Keywords
lipases
PCR
thiolases
Ulva lactuca
How to Cite
Abstract
Epiphytic bacteria from marine macroalgae synthesize enzymes of industrial and biotechnological interest. In this study, we obtained two DNA candidate fragments for lipid-degrading enzymes from the total DNA of Ulva lactuca-associated epiphytic bacteria. First, we evaluated a method for total bacterial DNA isolation from the surface of U. lactuca thalli. Then, we designed sets of primers and used them directly for PCR amplification. The resulting PCR products were sequence-analyzed and used for expression and functional evaluation with the Escherichia coli pBAD-TOPO system. We obtained high molecular weight and good quality total bacterial DNA that served as a template to identify a fragment corresponding to an Acetyl-CoA C-Acetyltransferase (or Thiolase), and a candidate fragment for a versatile “true” lipase. We expressed the possible “true” lipase gene fragment heterologously in Escherichia coli and obtained proof of hydrolytic activity on Tributyrin, Tween-20, and Olive-oil media. This study resulted in new knowledge on U. lactuca-associated epiphytic bacteria as possible brand-new sources of enzymes such as thiolases and “true” lipases. However, future studies are required to describe the characteristics and important applications of these candidate enzymes.
González NC, Hoyos ML, Kleine LL, Castaño DM. Production of enzymes and siderophores by epiphytic bacteria isolated from the marine macroalga Ulva lactuca, Aquatic Biology 27: 107-118, 2018.
doi: 10.3354/ab00700
Egan S, Harder T, Burke C, Steinberg P, Kjelleberg S, Thomas T. The seaweed holobiont: understanding seaweed-bacteria interactions. FEMS Microbiology Reviews, 37: 462-476, 2013.
doi: 10.1111/1574-6976.12011
Goecke F, Labes A, Wiese J, Imhoff JF. Chemical interactions between marine macroalgae and bacteria. Marine Ecology Progress Series, 409: 267-300, 2010.
doi: 10.3354/meps08607
Wahl M, Goecke F, Labes A, Dobretsov S, Weinberger F. The second skin: ecological role of epibiotic biofilms on marine organisms. Frontiers in microbiology, 3: 292, 2012.
doi: 10.3389/fmicb.2012.00292
Martin M, Portetelle D, Michel G, Vandenbol M. Microorganisms living on macroalgae: diversity, interactions, and biotechnological applications. Applied Microbiology and Biotechnology, 98: 2917-2935, 2014.
doi: 10.1007/s00253-014-5557-2
Singh RP, Reddy CRK. Seaweed–microbial interactions: key functions of seaweed-associated bacteria. FEMS Microbiology Ecology, 88: 213-230, 2014.
doi: 10.1111/1574-6941.12297
Martin M, Barbeyron T, Martin R, Portetelle D, Michel G, Vandenbol M. The Cultivable Surface Microbiota of the Brown Alga Ascophyllum nodosum is Enriched in MacroalgalPolysaccharide-Degrading Bacteria. Frontiers in microbiology, 6: 1487, 2015.
doi: 10.3389/fmicb.2015.01487
Kostetsky E, Chopenko N, Barkina M, Velansky P, Sanina N. Fatty Acid Composition and Thermotropic Behavior of Glycolipids and Other Membrane Lipids of Ulva lactuca (Chlorophyta) Inhabiting Different Climatic Zones. Marine drugs, 16 (23): 494, 2018.
doi: 10.3390/md16120494
Yaich H, Garna H, Besbes S, Paquot M, Blecker C, Attia H. Chemical composition and functional properties of Ulva lactuca seaweed collected in Tunisia. Food chemistry, 128 (4): 895-901, 2011.
doi: 10.1016/j.foodchem.2011.03.114
Krohn-Molt I, Wemheuer B, Alawi M, Poehlein A, Güllert S, Schmeisser C, Streit WR. Metagenome survey of a multispecies and algae-associated biofilm reveals key elements of bacterialalgae interactions in photobioreactors. Applied and environmental microbiology, 79 (20): 6196-6206, 2013.
