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Experimental Investigations on the Effects of Carbon and Nitrogen Sources on Concomitant Amylase and Polygalacturonase Production by Trichoderma viride BITRS-1001 in Submerged Fermentation

DOI: 10.1155/2012/904763

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Abstract:

The paper investigates the effects of different commercial carbon and nitrogen sources on the concomitant synthesis of amylase and polygalacturonase enzymes with the aim of optimizing them for maximal enzyme production. The microorganism used in this work was the fungus Trichoderma viride BITRS-1001, which had been previously identified as a highly active producer of amylase and polygalacturonase enzymes. The results showed that the different commercial carbon and nitrogen substrate significantly affected the concomitant syntheses of amylase and polygalacturonase in culture media supplemented with the different commercial carbon and nitrogen substrates. The result obtained suggested that for optimal and concomitant synthesis of the enzymes by Trichoderma viride BITRS-1001 in submerged fermentation, minimal medium supplemented with maltose and casein were the carbon and nitrogen substrates of choice. 1. Introduction Microbes are rich sources of enzymes [1]. In nature, they have been endowed with vast potentials to produce array of enzymes, which have been exploited commercially over the years. Traditionally, enzymes have been extracted from plants and animals. However, microbial enzymes have formed the basis of commercial enzyme production. In recent years, the potential of using microorganisms as biotechnological sources of industrially relevant enzymes has stimulated interest in the exploration of extracellular enzymatic activity in several microorganisms isolated from different environments owing to several reasons [2–7]. Amylase (EC 3.2.1.1) and polygalacturonase (EC 3.2.1.15) from microbial origin have high biotechnological interest such as in the processing of foods, manufacturing of detergents, textiles, pharmaceutical products, medical therapy, in molecular biology, and in many industrial processes as reviewed in [4, 6, 8–22]. While amylase has been reported to have approximately 25% of the enzyme market of industrial enzymes [17, 23, 24], microbial pectinases have been reported to account for 25% of the global food enzymes sales [4]. The synthesis of these enzymes by microorganisms has been reported to be highly influenced by factors such as carbon sources, temperature, pH, and operating parameter such as incubation time in submerged culture [25, 26]. Factors like carbon, nitrogen sources and their concentrations have always been of great interest to researchers in the industry for the low-cost media design. It is also known that 30–40% of the production cost of industrial enzymes is estimated to be the cost of growth medium. Therefore, it is of

