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Received August 2, 2009
Accepted October 8, 2009
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Optimization of the fermentation conditions and partial characterization for acido-thermophilic α-amylase from Aspergillus niger NCIM 548
School of Chemical Engineering, Noushirvani University of Technology, Babol, Iran
najafpour@nit.ac.ir
Korean Journal of Chemical Engineering, March 2010, 27(3), 919-924(6), 10.1007/s11814-010-0138-2
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Abstract
A high performance thermostable α-amylase at low pH values has been synthesized. Sugarcane bagasse was hydrolyzed in a dilute acid solution and utilized as carbon source for the growth of Aspergillus niger strain NCIM 548. Glucose, xylose and arabinose with the ratio of 1.0 : 0.9 : 0.3 (w/w/w) were detected in the hydrolyzate by HPLC analysis. Optimization of the fermentation conditions for α-amylase production was performed by varying four influential parameters such as Sugarcane bagasse hydrolyzate (SBH), NH4Cl, pH and incubation time using a central composite design (CCD) under response surface methodology (RSM). The optimum values of SBH, NH4Cl, pH and incubation time were 20.49, 2.34 g/l, 5.65 and 76.67 h, respectively. The acido-thermophilic enzyme showed maximum stability at 70 ℃ and pH value of 4. The rate constant, K(m) and maximum reaction rate, V(max) were 18.79 g/l and 15.85 g/l·min, respectively.
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References
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Najafpour GD, Biochemical Engineering and Biotechnology, Elsevier, Amsterdam (2007)
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Pandey A, Nigam P, Soccol CR, Soccol VT, Sing D, Mohan R, Biotechnol. Appl. Biochem., 31, 135 (2000)
Kandra L, J. Mol. Struct., 666-667, 487 (2003)
Leveque E, Janecek S, Haye B, Belarbi A, Enzyme Microb. Technol., 26(1), 3 (2000)
Najafpour GD, Shan CP, Bioresour. Technol., 86(1), 91 (2003)
Mitidieri S, Martinelli AHS, Schrank A, Vainstein MH, Bioresour. Technol., 97(10), 1217 (2006)
Konsula Z, Liakopoulou-Kyriakides M, Process Biochem., 39, 1745 (2004)
Asgher M, Asad MJ, Rahman SU, Legge RL, J. Food Eng., 79, 950 (2007)
Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B, Process Biochem., 38, 1599 (2003)
Baysal Z, Uyar F, Aytekin C, Process Biochem., 38, 1665 (2003)
Tanyildizi MS, Ozer D, Elibol M, Biochem. Eng. J., 37, 294 (2007)
Francis F, Sabu A, Nampoothiri KM, Ramachandran S, Ghosh S, Szakacs G, Pandey A, Biochem. Eng. J., 15, 107 (2003)
Sajedi RH, Naderi-Manesh H, Khajeh K, Ahmadvand R, Ranjbar BA, Asoodeh A, Moradian F, Enzyme Microb. Technol., 36(5-6), 666 (2005)
Pandey A, Soccol CR, Nigam P, Soccol VT, Bioresour. Technol., 74(1), 69 (2000)
Khosravi-Darani K, Zoghi A, Bioresour. Technol., 99, 6986 (2008)
Kuo CH, Lee CK, Bioresour. Technol., 100, 866 (2009)
Zhao XB, Peng F, Cheng K, Liu DH, Enzyme Microb. Technol., 44(1), 17 (2009)
Dey G, Mitra A, Banerjee R, Maiti BR, Biochem. Eng. J., 7, 227 (2001)
Miller GL, Anal. Chem., 31, 426 (1959)
Ba D, Boyaci H, J. Food Eng., 78, 836 (2007)
Gangadharan D, Sivaramakrishnan S, Nampoothiri KM, Sukumaran RK, Pandey A, Bioresour. Technol., 99, 4597 (2008)
Barrington S, Kim JW, Bioresour. Technol., 99(2), 368 (2008)
Lotfy WA, Ghanem KM, El-Helow ER, Bioresour. Technol., 98(18), 3464 (2007)