doi: 10.1128/AEM.01641-13
Naik MM, Naik D, Charya L, Mujawar SY, Vaingankar DC. Application of Marine Bacteria Associated with Seaweed, Ulva lactuca, for Degradation of Algal Waste, Proceedings of the National Academy of Sciences. India Section B: Biological Sciences, 89 (4): 1153-1160, 2018.
doi: 10.1007/s40011-018-1034-5
Jaeger KE, Kovacic F. Determination of lipolytic enzyme activities. Pseudomonas Methods and Protocols, 111-134, 2014.
doi: 10.1007/978-1-4939-0473-0_12
Hasan F, Shah AA, Hameed A. Industrial applications of microbial lipases. Enzyme and Microbial Technology, 39 (2): 235- 251, 2006.
doi: 10.1016/j.enzmictec.2005.10.016
Khan FI, Lan D, Durrani R, Huan W, Zhao Z, Wang Y. The lid domain in lipases: Structural and functional determinant of enzymatic properties. Frontiers in bioengineering and biotechnology, 5: 16, 2017.
doi: 10.3389/fbioe.2017.00016
Jaeger KE, Eggert T. Lipases for biotechnology. Current opinion in Biotechnology, 13 (4): 390-397, 2002.
doi: 10.1016/s0958-1669(02)00341-5
Javed S, Azeem F, Hussain S, Rasul I, Siddique MH, Riaz M, Nadeem H. Bacterial lipases: a review on purification and characterization. Progress in biophysics and molecular biology, 132: 23-34, 2018.
doi: 10.1016/j.pbiomolbio.2017.07.014
Kovacic F, Babic N, Krauss U, Jaeger K. Classification of Lipolytic Enzymes from Bacteria. Aerobic Utilization of Hydrocarbons, Oils, and Lipids, 24: 255-289, 2019.
doi: 10.1007/978-3-319-50418-6_39
Messaoudi A, Belguith H, Gram I, Hamida JB. Classification of EC 3.1. 1.3 bacterial true lipases using phylogenetic analysis. African journal of biotechnology, 9 (48): 8243-8247, 2010.
doi: 10.5897/AJB10.721
Arpigny JL, Jaeger KE. Bacterial lipolytic enzymes: classification and properties. Biochemical Journal, 343 (1): 177-183, 1999.
doi: 10.1042/bj3430177
Schaefer CM, Lu R, Nesbitt NM, Schiebel J, Sampson NS, Kisker C. FadA5 a thiolase from Mycobacterium tuberculosis: a steroid-binding pocket reveals the potential for drug development against tuberculosis. Structure, 23 (1): 21-33, 2015.
doi: 10.1016/j.str.2014.10.010
Tao T, Liu X, Chang J, Xu F, Yin Y. Cloning and characterisation of the gene encoding acetyl-coa c-acetyltransferase in Matricaria chamomilla. Journal of Pharmaceutical, Chemical and Biological, 4 (3): 386-393, 2016.
https://www.jpcbs.info/2016_4_3_08_Tingting.pdf
Fujita Y, Matsuoka H, Hirooka K. Regulation of fatty acid metabolism in bacteria. Molecular microbiology, 66 (4): 829-839, 2007.
doi: 10.1111 / j.1365-2958.2007.05947.x
Suo Y, Ren M, Yang X, Liao Z, Fu H, Wang J. Metabolic engineering of Clostridium tyrobutyricum for enhanced butyric acid production with high butyrate/acetate ratio. Applied microbiology and biotechnology, 102 (10): 4511-4522, 2018.
doi: 10.1007/s00253-018-8954-0
Lütke-Eversloh T. Application of new metabolic engineering tools for Clostridium acetobutylicum. Applied microbiology and biotechnology, 98 (13): 5823-5837, 2014.
doi: 10.1007/s00253-014-5785-5
Haapalainen AM, Meriläinen G, Wierenga RK. The thiolase superfamily: condensing enzymes with diverse reaction specificities. Trends in biochemical sciences, 31 (1): 64-71, 2006.
