References
- Bornscheuer, U. T. Microbial Carboxyl Esterases: Classification, Properties and Application in Biocatalysis. FEMS Microbiol. Rev. 2002, 26, 73–81. DOI: https://doi.org/10.1111/j.1574-6976.2002.tb00599.x.
- Hasan, F.; Shah, A. A.; Hameed, A. Industrial Applications of Microbial Lipases. Enzyme Microb. Technol. 2006, 39, 235–251. DOI: https://doi.org/10.1016/j.enzmictec.2005.10.016.
- Larsen, E. M.; Johnson, R. J. Microbial Esterases and Ester Prodrugs: An Unlikely Marriage for Combating Antibiotic Resistance. Drug Dev. Res. 2019, 80, 33–47. DOI: https://doi.org/10.1002/ddr.21468.
- Rodríguez, M. C.; Loaces, I.; Amarelle, V.; Senatore, D.; Iriarte, A.; Fabiano, E.; Noya, F. Est10: A Novel Alkaline Esterase Isolated from Bovine Rumen Belonging to the New Family XV of Lipolytic Enzymes. PLoS One. 2015, 10, e0126651. DOI: https://doi.org/10.1371/journal.pone.0126651.
- Le, L. T. H. L.; et al. Biodiesel and Flavor Compound Production Using a Novel Promiscuous Cold-Adapted SGNH-Type Lipase (HaSGNH1) from the Psychrophilic Bacterium Halocynthiibacter arcticus. Biotechnol. Biofuels 2020, 13, 1–13.
- Arpigny, J. L.; Jaeger, K. E. Bacterial Lipolytic Enzymes: Classification and Properties. Biochem. J. 1999, 343, 177–183. DOI: https://doi.org/10.1042/0264-6021:3430177.
- Ašler, I. L.; et al. Probing Enzyme Promiscuity of SGNH Hydrolases. Chem. Bio. Chem. 2010, 11, 2158–2167.
- Urbániková, Ľ. CE16 Acetylesterases: In Silico Analysis, Catalytic Machinery Prediction and Comparison with Related SGNH Hydrolases. 3 Biotech. 2021, 11, 84. DOI: https://doi.org/10.1007/s13205-020-02575-w.
- Akoh, C. C.; Lee, G. C.; Liaw, Y. C.; Huang, T. H.; Shaw, J. F. GDSL Family of Serine Esterases/Lipases. Prog. Lipid Res. 2004, 43, 534–552. DOI: https://doi.org/10.1016/j.plipres.2004.09.002.
- Leščić Ašler, I.; Štefanić, Z.; Maršavelski, A.; Vianello, R.; Kojić-Prodić, B. Catalytic Dyad in the SGNH Hydrolase Superfamily: In-Depth Insight into Structural Parameters Tuning the Catalytic Process of Extracellular Lipase from Streptomyces rimosus. ACS Chem. Biol. 2017, 12, 1928–1936. DOI: https://doi.org/10.1021/acschembio.6b01140.
- Korman, T. P.; Sahachartsiri, B., Charbonneau, D. M.; Huang, G. L.; Beauregard, M.; Bowie, J. U. Dieselzymes: Development of a Stable and Methanol Tolerant Lipase for Biodiesel Production by Directed Evolution. Biotechnol. Biofuels 2013, 6, 1–13.
- Jeon, J. H.; Kim, J. T.; Kang, S. G.; Lee, J. H.; Kim, S. J. Characterization and Its Potential Application of Two Esterases Derived from the Arctic Sediment Metagenome. Mar Biotechnol (NY) 2009, 11, 307–316. DOI: https://doi.org/10.1007/s10126-008-9145-2.
- Dieckelmann, M.; Johnson, L. A.; Beacham, I. R. The Diversity of Lipases from Psychrotrophic Strains of pseudomonas: A Novel Lipase from a Highly Lipolytic Strain of Pseudomonas fluorescens. J. Appl. Microbiol. 1998, 85, 527–536. DOI: https://doi.org/10.1046/j.1365-2672.1998.853530.x.
- Joseph, B.; Ramteke, P. W.; Thomas, G. Cold Active Microbial Lipases: Some Hot Issues and Recent Developments. Biotechnol. Adv. 2008, 26, 457–470. DOI: https://doi.org/10.1016/j.biotechadv.2008.05.003.
- Kavitha, M. Cold Active Lipases – an Update. Front. Life Sci. 2016, 9, 226–238. DOI: https://doi.org/10.1080/21553769.2016.1209134.
