Lipolytic activity of microorganisms isolated from waste waters contaminated with fats
Abstract
Lipases are one of the groups of enzymes with the highest number of industrial and biotechnological applications, processing of dairy foods and oils, detergents, cosmetics, leather, pharmaceuticals, paper, production of surfactants, biodiesel and recently as a promising alternative for the treatment of wastewater contaminated with lipids. In this study, microorganisms were isolated from wastewater samples containing fats and extracellular lipase production was determined using p-nitrophenylpalmitate. From the 149 isolates obtained, 37 showed lipolytic activity and strain CCEI-1, identified as Serratia marcescens, had the highest activity at alkaline pH and at 30°C. Also degraded lipids and produced pigmentation on solid medium at pH 8,0 and 50°C. The culture supernatants of S. marcescens used to determine thermal stability at 50°C indicate that the enzyme is stable at this temperature and at alkaline pH. The enzyme was partially purified and electrophoresed (SDS-PAGE) where bands between 40 and 116 kDa were detected. The results obtained in this study indicate that the strain CCEI-1 of S. marcescens can be a possible source of thermostable lipases with industrial and biotechnological applications.Downloads
Languages:
es;en.References
ANOBOM, C.D., PINHEIRO, A., DE-ANDRADE, R. et al. From Structure to Catalysis: Recent Developments in the Biotechnological Applications of Lipases. BioMed Research International, 2014, , 2014, p. 1-11.
SHARMA, S. and KANWAR, S. Organic Solvent Tolerant Lipases and Applications. The Scientific World Journal, 2014, 2014, p. 1-15.
RABBANI, M., BAGHERINEJAD, M., SADEGHI H., et al. Isolation and characterization of novel thermophilic lipase-secreting bacteria. Brazilian Journal of Microbiology, 44(4), 2013, p.1113-1119.
CHERIF, S., ALOUI, F., CARRIERRE, F., et al. Lipase Pre-Hydrolysis Enhance Anaerobic Biodigestion of Soap Stock from an Oil Refining Industry. Journal of Oleo Science, 63(2), 2014, p. 109-114.
BRABCOVÁ, J., DEMIANOVÁ, Z., VONDRÁŠEK, J., et al. Highly selective purification of three lipases from Geotrichum candidum 4013 and their characterization and biotechnological applications. Journal of Molecular Catalysis B: Enzymatic, 98, 2013, p. 62-72.
GOPINATH, S., ANBU, P., LAKSHMIPRIYA, T., et al. Strategies to Characterize Fungal Lipases for Applications in Medicine and Dairy Industry. BioMed Research International, 2013, 2013, p. 1-10.
SARANYA, P., SUKANYA, H., PRASAD, B., et al. Lipase production from a novel thermo-tolerant and extreme acidophile Bacillus pumilus using palm oil as the substrate and treatment of palm oil-containing wastewater. Environmental science and pollution research, 21(5), 2014, p. 3907-3919.
FACCHINI, A., VICI, A., PEREIRA, M., et al. Enhanced lipase production of Fusarium verticillioides by using response surface methodology and wastewater pretreatment application. Journal of Biochemical Technology, 6(3), 2015, p. 996-1002.
PALMEROS, B., GUERECA, L., ALAGÓN, A., et al. Biochemical characterization of the lipolytic activity of Pseudomonas aeruginosa IGB 83. Process Biochem, 29(3), 1994, p. 207-212.
KOUKER, G. and JAEGER, K.E. Specific and sensitive plate assay for bacterial lipases.Applied and Environmental Microbiology, 53 (1), 1987, p. 211–213.
LI, M., YANG, L., XU, G., et al. Screening, purification and characterization of a novel cold-active and organic solvent-tolerant lipase from Stenotrophomonas maltophilia CGMCC 4254. Bioresource Technology, 148, 2013, p. 114-120.
HASAN, F., SHAH, A. and HAMEED, A. Purification and characterization of a mesophilic lipase from Bacillus subtilis FH5 stable at high temperature and pH. Acta Biologica Hungarica, 58(1), 2007, p. 115-132.
CERVANTES, E., SALAZAR, L. y DIAZ, P. Lipasas inducidas por hidrocarburos de petróleo. Revista Internacional de Contaminación Ambiental, 29(2), 2013, p. 9-15.
RAO, L., XUE, Y., ZHENG, Y., et al. A Novel Alkaliphilic Bacillus Esterase Belongs to the 13th Bacterial Lipolytic Enzyme Family. PLoS One, 8(4), 2013, e60645.
JIANG, H., ZHANG, S., GAO, H., et al. Characterization of a cold-active esterase from Serratia sp. and improvement of thermostability by directed evolution. BMC Biotechnology, 16(1), 2016, p. 1-11.
GUPTA, R., RATHI, P., GUPTA, N., et al. Lipase Assays for Conventional and Molecular Screening: An Overview. Biotechnology and Applied Biochemistry, 37, 2003, p. 63-71.
MOHAMMADI, M., SEPEHRIZADEH, Z., EBRAHIM. H., et al.Bacterial expression and characterization of an active recombinant lipase A from Serratia marcescens with truncated C-terminal region. Journal of Molecular Catalysis B: Enzymatic, 120, 2015, p. 84-92.
ZHAO, L., XU, J., ZHAO, J., et al. Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010. Process Biochemistry, 43(6), 2008, p. 626-633.
SU, E., XU, J. and YOU, P.Functional expression of Serratia marcescens H30 lipase in Escherichia coli for efficient kinetic resolution of racemic alcohols in organic solvents. Journal of Molecular Catalysis B: Enzymatic, 106, 2014, p.11-16.
ŠIEKŠTELĖ, R., VETEIKYTĖ, A., TVASKA, B., et al. Yeast Kluyveromyces lactis as host for expression of the bacterial lipase: cloning and adaptation of the new lipase gene from Serratia sp. Journal of Industrial Microbiology & Biotechnology, 42(10), 2015, p.1309-1317
WANG, S., WANG, C., YEN, Y.,et al. Enhanced production of insecticidal prodigiosin from Serratia marcescens TKU011 in media containing squid pen. Process Biochemistry, 47(11), 2012, p. 1684-1690.
ZANG, C., YEH, C., CHANG, W., et al. Identification and enhanced production of prodigiosin isoform pigment from Serratia marcescens N10612. Journal of the Taiwan Institute of Chemical Engineers, 45(4), 2014, p. 1133-1139.
DARSHAN, N. and MANONMANI, H. Prodigiosin and its potential applications. Journal of Food Science and Technology, 52(9), 2015, p. 5393-5407
Spanish
English
.png)