doi: 10.1016/j.tibs.2005.11.011
Madhavan A, Sindhu R, Parameswaran B, Sukumaran RK, Pandey A. Metagenome analysis: a powerful tool for enzyme bioprospecting. Applied biochemistry and biotechnology, 183 (2): 636- 651, 2017.
doi: 10.1007/s12010-017-2568-3
Wilson MC, Piel J. Metagenomic approaches for exploiting uncultivated bacteria as a resource for novel biosynthetic enzymology. Chemistry & biology. 20 (5): 636-647, 2013.
doi: 10.1016/j.chembiol.2013.04.011
Solomon S, Kachiprath B, Jayanath G, Sajeevan TP, Singh I.B., Philip R. High-quality metagenomic DNA from marine sediment samples for genomic studies through a preprocessing approach. 3 Biotech, 6 (2): 160, 2016.
doi: 10.1007/s13205-016-0482-y
Alma’abadi AD, Gojobori T, Mineta K. Marine metagenome as a resource for novel enzymes. Genomics, proteomics & bioinformatics, 13 (5): 290-295, 2015.
doi: 10.1016/j.gpb.2015.10.001
Kodzius R, Gojobori T. Marine metagenomics as a source for bioprospecting. Marine genomics, 24: 21-30, 2015.
doi: 10.1016/j.margen.2015.07.001
Lee MH, Lee CH, Oh TK, Song JK, Yoon JH. Isolation and characterization of a novel lipase from a metagenomic library of tidal flat sediments: evidence for a new family of bacterial lipases. Applied and environmental microbiology, 72 (11): 7406-7409, 2006.
doi: 10.1128/AEM.01157-06
Chu X, He H, Guo C, Sun B. Identification of two novel esterases from a marine metagenomic library derived from South China Sea. Applied microbiology and biotechnology, 80 (4): 615-625, 2008.
doi: 10.1007/s00253-008-1566-3
Jeon JH, Kim JT, Lee HS, Kim SJ, Kang SG, Choi SH, Lee JH. Novel lipolytic enzymes identified from metagenomic library of deep-sea sediment. Evidence-Based Complementary and Alternative Medicine, 2011: 2011.
doi: 10.1155/2011/271419
Okamura Y, Kimura T, Yokouchi H, Meneses-Osorio M, Katoh M, Matsunaga T, Takeyama H. Isolation and characterization of a GDSL esterase from the metagenome of a marine spongeassociated bacteria. Marine biotechnology, 12 (4): 395-402, 2010.
doi: 10.1007/s10126-009-9226-x
Su J, Zhang F, Sun W, Karuppiah V, Zhang G, Li Z, Jiang Q. A new alkaline lipase obtained from the metagenome of marine sponge Ircinia sp. World Journal of Microbiology and Biotechnology, 31 (7): 1093-1102, 2015.
doi: 10.1007/s11274-015-1859-5
Martin M. Function-based Analyses of Bacterial Symbionts Associated with the Brown Alga Ascophyllum nodosum and Identification of Novel Bacterial Hydrolytic Enzyme Genes, Doctoral dissertation, Université de Liège, Liège, Belgique. 2016.
https://orbi.uliege.be/bitstream/2268/196617/1/Th%C3%A8se%20Marjolaine%20Martin.pdf
Martin M, Vandermies M, Joyeux C, Martin R, Barbeyron T, Michel G, Vandenbol M. Discovering novel enzymes by functional screening of plurigenomic libraries from alga-associated Flavobacteriia and Gammaproteobacteria. Microbiological Research, 186: 52-61, 2016.
doi: 10.1016/j.micres.2016.03.005
Yung PY, Burke C, Lewis M, Kjelleberg S, Thomas T. Novel antibacterial proteins from the microbial communities associated with the sponge Cymbastela concentrica and the green alga Ulva australis. Applied and environmental microbiology, 77 (4): 1512-1515, 2011.
doi: 10.1128/AEM.02038-10
Burke C, Kjelleberg S, Thomas T. Selective extraction of bacterial DNA from the surfaces of macroalgae. Applied and environmental microbiology, 75 (1): 252-256, 2009.