- Riedel, K.; Talker-Huiber, D.; Givskov, M.; Schwab, H.; Eberl, L. Identification and Characterization of a GDSL Esterase Gene Located Proximal to the Swr Quorum-Sensing System of Serratia liquefaciens MG1. Appl. Environ. Microbiol. 2003, 69, 3901–3910. DOI: https://doi.org/10.1128/AEM.69.7.3901-3910.2003.
- Alcaide, M.; , Tchigvintsev, A.; Martínez-Martínez, M.; Popovic, A.; Reva, O. N.; Lafraya, Á.; Bargiela, R.; Nechitaylo, T. Y.; Matesanz, R.; Cambon-Bonavita, M.-A.; et al. Identification and Characterization of Carboxyl Esterases of Gill Chamber-Associated Microbiota in the Deep-Sea Shrimp Rimicaris exoculata by Using Functional Metagenomics. Appl. Environ. Microbiol. 2015, 81, 2125–2136. DOI: https://doi.org/10.1128/AEM.03387-14.
- Borchert, E.; Selvin, J.; Kiran, S. G.; Jackson, S. A.; O’Gara, F.; Dobson, A. D. W. A Novel Cold Active Esterase from a Deep Sea Sponge Stelletta Normani Metagenomic Library. Front. Mar. Sci. 2017, 4, 287. DOI: https://doi.org/10.3389/fmars.2017.00287.
- Arnau, J.; Lauritzen, C.; Petersen, G. E.; Pedersen, J. Current Strategies for the Use of Affinity Tags and Tag Removal for the Purification of Recombinant Proteins. Protein Expr. Purif. 2006, 48, 1–13. DOI: https://doi.org/10.1016/j.pep.2005.12.002.
- de Almeida, J. M.; Moure, V. R.; Müller-Santos, M.; de Souza, E. M.; Pedrosa, F. O.; Mitchell, D. A.; Krieger, N. Tailoring Recombinant Lipases: Keeping the His-Tag Favors Esterification Reactions, Removing It Favors Hydrolysis Reactions. Sci. Rep. 2018, 8, 10000. DOI: https://doi.org/10.1038/s41598-018-27579-8.
- Singh, A.; Upadhyay, V.; Upadhyay, A. K.; Singh, S. M.; Panda, A. K. Protein Recovery from Inclusion Bodies of Escherichia coli Using Mild Solubilization Process. Microb. Cell Factories. 2015, 14, 41–51.
- Akbari, N.; Khajeh, K.; Rezaie, S.; Mirdamadi, S.; Shavandi, M.; Ghaemi, N. High-Level Expression of Lipase in Escherichia coli and Recovery of Active Recombinant Enzyme through in Vitro Refolding. Protein Expr. Purif. 2010, 70, 75–80. DOI: https://doi.org/10.1016/j.pep.2009.08.009.
- Rosano, G. L.; Ceccarelli, E. A. Recombinant Protein Expression in Escherichia coli: Advances and Challenges. Front. Microbiol. 2014, 5, 172. DOI: https://doi.org/10.3389/fmicb.2014.00172.
- Alibolandi, M.; Mirzahoseini, H. Chemical Assistance in Refolding of Bacterial Inclusion Bodies. Biochem. Res. Int. 2011, 2011, 631607. DOI: https://doi.org/10.1155/2011/631607.
- Humer, D.; Spadiut, O. Wanted: More Monitoring and Control during Inclusion Body Processing. J. Microbiol. Biotechnol. 2018, 34, 158.
- Plucinsky, S. M.; Root, K. T.; Glover, K. J. Efficient Solubilization and Purification of Highly Insoluble Membrane Proteins Expressed as Inclusion Bodies Using Perfluorooctanoic acid. Protein Expr. Purif. 2018, 143, 34–37. DOI: https://doi.org/10.1016/j.pep.2017.10.012.
- Bižić-Ionescu, M.; Amann, R.; Grossart, H. P. Massive Regime Shifts and High Activity of Heterotrophic Bacteria in an Ice-Covered Lake. PLoS One. 2014, 9, e113611. DOI: https://doi.org/10.1371/journal.pone.0113611.
- Gasteiger, E.; Hoogland, C.; Gattiker, A.; Duvaud, S.; Wilkins, M. R.; Appel, R. D.; Bairoch, A. Protein Identification and Analysis Tools on the ExPASy Server. In The Proteomics Protocols Handbook. Springer Protocols Handbooks. Humana Press. 2005. http://www.expasy.org/tools/. DOI: https://doi.org/10.1385/1-59259-890-0:571.
