geobacillus, Pseudomonas, Streptomyces, Burkholderia, Chromobacterium, Achromobacter, Arthobacter and Alcaligenes [41,42]. Among them, Bacillus lipases are the most explored enzymes, having stable activity at high temperatures in a broad range of pH conditions, besides their tolerance to organic solvents [41].…”

Section: Microbial Sources Of Lipasesmentioning

confidence: 99%

“…Technically heterologous expression systems comprise basically three steps: (i) cloning of the gene of interest in a vector having a selection marker, (ii) transformation of the host strain with the constructed plasmid, and (iii) expression of the gene of interest under the control of an inducible or constitutive promoter and a known terminator. The biological systems used for gene expression include prokaryotic and eukaryotic hosts, such as E. coli and K. phaffi, respectively [41,43,44]. Heterologous expression has also been the choice of many studies of recombinant lipases produced by uncultured microorganisms from extreme environmental conditions.…”

Section: Production Of Recombinant Lipasesmentioning

confidence: 99%

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Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry

et al. 2020

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Lipases are one of the most used enzymes in the pharmaceutical industry due to their efficiency in organic syntheses, mainly in the production of enantiopure drugs. From an industrial viewpoint, the selection of an efficient expression system and host for recombinant lipase production is highly important. The most used hosts are Escherichia coli and Komagataella phaffii (previously known as Pichia pastoris) and less often reported Bacillus and Aspergillus strains. The use of efficient expression systems to overproduce homologous or heterologous lipases often require the use of strong promoters and the co-expression of chaperones. Protein engineering techniques, including rational design and directed evolution, are the most reported strategies for improving lipase characteristics. Additionally, lipases can be immobilized in different supports that enable improved properties and enzyme reuse. Here, we review approaches for strain and protein engineering, immobilization and the application of lipases in the pharmaceutical industry.

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Section: Microbial Sources Of Lipasesmentioning

confidence: 99%

Section: Microbial Sources Of Lipasesmentioning

confidence: 99%

Section: Production Of Recombinant Lipasesmentioning

confidence: 99%

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Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry

et al. 2020

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“…In this context, lipolytic enzymes are highly useful in many industrially significant processes due to their stability in the presence of solvents; exquisite chemo-, regio-and enantioselectivities; activity over a broad range of substrates; and no need for cofactors [6][7][8][9][10]. Such characteristics allow lipolytic enzymes to be used in the production of pharmaceuticals; in the food industry (with the global enzyme market being dominated by these two fields [11]); in the leather and paper industries; as additives in detergents; in the synthesis and degradation of plastics and biopolymers; for the production of biodiesel; and in bioremediation processes [12][13][14][15][16]. Thus, they are promising and have high-growth potential in the valuable world industrial enzymes market; the global lipase market is expected to reach $590.5 million in 2020 [17,18].…”

Section: Introductionmentioning

confidence: 99%

Exploring Metagenomic Enzymes: A Novel Esterase Useful for Short-Chain Ester Synthesis

et al. 2020

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Enzyme-mediated esterification reactions can be a promising alternative to produce esters of commercial interest, replacing conventional chemical processes. The aim of this work was to verify the potential of an esterase for ester synthesis. For that, recombinant lipolytic enzyme EST5 was purified and presented higher activity at pH 7.5, 45 °C, with a Tm of 47 °C. Also, the enzyme remained at least 50% active at low temperatures and exhibited broad substrate specificity toward p-nitrophenol esters with highest activity for p-nitrophenyl valerate with a Kcat/Km of 1533 s−1 mM−1. This esterase exerted great properties that make it useful for industrial applications, since EST5 remained stable in the presence of up to 10% methanol and 20% dimethyl sulfoxide. Also, preliminary studies in esterification reactions for the synthesis of methyl butyrate led to a specific activity of 127.04 U·mg−1. The enzyme showed higher esterification activity compared to other literature results, including commercial enzymes such as LIP4 and CL of Candida rugosa assayed with butyric acid and propanol which showed esterification activity of 86.5 and 15.83 U·mg−1, respectively. In conclusion, EST5 has potential for synthesis of flavor esters, providing a concept for its application in biotechnological processes.