doi: 10.1128/AEM.01630-08
Fujimoto S, Nakagami Y, Kojima F. Optimal bacterial DNA isolation method using bead-beating technique. Memoirs Kyushu Univ Dep Of Health Scis Of Medical Sch, 3: 33-38, 2004.
https://www.digital-biology.co.jp/manufactured/products/ms-100/pdf/report_ms-100_07.pdf
Vandeventer PE, Weigel KM, Salazar J, Erwin B, Irvine B, Doebler R, Niemz A. Mechanical Disruption of Lysis Resistant Bacterial Cells by Use of a Miniature, Low-Power, Disposable Device. Journal of Clinical Microbiology, 49 (7): 2533-2539, 2011.
doi: 10.1128/JCM.02171-10
Burke C. A metagenomic analysis of the epiphytic bacterial community from the green macroalga Ulva australis. Doctoral dissertation, University of New South Wales, Australia. 2010.
http://citeseerx.ist.psu.edu/viewdoc/download?doi=10.1.1.476.3020&rep=rep1&type=pdf
Messaoudi A, Belguith H, Ghram I, Ben Hamida J. LIPABASE: a database for ‘true’ lipase family enzymes. International journal of bioinformatics research and applications, 7 (4): 390-401, 2011.
doi: 10.1504/IJBRA.2011.043770
Rose TM, Schultz ER, Henikoff JG, Pietrokovski S, McCallum CM, Henikoff S. Consensus-degenerate hybrid oligonucleotide primers for amplification of distantly related sequences. Nucleic acids research, 26 (7): 1628-1635, 1998.
doi: 10.1093/nar/26.7.1628
Rose TM, Henikoff JG, Henikoff S. CODEHOP (COnsensusDEgenerate hybrid oligonucleotide primer) PCR primer design. Nucleic acids research, 31 (13): 3763-3766, 2003.
doi: 10.1093/nar/gkg524
Jaric M, Segal J, Silva-Herzog E, Schneper L, Mathee K, Narasimhan G. Better primer design for metagenomics applications by increasing taxonomic distinguishability. BMC proceedings, 7 (1): 1, 2013.
doi: 10.1186/1753-6561-7-S7-S4
Dieffenbach CW, Lowe TM, Dveksler GS. General concepts for PCR primer design. PCR Methods Appl, 3 (3): S30-S37, 1993.
doi: 10.1093/nar/gkn290
Buck GA, Fox JW, Gunthorpe M, Hager KM, Naeve CW, Pon RT, Rush J. Design strategies and performance of custom DNA sequencing primers. BioTechniques, 27 (3): 528-537, 2018.
doi: 10.2144/99273rr01
Kouker G, Jaeger KE. Specific and sensitive plate assay for bacterial lipases. Applied and environmental microbiology, 53 (1): 211-213, 1987.
doi: 0099-2240/87/010211-03
Samad MYA, Razak CNA, Salleh AB, Yunus WZW, Ampon K, Basri M. A plate assay for primary screening of lipase activity, Journal of microbiological methods, 9 (1): 51-56, 1989.
doi: 10.1016/0167-7012(89)90030-4
Lanka S, Latha JNL. A Short Review on Various Screening Methods to Isolate Potential Lipase Producers: Lipases-the Present and Future Enzymes of Biotech Industry. International Journal of Biological Chemistry, 9 (5): 207-219, 2015.
doi: 10.3923/ijbc.2015.207.219
Kumar D, Kumar L, Nagar S, Raina C, Parshad R, Gupta VK. Screening, isolation and production of lipase/esterase producing Bacillus sp. strain DVL2 and its potential evaluation in esterification and resolution reactions. Archives of Applied Science Research, 4 (4): 1763-1770, 2012.
https://www.scholarsresearchlibrary.com/
Tigerstrom RGV, Stelmaschuk S. The use of Tween 20 in a sensitive turbidimetric assay of lipolytic enzymes. Canadian journal of microbiology, 35 (4): 511-514, 1989.
doi: 10.1139 / m89-079
Plou FJ, Ferrer M, Nuero OM, Calvo MV, Alcalde M, Reyes F, Ballesteros A. Analysis of Tween 80 as an esterase/lipase substrate for lipolytic activity assay. Biotechnology techniques, 12 (3): 183-186, 1998.