- Lazar, I.; Zwecker-Lazar, I.; GelAnalyzer. 2010a (www.gelanalyzer.com).
- Demir, B. S.; Tükel, S. S. Purification and Characterization of Lipase from Spirulina Platensis. J. Mol. Catal. B Enzym. 2010, 64, 123–128. DOI: https://doi.org/10.1016/j.molcatb.2009.09.011.
- Bateman, A. UniProt: A Worldwide Hub of Protein Knowledge. Nucleic Acids Res. 2019, 47, D506–D515.
- Han, M. J.; Park, S. J.; Park, T. J.; Lee, S. Y. Roles and Applications of Small Heat Shock Proteins in the Production of Recombinant Proteins in Escherichia coli. Biotechnol. Bioeng. 2004, 88, 426–436. DOI: https://doi.org/10.1002/bit.20227.
- Cabrita, L. D.; Bottomley, S. P. Protein Expression and refolding-a practical guide to getting the most out of inclusion bodies. Biotechnol. Annu. Rev. 2004, 10, 31–50. DOI: https://doi.org/10.1016/S1387-2656(04)10002-1.
- Baneyx, F.; Mujacic, M. Recombinant Protein Folding and Misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22, 1399–1407. DOI: https://doi.org/10.1038/nbt1029.
- Kyte, J.; Doolittle, R. F. A Simple Method for Displaying the Hydropathic Character of a Protein. J. Mol. Biol. 1982, 157, 105–132. DOI: https://doi.org/10.1016/0022-2836(82)90515-0.
- Rieth, M. D.; Root, K. T.; Glover, K. J. Reconstitution of Full-Length Human Caveolin-1 into Phospholipid Bicelles: Validation by Analytical Ultracentrifugation. Biophys. Chem. 2020, 259, 106339.
- Murray, D. T.; Griffin, J.; Cross, T. A. Detergent Optimized Membrane Protein Reconstitution in Liposomes for Solid State NMR. Biochemistry 2014, 53, 2454–2463. DOI: https://doi.org/10.1021/bi500144h.
- Mittendorf, K. F.; Marinko, J. T.; Hampton, C. M.; Ke, Z.; Hadziselimovic, A.; Schlebach, J. P.; Law, C. L.; Li, J.; Wright, E. R.; Sanders, C. R.; et al. Peripheral Myelin Protein 22 Alters Membrane Architecture. Sci. Adv. 2017, 3, e1700220. DOI: https://doi.org/10.1126/sciadv.1700220.
- Peterson, A. M.; Tan, Z.; Kimbrough, E. M.; Heemstra, J. M. 3. 3′-Dioctadecyloxacarbocyanine Perchlorate (DiO) as a Fluorogenic Probe for Measurement of Critical Micelle Concentration. Anal. Methods 2015, 7, 6877–6882. DOI: https://doi.org/10.1039/C5AY01444A.
- Hyde, A. M.; Zultanski, S. L.; Waldman, J. H.; Zhong, Y.-L.; Shevlin, M.; Peng, F. General Principles and Strategies for Salting-Out Informed by the Hofmeister Series. Org. Process Res. Dev. 2017, 21, 1355–1370. DOI: https://doi.org/10.1021/acs.oprd.7b00197.
- Makowski, M.; Bogunia, M. Influence of Ionic Strength on Hydrophobic Interactions in Water: Dependence on Solute Size and Shape. J. Phys. Chem. B. 2020, 124, 10326–10336. DOI: https://doi.org/10.1021/acs.jpcb.0c06399.
- Yang, Z.; Zhang, Y.; Shen, T.; Xie, Y.; Mao, Y.; Ji, C. Cloning, Expression and Biochemical Characterization of a Novel, Moderately Thermostable GDSL Family Esterase from Geobacillus thermodenitrificans T2. J. Biosci. Bioeng. 2013, 115, 133–137. DOI: https://doi.org/10.1016/j.jbiosc.2012.08.016.
- Soni, S.; Sathe, S. S.; Odaneth, A. A.; Lali, A. M.; Chandrayan, S. K. SGNH Hydrolase-Type Esterase Domain Containing Cbes-AcXE2: A Novel and Thermostable Acetyl Xylan Esterase from Caldicellulosiruptor bescii. Extremophiles 2017, 21, 687–697. DOI: https://doi.org/10.1007/s00792-017-0934-2.