References

[1]  I. Akpan, “Screening for novel fungal biocatalysts,” Nigerian Journal of Microbiology, vol. 18, pp. 288–292, 2004.
[2]  F. A. Akinyosoye, A. H. Adeniran, and G. Oboh, “Production of fungal amylase from agro-industrial wastes,” in Proceedings of the 16th Annual Conference of Biotechnological Society of Nigeria, pp. 35–40, 2003.
[3]  M. H. Alves, G. M. Campos-Takaki, F. A. L. Porto, and I. A. Milanez, “Screening of Mucor spp. for the production of amylase, lipase, polygalacturonase and protease,” Brazilian Journal of Microbiology, vol. 33, no. 4, pp. 325–330, 2002.
[4]  R. S. Jayani, S. Saxena, and R. Gupta, “Microbial pectinolytic enzymes: a review,” Process Biochemistry, vol. 40, no. 9, pp. 2931–2944, 2005.
[5]  I. O. Onyeocha and C. I. C. Ogbonna, “Extracellular enzyme production: a quick qualitative assay method,” Nigerian Journal of Biotechnology, vol. 1, pp. 48–59, 1983.
[6]  S. Alva, J. Anupama, J. Savla et al., “Production and characterization of fungal amylase enzyme isolated from Aspergillus sp. JGI 12 in solid state culture,” African Journal of Biotechnology, vol. 6, no. 5, pp. 576–581, 2007.
[7]  J. D. G. Vieira, E. C. Barbosa, and A. J. I. Garrim, “Enzymatic activity of endophytic bacterial isolates of Jacaranda decurrens Cham. (Carobinha-do-campo),” Brazilian Archives of Biology and Technology, vol. 49, no. 3, pp. 353–359, 2006.
[8]  V. P. Aiyer, “Amylases and their applications,” African Journal of Biotechnology, vol. 4, no. 13, pp. 1525–1529, 2005.
[9]  T. Akhilesh, R. Pahwa, S. Singh, and R. Gupta, “Production, purification, and characterization of polygalacturonase from Mucorcircinelloides ITCC 6025,” Enzyme Research, vol. 2010, Article ID 170549, 7 pages, 2010.
[10]  P. Blanco, C. Sieiro, and T. G. Villa, “Production of pectic enzymes in yeasts,” FEMS Microbiology Letters, vol. 175, no. 1, pp. 1–9, 1999.
[11]  M. F. Gailing, A. Guibert, and D. Combes, “Fractional factorial designs applied to enzymatic sugar beet pulps pressing improvement,” Bioprocess Engineering, vol. 22, no. 1, pp. 69–74, 2000.
[12]  R. Gupta, P. Gigras, H. Mohapatra, V. K. Goswami, and B. Chauhan, “Microbial α-amylases: a biotechnological perspective,” Process Biochemistry, vol. 38, no. 11, pp. 1599–1616, 2003.
[13]  G. Kaur, S. Kumar, and T. Satyanarayana, “Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile apinis,” Bioresource Technology, vol. 94, no. 3, pp. 239–243, 2004.
[14]  K. Mojsov, “Experimental investigations of submerged fermentation and synthesis of pectinolytic enzymes by aspergillusniger: effect of inoculum size and old of spores,” Applied Technologies & Innovations, vol. 2, no. 2, pp. 40–46, 2010.
[15]  A. Pandey, P. Nigam, C. R. Soccol, V. T. Soccol, D. Singh, and R. Mohan, “Advances in microbial amylases,” Biotechnology and Applied Biochemistry, vol. 31, no. 2, pp. 135–152, 2000.
[16]  D. B. Pedrolli, A. C. Monteiro, E. Gomes, and E. C. Carmona, “Pectin and pectinases: production, characterization and industrial application of microbial pectinolytic enzymes,” Open Biotechnology Journal, vol. 3, pp. 9–18, 2009.
[17]  M. B. Rao, A. M. Tanksale, M. S. Gathge, and V. V. Deshpande, “Molecular and biotechnological aspects of microbial proteases,” Microbiology and Molecular Biology Reviews, vol. 62, no. 3, pp. 597–635, 1998.
[18]  I. Revilla and M. L. Gonzalez-San Jose, “Addition of pectolytic enzymes: an enological practice which improves the chromaticity and stability of red wines,” International Journal of Food Science and Technology, vol. 38, no. 1, pp. 29–36, 2003.
[19]  E. R. Riegal, H. G. Bissinger, et al., “Industrial fermentation: principles, processes and products,” in Riegal's Handbook of Industrial Chemistry, J. A. Kent, Ed., pp. 963–1045, Kluwer Academic/Plenum Publishers, New York, NY, USA, 2003.
[20]  S. Sivaramakrishnan, D. Gangadharan, K. M. Nampoothiri, C. R. Soccol, and A. Pandey, “α-Amylases from microbial sources—an overview on recent developments,” Food Technology and Biotechnology, vol. 44, no. 2, pp. 173–184, 2006.
[21]  K. L. Tiwari, S. K. Jadhav, and A. Fatima, “Culturecondition for the production of thermostable amylase by Penicillumrugulosum,” Global Journal of Biotechnology and Biochemistry, vol. 2, no. 1, pp. 21–24, 2007.