doi: 10.1023/A:1008809105270
Corbellini VA, Scroferneker ML, Carissimi M, Stopiglia CDO, Souza TFD. Comparison of lipolytic activity of Sporothrix schenckii strains utilizing olive oil-rhodamine B and tween 80. Tecno-Lógica, 11 (2): 33-36, 2007.
http://hdl.handle.net/10183/187479
Dittami SM, Duboscq-Bidot L, Perennou M, Gobet A, Corre E, Boyen C, Tonon T. Host-microbe interactions as a driver of acclimation to salinity gradients in brown algal cultures. The ISME journal, 10 (1): 51-63, 2016.
doi: 10.1038/ismej.2015.104
Comba-González NB, Ruiz-Toquica JS, Lopez-Kleine L, Montoya-Castano D. Epiphytic Bacteria of Macroalgae of the Genus Ulva and their Potential in Producing Enzymes Having Biotechnological Interest. Journal of Marine Biology & Oceanography,5 (2): 2-9, 2016.
doi: 10.4172/2324-8661.1000153
Devi SG, Fathima AA, Radha S, Arunraj R, Curtis WR, Ramya M. A rapid and economical method for efficient DNA extraction from diverse soils suitable for metagenomic applications. PLoS One, 10 (7): e0132441, 2015.
doi: 10.1371/journal.pone.0132441
Tujula NA, Crocetti GR, Burke C, Thomas T, Holmström C, Kjelleberg S. Variability and abundance of the epiphytic bacterial community associated with a green marine Ulvacean alga. The ISME journal, 4 (2): 301-311, 2009.
doi: 10.1038/ismej.2009.107
Longford SR, Tujula NA, Crocetti GR, Holmes AJ, Holmström C, Kjelleberg S, Taylor MW. Comparisons of diversity of bacterial communities associated with three sessile marine eukaryotes. Aquatic microbial ecology, 48 (3): 217-229, 2007.
doi: 10.3354/ame048217
Bag S, Saha B, Mehta O, Anbumani D, Kumar N, Dayal M, Hansen T. An Improved Method for High Quality Metagenomics DNA Extraction from Human and Environmental Samples. Scientific Reports, 6: 26775, 2016.
doi: 10.1038/srep26775
Ismail A, Ktari L, Ahmed M, Bolhuis H, Bouhaouala-Zahar B, Stal LJ, El Bour M. Heterotrophic bacteria associated with the green alga Ulva rigida: identification and antimicrobial potential. Journal of Applied Phycology, 30 (5): 2883-2899, 2018.
doi: 10.1007/s10811-018-1454-x
Burke C, Thomas T, Lewis M, Steinberg P, Kjelleberg S. Composition, uniqueness and variability of the epiphytic bacterial community of the green alga Ulva australis. ISME Journal: Multidisciplinary Journal of Microbial Ecology, 5 (4): 590- 600, 2011.
doi: 10.1038/ismej.2010.164
Dineen SM, Aranda IVR, Anders DL, Robertson JM. An evaluation of commercial DNA extraction kits for the isolation of bacterial spore DNA from soil. Journal of applied microbiology, 109 (6): 1886-1896, 2010.
doi: 10.1111/j.1365-2672.2010.04816.x
Shepherd ML, Swecker JrWS, Ponder MA. Effect of Two Different Commercial DNA Extraction Kits on the Bacterial 16S Ribosomal RNA Gene Denaturing Gradient Gel Electrophoresis Profile of Arabian Gelding Feces. Journal of Equine Veterinary Science, 35 (2): 165-169, 2015.
doi: 10.1016/j.jevs.2014.12.006
Yeates C, Gillings MR, Davison AD, Altavilla N, Veal DA. Methods for microbial DNA extraction from soil for PCR amplification. Biological procedures online, 1 (1): 40-47, 1998.
doi: 10.1251/bpo6
Jensen MA, Fukushima M, Davis RW. DMSO and betaine greatly improve amplification of GC-rich constructs in de novo synthesis. PLoS One, 5 (6): e11024, 2010.
