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Optimization of Protease Production from Wild and Mutant Strains of Aspergillus sp. under Submerged Fermentation


Affiliations
1 Department of Bioscience and Biotechnology, Banasthali University, Rajasthan, India
2 Department of Biochemical Engineering, Bipin Tripathi Kumaon Institute of Technology, Dwarahat, Uttrakhand, India
 

Proteases are one of the most significant groups of commercial enzymes and contribute 60% of the world enzyme market. The choice of proteases is the microbial proteases due to their versatility, stability and distinctive properties. Today, microbial proteases are utilized in various industries viz., meat processing, ripening of cheese, detergents, textile, recovery of silver from photographic image etc. Therefore, the present study was undertaken to increase the protease production from wild and mutagenic strain of Aspergillus sp. Wild and mutagenic strain of proteolytic soil fungus Aspergillus sp. was used for optimization study. Different parameters (nitrogen, carbon sources, temperature, pH and incubation time) were optimized in submerged fermentation (SmF) for enhanced protease production. Wild strain demonstrated highest protease activity at pH 10.0 after 48 h of incubation at 37 °C in the medium containing glucose as carbon source and yeast extract as nitrogen source whereas optimum protease activity from mutagenic strain was found at pH 10.0 after 94 h of incubation at 37 °C in the medium containing fructose as carbon source and peptone as nitrogen source. Protease production was increased from wild and mutagenic strain of Aspergillus sp. after parameters optimization in SmF.

Keywords

Optimization, Protease Activity, Aspergillus sp., Carbon Source, Temperature, pH.
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  • Negi, S. and Banerjee, R (2006) Optimization of amylase and protease production from Aspergillus awamori in single bioreactor through EVOP factorial design technique. Food Technol Biotechnol. 44, 257-261.
  • Rani, K., Rana, R. and Datt, S (2012) Review on latest overview of proteases. Int J Curr Life Sci 2, 12-18.
  • Rocha, MV., Romanini, D., Nerli, BB. and Tubio, G (2012) Pancreatic serine protease extraction by affinity partition using a free triazine dye. Int J Biol Macromol. 50, 303-309.
  • Gupta, R., Beg, QK. and Lorenz, P (2002) Bacterial alkaline proteases: molecular approaches and industrial applications. Appl Microbiol Biotechnol. 59:15-32.
  • Rao, MB., Tanksale, AM., Ghatge, MS. and Deshpande, VV (1998) Molecular and biotechnological aspects of microbial proteases. Microbiol Mol Biol Rev. 62, 597-635.
  • Nirmal, NP., Shankar, S. and Laxman, RS (2011) Fungal proteases: an overview. Int J Biotech Biosci. 1, 1-40.
  • Laxman, RS., Sonawane, AP., More, SV., Rao, BS., Rele, MV., Jogdand, VV., Deshpande, VV. and Rao, MB (2005) Optimization and scale up of production of alkaline protease from Conidiobolus coronatus. Process Biochem. 40, 3152-3158.
  • Shankar, S., Rao, M. and Laxman, SR (2011) Purification and characterization of an alkaline protease by a new strain of Beauveria sp. Process Biochem. 46, 579-585.
  • Wu, TY., Mohammad, AW., Jahim, JM. and Anuar, N (2006) Investigations on protease production by a wild-type Aspergillus terreus strain using diluted retentate of pre-filtered palm oil mill effluent (POME) as substrate. Enzyme Microb Tech. 39, 1223-1229.
  • Farley, PC. and Ikasari, L (1992) Regulation of the secretion of Rhizopus Oligosporus extracellular carboxyl proteinase. J Gen Microbiol. 138, 2539-2544.
  • Fan-Ching, Y. and Lin, IH (1998) Production of acid protease using thin stillage from a rice-spirit distillery by Aspergillus niger. Enzyme Microb Technol. 23, 397-402.
  • Chrzanowska, J., Kolaczkowska, M. and Polanowski, A (1993) Production of exocellular proteolytic enzymes by various species of Penicillium. Enzyme Microb Technol. 15, 140-143.
  • Aleksieva, P. and Peeva, L (2000) Investigation of acid proteinase biosynthesis by the fungus Humicola lutea 120-5 in an airlift bioreactor. Enzyme Microb Technol. 26, 402-405.
  • Lasure, LL (1980) Regulation of extracellular acid protease in Mucor miehei. Mycologia, 72, 483-493.
  • Rao, MB., Tanksale, AM., Ghatge, MS. and Deshpande, VV (1998) Molecular and biotechnological aspects of microbial proteases. Microbiol Mol Biol Rev. 62, 597-635.
  • Tsuchida, O., Yamagota, Y., Ishizuka, J., Arai, J., Yamada, J., Takeuchi, M. and Ichishima, E (1986) An alkaline protease of an alkalophilic Bacillus sp. Curr Microbiol. 14, 7-12.
  • Rajput, K., Chanyal, S. and Agrawal, PK. Optimization of protease production by endophytic fungus, Alternaria alternata isolated from gymnosperm tree- cupressus torulosa d.don. World J Pharma Pharm Sci. 5, 1034-1054, 2016.
  • Srinubabu, G., Lokeswari, N. and Jayaraju, K (2007) Screening of Nutritional Parameters for the Production of Protease from Aspergillus Oryzae. E-Journal of Chemistry. 4, 208-215.
  • Venkat Kumar, S., Rao, A. and Nazareth, JR (2015) Screening, media optimization and partial purification of protease by Trichosporon japonicum vitvk1. International Journal of Pharmacy and Pharmaceutical Sciences. 7, 187-191.
  • Muthukrishnan, S. and Mukilarasi, K (2016) Industrial Important Protease Screening and Optimization from Micro-Fungal Isoltaes of Ayyanar Falls Forest Samples, Rajapalalyam. World Appl Sci J. 34, 343-347.
  • Sharma, AK., Sharma, V., Saxena, J., Yadav, B., Alam, A. and Prakash, A. (2015) Effect of Culture Conditions on Protease Production and Activity of Protease from Soil Borne Fungi. International Journal of Scientific Research in Environmental Science. 3, 0411-0419.
  • Zaferanloo, B., Quang, TD., Daumoo, S., Ghorbani, MM. and Palombo, EA (2014) Optimization of protease production by endophytic fungus, Alternaria alternata, isolated from an Australian native plant. World J Microbiol Biotechnol. 30, 1755-1762.
  • Milala, MA., Jatau, IA. and Abdulrahman, AA (2016) Production and Optimization of Protease from Aspergillus niger and Bacillus subtilis using Response Surface Methodology. IOSR J Biotechnol Biochem. 2, 01-07.

