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Received June 3, 2021
Accepted September 26, 2021
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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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Optimization of protease production process using bran wasteusing Bacillus licheniformis
Faculty of Chemical Engineering, Babol Noshirvani University of Technology, Iran
Korean Journal of Chemical Engineering, March 2022, 39(3), 674-683(10), 10.1007/s11814-021-0965-3
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Abstract
Protease enzyme production by Bacillus licheniformis bacteria was investigated. Various agricultural wastes as substrate such as wheat bran, rice bran, and sugarcane bagasse were considered. The most important effective parameters on enzyme production, like incubation time, various substrates and solid substrate particle size, media pH, different nitrogen sources in a bench-scale designed bioreactor, were optimized. The optimum protease production conditions, for both Erlenmeyer flask and batch bioreactor, at 37°C, pH of 8, incubation time of 48h, wheat bran (5 wt%) with the particle size of 1mm, an equal amount of peptone and yeast extract (1% w/w) and agitation rate of_x000D_
180 rpm were defined. In addition, maximum protease activity in the Erlenmeyer flask and batch bioreactor was 596 and 683.93U/mL, respectively. The pH and thermal stability of produced protease were studied; the highest amount of remaining activities at pH 8 and 60°C were 97 and 63% of initial activities, respectively. Also, shelf-life of the produced protease enzyme retained up to 88% of its initial activity after 30 days of storage at 4°C. However, the produced enzyme was exposed remarkably compatible with the commercial detergent; the enzyme perfectly washed and removed the stains from the sample cotton textile.
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Singh S, Bajaj BK, Waste Biomass Valorization, 8, 453 (2017)
Potumarthi R, Ch S, Jetty A, Biochem. Eng. J., 34, 185 (2007)
Banerjee UC, Sani RK, Azmi W, Soni R, Process Biochem., 35, 213 (1999)
Bergkvist R, Acta Chem. Scand., 17, 8 (1963)
Bashir F, Asgher M, Hussain F, Randhawa MA, Int. J. Biol. Macromol., 113, 944 (2018)
Bradford MM, Anal. Biochem., 72, 248 (1976)
Sellami-Kamoun A, Haddar A, Ali NEH, Ghorbel-Frikha B, Kanoun S, Nasri M, Microbiol. Res., 163, 299 (2008)
Yang JK, Shih L, Tzeng YM, Wang SL, Enzyme Microb. Technol., 26, 406 (2000)
Deb P, Talukdar SA, Mohsina K, Sarker PK, Sayem SA, Springerplus, 2, 1 (2013)
Olajuyigbe FM, Ajele JO, Afr. J. Biochem. Res., 2, 206 (2008)
Ahmed I, Zia MA, Iftikhar T, Iqbal HM, BioResources, 6, 4505 (2011)
Uyar F, Baysal Z, Process Biochem., 39, 1893 (2004)
Sharan A, Darmwal NS, Bioresour. Technol., 98, 881 (2007)
Mukhtar H, Haq I, Sci. World J., 2013 (2013)
Sumantha A, Deepa P, Sandhya C, Szakacs G, Soccol CR, Pandey A, Braz. Arch. Biol. Technol., 49, 843 (2006)
Abd Rahman RNZR, Geok LP, Basri M, Salleh AB, Enzyme Microb. Technol., 36, 749 (2005)
Gilani S, Najafpour G, Heydarzadeh H, Zare H, Chem. Ind. Chem. Eng. Q., 17, 179 (2011)
Jellouli K, Ghorbel-Bellaaj O, Ayed HB, Manni L, Agrebi R, Nasri M, Process Biochem., 46, 1248 (2011)
Haddar A, Agrebi R, Bougatef A, Hmidet N, Sellami-Kamoun A, Nasri M, Bioresour. Technol., 100, 3366 (2009)
Abidi F, Limam F, Nejib MM, Process Biochem., 43, 1202 (2008)