doi: 10.1371/journal.pone.0011024
Farell EM, Alexandre G. Bovine serum albumin further enhances the effects of organic solvents on increased yield of polymerase chain reaction of GC-rich templates. BMC Research Notes, 5 (1): 257-257, 2012.
doi: 10.1186/1756-0500-5-257
Hardjasa A, Ling M, Ma K, Yu H. Investigating the effects of DMSO on PCR fidelity using a restriction digest based method. Journal of Experimental Microbiology and Immunology (JEMI), 14: 161-164, 2010.
https://www.microbiology.ubc.ca/sites/default/files/roles/drupal_ungrad/JEMI/14/JEMI14_161-164.pdf
Bonk BM, Tarasova Y, Hicks MA, Tidor B, Prather KL. Rational design of thiolase substrate specificity for metabolic engineering applications. Biotechnology and bioengineering, 115 (9): 2167-2182, 2018.
doi: 10.1002/bit.26737
Ratledge C. Biochemistry of microbial degradation. Springer Science and Business Media, 2012.
doi: 10.1007/978-94-011-1687-9
Jimenez-Diaz L, Caballero A, Segura A. Pathways for the degradation of fatty acids in bacteria, Aerobic Utilization of Hydrocarbons, Oils and Lipids, Springer, 1-23, 2017.
doi: 10.1007/978-3-319-39782-5_42-1
Fox AR, Soto G, Mozzicafreddo M, Garcia AN, Cuccioloni M, Angeletti M, Ayub ND. Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches. Gene, 533 (1): 5-10, 2014.
doi: 10.1016/j.gene.2013.09.096
Harijan RK. Coenzyme-A dependent catalysis: An overview of thiolase superfamily enzymes and drug discovery. Research on Chronic Diseases, 1 (2): 017-019, 2017.
https://www.openaccessjournals.com/articles
Soto G, Stritzler M, Lisi C, Alleva K, Pagano ME, Ardila F, Ayub ND. Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation. Journal of experimental botany, 62 (15): 5699-5711, 2011.
doi: 10.1093/jxb/err287
Nesbitt M, Yang X, Fontán P, Kolesnikova I, Smith I, Sampson S, Dubnau E. A thiolase of Mycobacterium tuberculosis is required for virulence and production of androstenedione and androstadienedione from cholesterol. Infection and immunity, 78 (1): 275-282, 2010.
doi: 10.1128/IAI.00893-09
Martines ACM, Van Eunen K, Reijngoud DJ, Bakker BM. The promiscuous enzyme medium-chain 3-keto-acyl CoA thiolase triggers a vicious cycle in fatty-acid beta-oxidation. PLoS computational biology, 13 (4): e1005461, 2017.
doi: 10.1371/journal.pcbi.1005461
Wiesenborn DP, Rudolph FB, Papoutsakis ET. Thiolase from Clostridium acetobutylicum ATCC 824 and its role in the synthesis of acids and solvents. Applied and environmental microbiology, 54 (11): 2717-2722, 1988.
https://aem.asm.org/content/54/11/2717
Mann MS, Lütke-Eversloh T. Thiolase engineering for enhanced butanol production in Clostridium acetobutylicum. Biotechnology and bioengineering, 110 (3): 887-897, 2013.
doi: 10.1002/bit.24758
Chung A, Liu Q, Ouyang SP, Wu Q, Chen GQ. Microbial production of 3-hydroxydodecanoic acid by pha operon and fadBA knockout mutant of Pseudomonas putida KT2442 harboring tesB gene. Applied microbiology and biotechnology, 83 (3): 513-519, 2009.
doi: 10.1007/s00253-009-1919-6
Kim EJ, Son HF, Kim S, Ahn JW, Kim KJ. Crystal structure and biochemical characterization of beta-keto thiolase B from polyhydroxyalkanoate-producing bacterium Ralstonia eutropha H16. Biochemical and biophysical research communications, 444 (3): 365-369, 2014.
