1 |
Schulze B, Klibanov AM. 1991. Inactivation and stabilization of stabilisins in neat organic solvents. Biotechnol. Bioeng. 38: 1001-1006.
DOI
|
2 |
Gorman LA, Dordick JS. 1992. Organic solvents strip water off enzymes. Biotechnol. Bioeng. 39: 392-397.
DOI
|
3 |
Trodler P, Pleiss J. 2008. Modeling structure and flexibility of Candida antarctica lipase B in organic solvents. BMC Struct. Biol. 8: 9.
DOI
|
4 |
Dachuri V, Boyineni J, Choi S, Chung H-S, Jang S-H, Lee C. 2016. Organic solvent-tolerant, cold-adapted lipases PML and LipS exhibit increased conformational flexibility in polar organic solvents. J. Mol. Catal. B: Enzym. 131: 73-78.
DOI
|
5 |
Hwang S, Shao Q, Williams H, Hilty C, Gao YQ. 2011. Methanol strengthens hydrogen bonds and weakens hydrophobic interactions in proteins--a combined molecular dynamics and NMR study. J. Phys. Chem. B. 115: 6653-6660.
DOI
|
6 |
Moore JC, Arnold FH. 1996. Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat. Biotechnol. 14: 458-467.
DOI
|
7 |
Martinez P, Van Dam ME, Robinson AC, Chen K, Arnold FH. 1992. Stabilization of substilisin E in organic solvents by site-directed mutagenesis. Biotechnol. Bioeng. 39: 141-147.
DOI
|
8 |
Sood S, Sharma A, Sharma N, Kanwar SS. 2016. Carboxylesterases: sources, characterization and broader applications. Insight Enzy. Res. 1: 1-11.
|
9 |
Hong S, Lee C, Jang SH. 2012. Purification and properties of an extracellular esterase from a cold-adapted Pseudomonas mandelii. Biotechnol. Lett. 34: 1051-1055.
DOI
|
10 |
Dou S, Kong XD, Ma BD, Chen Q, Zhang J, Zhou J, et al. 2014. Crystal structures of Pseudomonas putida esterase reveal the functional role of residues 187 and 287 in substrate binding and chiral recognition. Biochem. Biophys. Res. Commun. 446: 1145-1150.
DOI
|
11 |
Santiago M, Ramirez-Sarmiento CA, Zamora RA, Parra LP. 2016. Discovery, molecular mechanisms, and industrial applications of cold-active enzymes. Front. Microbiol. 7: 1408.
|
12 |
Kawata T, Ogino H. 2009. Enhancement of the organic solvent-stability of the LST-03 lipase by directed evolution. Biotechnol. Prog. 25: 1605-1611.
|
13 |
Kawata T, Ogino H. 2010. Amino acid residues involved in organic solvent-stability of the LST-03 lipase. Biochem. Biophys. Res. Commun. 400: 384-388.
DOI
|
14 |
Affleck R, Haynes CA, Clark DS. 1992. Solvent dielectric effects on protein dynamics. Proc. Natl. Acad. Sci. USA 89: 5167-5170.
DOI
|
15 |
Dachuri V, Boyineni J, Choi S, Chung H-S, Jang S-H, Lee C. 2016. Organic solvent-tolerant, cold-adapted lipases PML and LipS exhibit increased conformational flexibility in polar organic solvents. J. Mol. Catal. B Enzym. 131: 73-78.
DOI
|
16 |
Lee C, Jang S-H, Chung H-S. 2017. Improving the stability of cold-adapted enzymes by immobilization. Catalysts 7: 112.
DOI
|
17 |
Wang Y, Ryu BH, Yoo W, Lee CW, Kim KK, Lee JH, et al. 2018. Identification, characterization, immobilization, and mutational analysis of a novel acetylesterase with industrial potential (LaAcE) from Lactobacillus acidophilus. Biochim. Biophys. Acta 1862: 197-210.
DOI
|
18 |
Korman TP, Sahachartsiri B, Charbonneau DM, Huang GL, Beauregard M, Bowie JU. 2013. Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution. Biotechnol. Biofuels. 6: 70.
DOI
|
19 |
Chen KQ, Robinson AC, Van Dam ME, Martinez P, Economou C, Arnold FH. 1991. Enzyme engineering for nonaqueous solvents. II. Additive effects of mutations on the stability and activity of subtilisin E in polar organic media. Biotechnol. Prog. 7: 125-129.
DOI
|
20 |
Horvath C. 1974. Pellicular immobilized enzymes. Biochim. Biophys. Acta 358: 164-177.
DOI
|
21 |
Inada Y, Takahashi K, Yoshimoto T, Ajima A, Matsushima A, Saito Y. 1986. Application of polyethylene glycol-modified enzymes in biotechnological processes: organic solvent-soluble enzymes. Trends Biotechnol. 4: 190-194.
DOI
|
22 |
Okahata Y, Mori T. 1997. Lipid-coated enzymes as efficient catalysts in organic media. Trends Biotechnol. 15: 50-54.
DOI
|
23 |
Ogino H, Ishikawa H. 2001. Enzymes which are stable in the presence of organic solvents. J. Biosci. Bioeng. 91: 109-116.
