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Received January 19, 2018
Accepted June 24, 2018
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This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits
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Investigation of the cell disruption methods for maximizing the extraction of arginase from mutant Bacillus licheniformis (M09) using statistical approach
Department of Food Engineering and Technology, Institute of Chemical Technology, Mumbai 400019, India
Korean Journal of Chemical Engineering, October 2018, 35(10), 2024-2035(12), 10.1007/s11814-018-0107-8
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Abstract
Arginase, an intracellular enzyme produced by Bacillus licheniformis (NRS-1264) is effectively used as a drug in the treatment of arginine-dependent cancers, and it is essential for controlling acute neurological disorders. We investigated the effect of various cell disruption methods for maximizing the extraction of intracellular arginase from mutant Bacillus licheniformis (M09), followed by comparing optimization methods, one factor at a time (OFAT), evolutionary operation (EVOP) and response surface method (RSM). Ultrasonication for 2-5min having a suspension volume in the range of 12-20mL at a radio frequency power between 30-70 W appeared to be the most effective extraction technique for arginase. The arginase yield decreased in the range of 50-70 W of RF power/16-20mL suspension volume and 4-5min sonication time. EVOP predicted a maximum arginase extraction of 3,910 IUㆍL-1 at 2min sonication having 16mL suspension volume at 30W RF power. However, response surface optimization suggested an optimized condition of 3min sonication having 14.5mL suspension volume at 35W RF power in which the maximum arginase activity in the medium was 3,600 IUㆍL-1.
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References
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Borkovich KA, Weiss RL, J. Biol. Chem., 262, 7081 (1987)
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Chang YK, Chu L, Biochem. Eng. J., 35, 37 (2007)
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Barba FJ, Grimi N, Vorobiev E, Food Eng. Rev., 7, 45 (2015)
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Rosello-Soto E, Parniakov O, Barba FJ, Food Eng. Rev., 8, 214 (2016)
Puri M, Gupta S, Pahuja P, Kaur A, Kanwar JR, Kennedy JF, Appl. Biochem. Biotechnol., 160(1), 98 (2010)
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Barba FJ, Zhu Z, Orlien V, Trends Food Sci. Technol., 49, 96 (2016)
Banerjee R, Bhattacharyya BC, Biotechnol. Bioeng., 41, 67 (1993)
Dagbagli S, Goksungur Y, Electron. J. Biotechnol., 11, 11 (2008)
Liu Y, Gong G, Wu S, Carbohydr. Polym., 110, 278 (2014)
Joshi C, Singhal RS, Biocat. Agri. Biotech., 8, 228 (2016)
Andersen CJ, Strange B, Scand. J. Clin. Lab. Investig., 11, 122 (1959)
Asakura T, Adachi K, Schwartz E, J. Biol. Chem., 253, 6423 (1978)
Dange AD, Masurekar VB, J. Biosci., 3, 129 (1981)
Mukherjee G, Banerjee R, Appl. Biochem. Biotechnol., 118(1-3), 33 (2004)
Middelberg APJ, Biotechnol. Adv., 13, 491 (1995)
Singhal RS, Jayakar SS, Glob. J. Biotechnol. Biochem., 7, 90 (2012)
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Helenius A, Simons K, Biochim. Biophys. Acta, 415, 29 (1975)
Galabova D, Tuleva B, Spasova D, Enzyme Microb. Technol., 18(1), 18 (1996)
Harrison ST, Chase HA, Dennis JS, Biotechnol. Tech., 5, 115 (1991)
Zhao FS, Yu JY, Biotechnol. Prog., 17(3), 490 (2001)
Lovitt RW, Jones M, Collins SE, Coss GM, Yau CP, Attouch C, Process Biochem., 36(5), 415 (2000)
Feril LB, Kondo T, Ultrason. Sonochem., 12, 353 (2005)
Lee KJ, Row KH, Korean J. Chem. Eng., 23(5), 779 (2006)
Gogate PR, Kabadi AM, Biochem. Eng. J., 44, 60 (2009)
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Yaldagard M, Mortazavi SA, Tabatabaie F, Korean J. Chem. Eng., 25(3), 517 (2008)
Pchelintsev NA, Adams PD, Nelson DM, PLoS One, 11, 1 (2016)
