Abstract
Pseudomonas aeruginosa is a Gram-negative and rod-shaped bacterium. It can use a variety of carbon sources and grow in different culture media. Its versatile extracellular enzymes give it the ability to grow on complex carbon sources. One of the most important enzymes of this bacterium is lipase, which is an extracellular enzyme. Lipases are one of the most useful enzymes in medicine and industry, especially in the detergent industry. In recent years, lipases have become an important component of detergent powders, so it is important to evaluate the performance of lipases in the presence of detergents. The aim of this study was to investigate the effect of non-ionic detergents Tween 20 and 80 on the activity of the Pseudomonas lipase. These detergents reduced Km and increased Vmax of the enzyme. The enzyme activity increased in the presence of these detergents at optimal pH and temperature. Conformational studies with the purified enzyme by fluorescence spectrophotometry showed that in the presence of Tween 20 and 80, there was a hypochromicity in emission peak of the enzyme, which indicated that the enzyme became less compact in vicinity of these detergents.
Similar content being viewed by others
References
Gellatly, S. L., & Hancock, R. E. (2013). Pseudomonas aeruginosa: new insights into pathogenesis and host defenses. Pathogens and Disease, 67, 159–173.
Williams, B. J., Dehnbostel, J., & Blackwell, T. S. (2010). Pseudomonas aeruginosa: host defense in lung diseases. Respirology, 15, 1037–1056 .
Traill, Z. C., Miller, R. F., Ali, N., & Shaw, P. J. (1996). Pseudomonas aeruginosa bronchopulmonary infection in patients with advanced human immunodeficiency virus disease. British Journal of Radiology, 69, 1099–1103.
Allouche, N., Damak, M., Ellouz, R., & Sayadi, S. (2004). Use of whole cells of Pseudomonas aeruginosa for synthesis of the antioxidant hydroxytyrosol via conversion of Tyrosol. Applied and Environmental Microbiology, 70, 2105–2109.
Kalyani, D. C., Telke, A. A., Surwase, S. N., et al. (2012). Effectual decolorization and detoxification of triphenylmethane dye malachite green (MG) by Pseudomonas aeruginosa NCIM 2074 and its enzyme system. Clean Technologies and Environmental Policy, 14, 989–1001.
Ojewumi, M. E., Okeniyi, J. O., Ikotun, J. O., Okeniyi, E. T., Ejemen, V. A., & Popoola, A. P. I. (2018). Bioremediation: data on Pseudomonas aeruginosa effects on the bioremediation of crude oil polluted soil. Data Brief, 19, 101–113.
Lee, J., Boyapati, G., Song, K., Rhee, S., & Kim, C. (2000). Cloning and sequence analysis of the estA gene encoding enzyme for producing(R)-beta-acetyl mercapto isobutyric acid from Pseudomonas aeruginosa 1001. Journal of Bioscience and Bioengineering, 90, 684–687.
Javed, S., Azeem, F., Hussain, S., Rasul, I., Siddique, M. H., Riaz, M., Afzal, M., Kouser, A., & Nadeem, H. (2018). Bacterial lipases: a review on purification and characterization. Progress in Biophysics and Molecular Biology, 132, 23–34.
Houde, A., Kademi, A., & Leblanc, D. (2004). Lipases and their industrial applications: an overview. Applied Biochemistry and Biotechnology, 118, 155–170.
Kumar, C. G., Malik, R. K., & Tiwari, M. P. (1998). Novel enzyme-based detergents: an Indian perspective. Current Science, 75, 1312–1318.
Ito, S., Kobayashi, T., Ara, K., Ozaki, K., Kawai, S., & Hatada, Y. (1998). Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures. Extremophiles, 2, 185–190.
Hasan, F., Shah, A. A., Javed, S., & Hameed, A. (2010). Enzymes used in detergents: Lipases. African Journal of Biotechnology, 9, 4836–4844.
Smulders, S., Rybinski, W., Sung, E., Rähse, W., Steber, J., Wiebel, F., & Nordskog, N. (2007). Laundry detergents. In Ullmann’s encyclopedia of industrial chemistry, 7th edn. Wiley-VCH: Weinheim, Germany (pp. 1–184).
Glittenberg, D. (2012). Starch-based biopolymers in paper, corrugating, and other industrial applications. Polymer Science, 10, 165–193.