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“…Lipolytic enzymes (LEs) are a diverse group of water-soluble hydrolases that catalyze the cleavage and formation of ester and even non-ester bonds (Rao et al 2009b;Thakur 2012;Samoylova et al 2019). They have been studied for more than 150 years since Bernard (1856) first reported the degradation of fats by mammalian pancreatic fluids.…”

Section: General Properties and Biological Functionsmentioning

confidence: 99%

Metagenomic approaches to discover lipolytic enzymes

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Stable in a Microorganism Pseudomonas aeruginosa san-ai 30 °C, 48 h 25 % (v/v) chloroform and n-hexane Karadzic et al. 2006 Bacillus sphaericus 205y 37 °C, 30 min 25 % (v/v) n-hexane and p-xylene. Hun et al. 2003 Bacillus megaterium 29 °C, 1 h 25-80 % (v/v) ethanol and acetone 100 % (v/v) 2-propanol, 1-butanol, Tol, n-hexane and n-heptane Lima et al. 2004 Sulfolobus solfataricus P1 30 °C or 70 °C, 1 h 40 % (v/v) methanol, ethanol and 2propanol. Mandrich et al. 2005 Stenotrophomonas maltophilia CGMCC 4254 30 °C, 24 h 20 and 50 % (v/v) benzene, toluene, nhexane and n-heptane. Li et al. 2013 Pseudomonas aeruginosa MH38 25 °C, 1 h 30 and 50 % (v/v) benzene and hexane Jang et al. 2014 Monascus purpureus 40 °C, 24 h 20 % (v/v) methanol, ethanol, acetonitrile, glycerol, acetone, n-Hexane, toluene and chloroform Kang et al. 2017 Chromohalobacter sp. 35 °C, 30 min 20 and 50 % (v/v) benzene and hexane Ai et al. 2018 Psychrobacter sp. ZY124 37 °C, 5 h 10, 30 and 50 % (v/v) DMSO, methanol, ethanol, acetone, acetonitrile, toluene, pentane, hexane and octane Zhang et al. 2018b Metagenome Marine mud 30 °C, 12 h 20 % (v/v) ethanol, acetonitrile, DMF and cyclohexane Gao et al. 2016 Forest soil sample. 37 °C, 2 h 25 % (v/v) DMSO, Benzene and p-xylene Berlemont et al. 2013 Wastewater treatment plant of a meat packing and dairy industry 4 °C, 48 h 15 and 30 % (v/v) methanol, ethanol, 1propanol, 2-propanol, glycerol, THF, dioxane, DMSO Glogauer et al. 2011 Soil 30 °C, 2 h 15 and 30 % (v/v) DMSO, DMF, p-xylene, hexane, heptane, and octane Wang et al. 2013 Compost Room temp., 26 d 30 % (v/v) methanol, ethanol, isopropanol, DMSO, acetone Lu et al., 2019 Soil contaminated with petroleum hydrocarbons No data 30 % (v/v) DMF and DMSO Pereira et al. 2015 a Abbreviations for the organic solvents are: DMF, N,N-dimethylformamide; DMSO, dimethylsulfoxide; THF, tetrahydrofuran. Halotolerance Among extremophilic LEs, halophilic/halotolerant LEs are another major group of industrial relevant enzymes. In comparison to the non-halophilic/non-halotolerant Source of LEs Enzyme properties Reference Salt range Maximum activity (%) a Microorganism Pelagibacterium halotolerans 0-4 M ~ 160 % at 3 M Jiang et al. 2012 Alcanivorax borkumensis 0-3.5 M 100 % at 0 M Tchigvintsev et al. 2015 Serratia sp. 0-4 M 100 % at 0 M Jiang et al. 2016 Alkalibacterium sp. 0-4 M ~ 105 % at 2 M Wang et al. 2016 Psychrobacter pacificensis 0-5 M 143.2 % at 2 M Wu et al. 2013a Lactobacillus plantarum 0-25 % ~ 250 % at 1M Esteban-Torres et al. 2014 Zunongwangia profunda 0-4.5 M 100 % at 0 M Rahman et al. 2016 Haloarcula marismortui 0-5 M 800 mU at 3 M Rao et al. 2009 Thalassospira sp. 0-4 M 283 % at 3 M De Santi et al. 2016b Bacillus licheniformis 0-5 M 588 % at 3.5 M Zhang et al. 2018 Metagenome Deep sea sponge 0-24% 100 % at 0 M Borchert et al. 2017 Marine sponge 0-4 M 234 % at 5 M Selvin et al. 2012 Soil 0-5 M 155 % at 1 M Jayanath et al. 2018 Marine arctic sediment 0-4 M 675 % at 3 M De Santi et al. 2016a Deep-sea shrimp 0-4 M ~ 250 % at 3.2 M Alcaide et al. 2015b 0-4 M ~ 250 %...

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Application of Bacterial Thermostable Lipolytic Enzymes in the Modern Biotechnological Processes: A Review

Cited by 12 publications

References 98 publications

Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry

Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry

Exploring Metagenomic Enzymes: A Novel Esterase Useful for Short-Chain Ester Synthesis

Metagenomic approaches to discover lipolytic enzymes

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