doi: 10.1016/j.bbrc.2014.01.055
Gao J, Vo MT, Ramsay JA, Ramsay BA. Overproduction of MCL-PHA with high 3-hydroxydecanoate Content. Biotechnology and bioengineering, 115 (2): 390-400, 2018.
doi: 10.1002/bit.26474
Inui H, Ishikawa T, Tamoi M. Wax ester fermentation and its application for biofuel production, Euglena: Biochemistry, Cell and Molecular Biology, Springer, 269-283, 2017.
doi: 10.1007/978-3-319-54910-1_13
Nandavaram A, Sagar AL, Madikonda AK, Siddavattam D. Proteomics of Sphingobium indicum B90A for a deeper understanding of hexachlorocyclohexane (HCH) bioremediation, Reviews on environmental health, 31 (1): 57-61, 2016.
doi: 10.1515/reveh-2015-0042
Bazinet AL, Cummings MP. A comparative evaluation of sequence classification programs. BMC bioinformatics, 13 (1): 92, 2012.
doi: 10.1186/1471-2105-13-92
Patel U, Chandpura J, Chauhan K, Gupte S. Screening and isolation of an organic solvent tolerant lipase producing bacteria from various oil contaminated sites. Indian J. Appl. Microbiol, 21: 22-36, 2018.
http://www.ijamicro.com/21-1-2018/Unisha%20patel.pdf
Lee LP, Karbul HM, Citartan M, Gopinath SC, Lakshmipriya T, Tang TH. Lipase-secreting Bacillus species in anoil-contaminated habitat: promising strains to alleviate oil pollution. BioMed research international, 2015.
doi: 10.1155/2015/820575
Classen T, Kovacic F, Lauinger B, Pietruszka J, Jaeger KE. Screening for Enantioselective Lipases, Hydrocarbon and Lipid Microbiology Protocols, Springer 37-69, 2016.
doi: 10.1007/8623_2016_218
Zottig X, Meddeb-Mouelhi F, Beauregard M. Development of a high-throughput liquid state assay for lipase activity using natural substrates and rhodamine B. Analytical biochemistry, 496: 25-29, 2016.
doi: 10.1016 / j.ab.2015.11.020
Kumar D, Kumar L, Nagar S, Raina C, Parshad R, Gupta VK. Isolation, production and application of lipase/esterase from Bacillus sp. strain DVL43. Journal of Microbiology and Biotechnology Research, 2: 521-528, 2017.
https://pdfs.semanticscholar.org/f959/bb3f9d549c47f24860f9d61eb4f5110082cc.pdf%20
Akoh CC, Lee GC, Liaw YC, Huang TH, Shaw JF. GDSL family of serine esterases/lipases. Progress in lipid research, 43 (6): 534-552, 2004.
doi: 10.1016/j.plipres.2004.09.002
Ramnath L, Sithole B, Govinden R. Classification of lipolytic enzymes and their biotechnological applications in the pulping industry. Canadian journal of microbiology, 63 (3): 179-192, 2016.
doi: 10.1139/cjm-2016-0447
Seghal-Kiran G, Nishanth-Lipton A, Kennedy J, Dobson AD, Selvin J. A halotolerant thermostable lipase from the marine bacterium Oceanobacillus sp. PUMB02 with an ability to disrupt bacterial biofilms. Bioengineered, 5 (5): 305-318, 2014.
doi: 10.4161/bioe.29898
Kiran GS, Shanmughapriya S, Jayalakshmi J, Selvin J, Gandhimathi R, Sivaramakrishnan S, Natarajaseenivasan K. Optimization of extracellular psychrophilic alkaline lipase produced by marine Pseudomonas sp. (MSI057). Bioprocess and Biosystems Engineering, 31 (5): 483-492, 2008.
doi: 10.1007/s00449-007-0186-0
Selvin J, Kennedy J, Lejon DP, Kiran GS, Dobson AD. Isolation identification and biochemical characterization of a novel halotolerant lipase from the metagenome of the marine sponge Haliclona simulans. Microbial cell factories, 11 (1): 72, 2012.