DOI
|
24 |
Ogino H, Miyamoto K, Yasuda M, Ishimi K, Ishikawa H. 1999. Growth of organic solvent-tolerant Pseudomonas aeruginosa LST-03 in the presence of various organic solvents and production of lipolytic enzyme in the presence of cyclohexane. Biochem. Eng. J. 4: 1-6.
DOI
|
25 |
Lee YM, Kim G, Jung YJ, Choe CD, Yim JH, Lee HK, et al. 2012. Polar and alpine microbial collection (PAMC): a culture collection dedicated to polar and alpine microorganisms. Polar Biol. 35: 1433-1438.
DOI
|
26 |
Shin SC, Ahn DH, Lee JK, Kim SJ, Hong SG, Kim EH, et al. 2012. Genome sequence of Sphingomonas sp. strain PAMC 26605, isolated from Arctic lichen (Ochrolechia sp.). J. Bacteriol. 194: 1607.
DOI
|
27 |
Chun J, Lee JH, Jung Y, Kim M, Kim S, Kim BK, et al. 2007. EzTaxon: a web-based tool for the identification of prokaryotes based on 16S ribosomal RNA gene sequences. Int. J. Syst. Evol. Microbiol. 57: 2259-2261.
DOI
|
28 |
Tanaka A, Kawamoto T. 1991. Immobilized enzymes in organic solvents. Bioprocess Technol. 14: 183-208.
|
29 |
Ribera J, Estupinan M, Fuentes A, Fillat A, Martinez J, Diaz P. 2017. Bacillus sp. JR3 esterase LipJ: A new mesophilic enzyme showing traces of a thermophilic past. PLoS One 12: e0181029.
DOI
|
30 |
Ogino H, Miyamoto K, Ishikawa H. 1994. Organic-solvent-tolerant bacterium which secretes organic-solvent-stable lipolytic enzyme. Appl. Environ. Microbiol. 60: 3884-3886.
|
31 |
Ogino H, Yasui K, Shiotani T, Ishihara T, Ishikawa H. 1995. Organic solvent-tolerant bacterium which secretes an organic solvent-stable proteolytic enzyme. Appl. Environ. Microbiol. 61: 4258-4262.
|
32 |
Bahar FG, Imai T. 2013. Aspirin hydrolysis in human and experimental animal plasma and the effect of metal cations on hydrolase activities. Drug Metab. Dispos. 41: 1450-1456.
DOI
|
33 |
Kyte J, Doolittle RF. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105-132.
DOI
|
34 |
Markowitz VM, Chen IM, Palaniappan K, Chu K, Szeto E, Grechkin Y, et al. 2012. IMG: the Integrated Microbial Genomes database and comparative analysis system. Nucleic Acids Res. 40: D115-122.
DOI
|
35 |
Nakamura AM, Nascimento AS, Polikarpov I. 2017. Structural diversity of carbohydrate esterases. Biotechnol. Res. Innov. 1: 35-51.
DOI
|
36 |
Cameron GW, Jordan KN, Holt PJ, Baker PB, Lowe CR, Bruce NC. 1994. Identification of a heroin esterase in Rhodococcus sp. strain H1. Appl. Environ. Microbiol. 60: 3881-3883.
|
37 |
Pereira MR, Maester TC, Mercaldi GF, de Macedo Lemos EG, Hyvonen M, Balan A. 2017. From a metagenomic source to a high-resolution structure of a novel alkaline esterase. Appl. Microbiol. Biotechnol. 101: 4935-4949.
DOI
|
38 |
Hong DK, Jang S-H, Lee C. 2016. Gene cloning and characterization of a psychrophilic phthalate esterase with organic solvent tolerance from an Arctic bacterium Sphingomonas glacialis PAMC 26605. J. Mol. Catal. B: Enzym. 133: S337-S345.
DOI
|
39 |
Tutino ML, di Prisco G, Marino G, de Pascale D. 2009. Cold-adapted esterases and lipases: from fundamentals to application. Protein Pept. Lett. 16: 1172-1180.
DOI
|
40 |
Zhang DC, Busse HJ, Liu HC, Zhou YG, Schinner F, Margesin R. 2011. Sphingomonas glacialis sp. nov., a psychrophilic bacterium isolated from alpine glacier cryoconite. Int. J. Syst. Evol. Microbiol. 61: 587-591.
DOI
|
41 |
Gupta MN. 1992. Enzyme function in organic solvents. Eur. J. Biochem. 203: 25-32.
DOI
|
42 |
Kumar A, Dhar K, Kanwar SS, Arora PK. 2016. Lipase catalysis in organic solvents: advantages and applications. Biol. Proced. Online 18: 1-11.
DOI
|
43 |
Khmelnitsky YL, Levashov AV, Klyachko NL, Martinek K. 1988. Engineering biocatalytic systems in organic media with low water content. Enzyme Microb. Tech. 10: 710-724.
DOI
|
44 |
Dordick JS. 1989. Enzymatic catalysis in monophasic organic solvents. Enzyme Microb. Tech. 11: 194-211.
DOI
|