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  • Optimization of Protease Production from Wild and Mutant Strains of Aspergillus sp. under Submerged Fermentation

Abstract Views: 526  |  PDF Views: 163

Authors

Arun Kumar Sharma
Department of Bioscience and Biotechnology, Banasthali University, Rajasthan, India
Shreya Negi
Department of Bioscience and Biotechnology, Banasthali University, Rajasthan, India
Vinay Sharma
Department of Bioscience and Biotechnology, Banasthali University, Rajasthan, India
Jyoti Saxena
Department of Biochemical Engineering, Bipin Tripathi Kumaon Institute of Technology, Dwarahat, Uttrakhand, India

Abstract


Proteases are one of the most significant groups of commercial enzymes and contribute 60% of the world enzyme market. The choice of proteases is the microbial proteases due to their versatility, stability and distinctive properties. Today, microbial proteases are utilized in various industries viz., meat processing, ripening of cheese, detergents, textile, recovery of silver from photographic image etc. Therefore, the present study was undertaken to increase the protease production from wild and mutagenic strain of Aspergillus sp. Wild and mutagenic strain of proteolytic soil fungus Aspergillus sp. was used for optimization study. Different parameters (nitrogen, carbon sources, temperature, pH and incubation time) were optimized in submerged fermentation (SmF) for enhanced protease production. Wild strain demonstrated highest protease activity at pH 10.0 after 48 h of incubation at 37 °C in the medium containing glucose as carbon source and yeast extract as nitrogen source whereas optimum protease activity from mutagenic strain was found at pH 10.0 after 94 h of incubation at 37 °C in the medium containing fructose as carbon source and peptone as nitrogen source. Protease production was increased from wild and mutagenic strain of Aspergillus sp. after parameters optimization in SmF.

Keywords


Optimization, Protease Activity, Aspergillus sp., Carbon Source, Temperature, pH.

References