- Wang, G.; Wang, Q.; Lin, X.; Ng, T. B.; Yan, R.; Lin, J.; Ye, X. A Novel Cold-Adapted and Highly Salt-Tolerant Esterase from Alkalibacterium sp. SL3 from the Sediment of a Soda Lake. Sci. Rep. 2016, 6, 19494. DOI: https://doi.org/10.1038/srep19494.
- Shakiba, M. H.; Ali, M. S. M.; Rahman, R. N. Z. R. A.; Salleh, A. B.; Leow, T. C. Cloning, Expression and Characterization of a Novel Cold-Adapted GDSL Family Esterase from Photobacterium sp. strain J15. Extremophiles 2016, 20, 45–55. DOI: https://doi.org/10.1007/s00792-015-0796-4.
- Cieśliński, H.; Białkowska, A. M.; Długołecka, A.; Daroch, M.; Tkaczuk, K. L.; Kalinowska, H.; Kur, J.; Turkiewicz, M. A Cold-Adapted Esterase from Psychrotrophic Pseudoalteromas sp. strain 643A. Arch. Microbiol. 2007, 188, 27–36. DOI: https://doi.org/10.1007/s00203-007-0220-2.
- Wicka, M.; Wanarska, M.; Krajewska, E.; Pawlak-Szukalska, A.; Kur, J.; Cieśliński, H. Cloning, Expression, and Biochemical Characterization of a Cold-Active GDSL-Esterase of a Pseudomonas sp. S9 Isolated from Spitsbergen Island Soil. Acta Biochim Pol. 2016, 63, 117–125. DOI: https://doi.org/10.18388/abp.2015_1074.
- de Groot, N. S.; Ventura, S. Effect of Temperature on Protein Quality in Bacterial Inclusion Bodies. FEBS Lett. 2006, 580, 6471–6476. DOI: https://doi.org/10.1016/j.febslet.2006.10.071.
- Fink, A. L. Protein Aggregation: Folding Aggregates, Inclusion Bodies and Amyloid. Fold. Des. 1998, 3, R9–R23. DOI: https://doi.org/10.1016/S1359-0278(98)00002-9.
- Schomburg, I.; et al. BRENDA in 2013: Integrated Reactions, Kinetic Data, Enzyme Function Data, Improved Disease Classification: New Options and Contents in BRENDA. Nucleic Acids Res. 2013, 41, D764-D772.
- Alalouf, O.; Balazs, Y.; Volkinshtein, M.; Grimpel, Y.; Shoham, G.; Shoham, Y. A New Family of Carbohydrate Esterases is Represented by a GDSL Hydrolase/Acetylxylan Esterase from Geobacillus stearothermophilus. J. Biol. Chem. 2011, 286, 41993–42001. DOI: https://doi.org/10.1074/jbc.M111.301051.
- Dimitriou, P. S.; Denesyuk, A.; Takahashi, S.; Yamashita, S.; Johnson, M. S.; Nakayama, T.; Denessiouk, K. Alpha/Beta-Hydrolases: A Unique Structural Motif Coordinates Catalytic Acid Residue in 40 Protein Fold Families. Proteins 2017, 85, 1845–1855. DOI: https://doi.org/10.1002/prot.25338.
- Li, Z.; et al. Structure-Guided Protein Engineering Increases Enzymatic Activities of the SGNH Family Esterases. Biotechnol. Biofuels 2020, 13, 1–14.
- Novototskaya-Vlasova, K.; Petrovskaya, L.; Yakimov, S.; Gilichinsky, D. Cloning, Purification, and Characterization of a Cold-Adapted Esterase Produced by Psychrobacter cryohalolentis K5T from Siberian Cryopeg. FEMS Microbiol Ecol. 2012, 82, 367–375. DOI: https://doi.org/10.1111/j.1574-6941.2012.01385.x.
- Novototskaya-Vlasova, K.; Petrovskaya, L.; Kryukova, E.; Rivkina, E.; Dolgikh, D.; Kirpichnikov, M. Expression and Chaperone-Assisted Refolding of a New Cold-Active Lipase from Psychrobacter cryohalolentis K5(T). Protein Expr. Purif. 2013, 91, 96–103. DOI: https://doi.org/10.1016/j.pep.2013.07.011.
- Yoo, W.; Le, L. T. H. L.; Lee, J. H.; Kim, K. K.; Kim, T. D. A Novel Enantioselective SGNH Family Esterase (NmSGNH1) from Neisseria Meningitides: Characterization, Mutational Analysis, and Ester Synthesis. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 2019, 1864, 1438–1448. DOI: https://doi.org/10.1016/j.bbalip.2019.07.007.