doi: 10.1186/1475-2859-11-72
Joseph D, Chakraborty K. Production and Biotechnological Application of Extracellular Alkalophilic Lipase from Marine Macroalga-Associated Shewanella algae to Produce Enriched C 20-22 n-3 Polyunsaturated Fatty Acid Concentrate. Applied biochemistry and biotechnology, 185 (1): 55-71, 2017.
doi: 10.1007/s12010-017-2636-8
López-López O, Cerdan M, Gonzalez-Siso M. New extremophilic lipases and esterases from metagenomics. Current Protein and Peptide Science, 15 (5): 445-455, 2014.
doi: 10.2174/1389203715666140228153801
Yuan D, Lan D, Xin R, Yang B, Wang Y. Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007. Biotechnology and applied biochemistry, 63 (1): 41-50, 2016.
doi: 10.1002/bab.1338
De Santi C, Leiros HKS, Di Scala A, de Pascale D, Altermark B, Willassen NP. Biochemical characterization and structural analysis of a new cold-active and salt-tolerant esterase from the marine bacterium Thalassospira sp. Extremophiles, 20 (3): 323-336, 2016.
doi: 10.1007/S00792-016-0824-Z
Hassan SW, Abd El Latif HH, Ali SM. Production of cold active lipase by free and immobilized marine Bacillus cereus HSS: Application in wastewater treatment. Frontiers in microbiology, 9: 2377, 2018.
Esakkiraj P, Prabakaran G, Maruthiah T, Immanuel G, Palavesam A. Purification and Characterization of Halophilic Alkaline Lipase from Halobacillus sp. Proceedings of the National Academy of Sciences, India Section B: Biological Sciences, 86 (2): 309- 314, 2016.
doi: 10.1007/s40011-014-0437-1
Park SH, Kim SJ, Park S, Kim HK. Characterization of Organic Solvent-Tolerant Lipolytic Enzyme from Marinobacter lipolyticus Isolated from the Antarctic Ocean. Applied biochemistry and biotechnology, 187 (3): 1046-1060, 2019.
doi: 10.1007/s12010-018-2865-5
Deng D, Zhang Y, Sun A, Liang J, Hu Y. Functional characterization of a novel marine microbial GDSL lipase and its utilization in the resolution of (±)-1-phenylethanol. Applied biochemistry and biotechnology, 179 (1): 75-93, 2016.
doi: 10.1007/s12010-016-1980-4
Urbanek AK, Rymowicz W, Mirończuk AM. Degradation of plastics and plastic-degrading bacteria in cold marine habitats. Applied microbiology and biotechnology, 102 (18): 7669-7678, 2018.
doi: 10.1007/s00253-018-9195-y
Hama S, Noda H, Kondo A. How lipase technology contributes to evolution of biodiesel production using multiple feedstocks. Current opinion in biotechnology, 50: 57-64, 2018.
doi: 10.1016/j.copbio.2017.11.001
Aykin E, Omuzbuken B, Kacar A. Antibiofilm potential of enzymes as ecofriendly antifouling additives. Fresenius environmental bulletin, 27 (6): 4093-4103, 2018.
Univ. Sci. is registered under a Creative Commons Attribution 4.0 International Public License. Thus, this work may be reproduced, distributed, and publicly shared in digital format, as long as the names of the authors and Pontificia Universidad Javeriana are acknowledged. Others are allowed to quote, adapt, transform, auto-archive, republish, and create based on this material, for any purpose (even commercial ones), provided the authorship is duly acknowledged, a link to the original work is provided, and it is specified if changes have been made. Pontificia Universidad Javeriana does not hold the rights of published works and the authors are solely responsible for the contents of their works; they keep the moral, intellectual, privacy, and publicity rights. Approving the intervention of the work (review, copy-editing, translation, layout) and the following outreach, are granted through an use license and not through an assignment of rights. This means the journal and Pontificia Universidad Javeriana cannot be held responsible for any ethical malpractice by the authors. As a consequence of the protection granted by the use license, the journal is not required to publish recantations or modify information already published, unless the errata stems from the editorial management process. Publishing contents in this journal does not generate royalties for contributors.