European Food Safety Authority (EFSA). (2015). Scientific opinion on the re-evaluation of polyoxyethylene sorbitan monolaurate (E 432), polyoxyethylene sorbitan monooleate (E 433), polyoxyethylene sorbitan monopalmitate (E 434), polyoxyethylene sorbitan monostearate (E 435) and polyoxyethylene sorbitan tristearate (E 436) as food additives. EFSA Journal, 13(7), 4152.
Talebi, M., Minai-Tehrani, D., Fazilati, M., & Minai-Tehrani, A. (2018). Inhibitory action of dicyclomine on lipase activity, kinetics and molecular study. International Journal of Biological Macromolecules, 107, 2422–2428.
Kerwin, B. A. (2008). Polysorbates 20 and 80 used in the formulation of protein biotherapeutics: structure and degradation pathways. Journal of Pharmaceutical Sciences, 97, 2924–2935.
Mozaffar, Z., Weete, J. D., & Dute, R. (1994). Influence of surfactants on an extracellular lipase from Pythium ultimum. Journal of the American Oil Chemists’ Society, 71, 75.
Xia, J., Chen, X., & Nnanna, I. A. (1996). Activity and stability of Penicillium cyclopium lipase in surfactant and detergent solutions. Journal of the American Oil Chemists’ Society, 73, 115–120.
Mogensen, J. E., Sehgal, P., & Otzen, D. E. (2005). Activation, inhibition, and destabilization of Thermomyces lanuginosus lipase by detergents. Biochemistry, 44, 1719–1730.
Liu, Y. Y., Xu, J. H., & Hu, Y. (2000). Enhancing effect of Tween-80 on lipase performance in enantioselective hydrolysis of ketoprofen ester. Journal of Molecular Catalysis B: Enzymatic, 10, 523–529.
Goswami, D. (2020). Lipase catalysis in presence of nonionic surfactants. Applied Biochemistry and Biotechnology, 191, 744–762.
Lailaja, V. P., & Chandrasekaran, M. (2013). Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11. World Journal of Microbiology & Biotechnology, 29, 1349–1360.
Mobarak-Qamsari, E., Kasra-Kermanshahi, R., & Moosavi-Nejad, Z. (2011). Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110. Iranian Journal of Microbiology, 3, 92–98.
Saisubramanian, N., Edwinoliver, N. G., Nandakumar, N., Kamini, N. R., & Puvanakrishnan, R. (2006). Efficacy of lipase from Aspergillus niger as an additive in detergent formulations: a statistical approach. Journal of Industrial Microbiology and Biotechnology, 33, 669–676.
Chauhan, M., Chauhan, R. S., & Garlapati, V. K. (2013). Evaluation of a new lipase from Staphylococcus sp. for detergent additive capability. BioMed Research International, 2013, 1–6.
Cherif, S., Mnif, S., Hadrich, F., Abdelkafi, S., & Sayadi, S. (2011). A newly high alkaline lipase: an ideal choice for application in detergent formulations. Lipids in Health and Disease, 10, 221–228.
Niyonzima, F. N., & More, S. S. (2015). Microbial detergent compatible lipases. Journal of Scientific and Industrial Research (India), 74, 105–113.
Jafari, N., Dehganpour, H., Ghavanini, N., Mollasalehi, H., & Minai-Tehrani, D. (2017). Interaction of antipsychotic drugs with sucrase, kinetics and structural study. Current Clinical Pharmacology, 12, 50–54.
Lundahl, P., Mascher, E., Kameyama, K., & Takagi, T. (1990). Water-soluble proteins do not bind octyl glucoside as judged by molecular sieve chromatographic techniques. Journal of Chromatography A, 518, 111–21.
Otzen, D. E., Sehgal, P., & Westh, P. (2009). Alpha-Lactalbumin is unfolded by all classes of surfactants but by different mechanisms. Journal of Colloid and Interface Science, 329, 273–283.
Yang, Z., Wang, C., Zhou, Q., et al. (2014). Membrane protein stability can be compromised by detergent interactions with the extramembranous soluble domains. Protein Science, 23, 769–789.
Dwivedi, P., Rodriguez, J., Ibe, N. U., & Weers, P. M. M. (2016). Deletion of the N- or C-terminal helix of apolipophorin III to create a four-helix bundle protein. Biochemistry, 55, 3607–3615.
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interest.
Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Shoja, M., Minai-Tehrani, D. Effect of Tween Type Non-Ionic Detergent on the Activity of Lipase of Pseudomonas aeruginosa. Cell Biochem Biophys 79, 87–92 (2021). https://doi.org/10.1007/s12013-020-00946-x
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s12013-020-00946-x