[22]  M. J. E. C. Van Der Maarel, B. Van Der Veen, J. C. M. Uitdehaag, H. Leemhuis, and L. Dijkhuizen, “Properties and applications of starch-converting enzymes of the α-amylase family,” Journal of Biotechnology, vol. 94, no. 2, pp. 137–155, 2002.
[23]  G. S. Sidhu, P. Sharma, T. Chakrabarti, and J. K. Gupta, “Strain improvement for the production of a thermostable α-amylase,” Enzyme and Microbial Technology, vol. 21, no. 7, pp. 525–530, 1997.
[24]  S. Sudharhsan, S. Senthilkumar, and K. Ranjith, “Physical and nutritional factors affecting the production of amylase from species of bacillus isolated from spoiled food waste,” African Journal of Biotechnology, vol. 6, no. 4, pp. 430–435, 2007.
[25]  N. Jacob and P. Prema, “Influence of mode of fermentation on production of polygalacturonase by a novel strain of Streptomyces lydicus,” Food Technology and Biotechnology, vol. 44, no. 2, pp. 263–267, 2006.
[26]  M. Palaniyappan, V. Vijayagopal, V. Renukal, R. Viswanathan, and T. Viruthagiri, “Screening of natural substrates and optimization of operating variables on the production of pectinase by submerged fermentation using Aspergillus niger MTCC 281,” African Journal of Biotechnology, vol. 8, no. 4, pp. 682–686, 2009.
[27]  S. Negi and R. Banerjee, “Optimization of culture parameters to enhance production of amylase and protease from Aspergillusawamori in a single fermentation,” African Journal of Biochemistry Research, vol. 4, no. 3, pp. 73–80, 2010.
[28]  D. J. Arotupin and F. E. Ogunmolu, “Effect of carbon and nitrogen sources on polygalacturonase production by TrichodermaViride (BITRS-1001) isolated from tar sand in Ondo State Nigeria,” Malaysian Journal of Microbiology, vol. 7, no. 3, pp. 164–169, 2011.
[29]  D. J. Arotupin, Microbiology and pectinase activity of fungi associated with soils cultivated with different crops [Ph.D. thesis], F.U.T., Akure, Nigeria, 2007.
[30]  G. Narasimha, A. Sridevi, V. Buddolla, M. Subhosh Chandra, and B. Rajasekhar Reddy, “Nutrient effects on production of cellulolytic enzymes by Aspergillus niger,” African Journal of Biotechnology, vol. 5, no. 5, pp. 472–476, 2006.
[31]  D. J. Arotupin and F. E. Ogunmolu, “Screening of fungal isolates from Nigerian tar sand deposit in Ondo state for novel biocatalysts,” Journal of Biological Sciences, vol. 12, no. 1, pp. 57–61, 2012.
[32]  D. P. S. T. G. Attanayaka, S. N. T. De Silva, S. R. Nirosha, and A. M. W. S. Aththanayaka, “Isolation of raw starch hydrolysing fungi and purification of a-amylase from Geotrichum candidum CMSS06,” Journal of the National Science Foundation of Sri Lanka, vol. 37, no. 2, pp. 93–98, 2009.
[33]  B. J. Akinyele and F. C. Adetuyi, “Effect of agrowastes, pH and temperature variation on the growth of Volvariellavolvacea,” African Journal of Biotechnology, vol. 4, no. 12, pp. 1390–1395, 2005.
[34]  E. Moore-Landecker, Fundamentals of Fungi, Prentice Hall, Upper Saddle River, NJ, USA, 4th edition, 1996.
[35]  F. A. Akinyosoye and J. A. Akinyanju, “Effects of different carbon sources on the growth and sporulation of Geotrichumcandidum,” Nigerian Journal of Botany, vol. 2, pp. 85–95, 1989.
[36]  D. J. Arotupin, “Evaluation of microorganisms from cassava waste water for production of amylase and cellulase,” Research Journal of Microbiology, vol. 2, no. 5, pp. 475–480, 2007.
[37]  D. H. Griffin, Fungi Physiology, A Wiley-Interscience, 2nd edition, 1994.
[38]  B. L. Turner, “Variation in the optimum pH enzyme activities in tropical rain forest soils,” Applied Environmental Microbiology, vol. 76, no. 19, pp. 6485–6493, 2010.
[39]  E. Nahas and M. M. Waldemarin, “Control of amylase production and growth characteristics of Aspergillus ochraceus,” Latin American Journal of Microbiology, vol. 44, no. 1, pp. 5–10, 2002.
[40]  K. J. P. Narayana and M. Vijayalakshmi, “Production of extracellular α-amylase by Streptomyces albidoflavus,” Asian Journal of Biochemistry, vol. 3, no. 3, pp. 194–197, 2008.
[41]  A. Sasi, M. Kani, A. Panneerselvam, G. Jegadeesh, K. Muthu, and R. M. Kumar, “Optimizing the conditions of α-amylase by an Esturian strain of Aspergillus spp,” African Journal of Microbiology Research, vol. 4, no. 8, pp. 581–586, 2010.
[42]  E. Favela-Torres, T. Volke-Sepúlveda, and G. Viniegra-González, “Production of hydrolytic depolymerising pectinases,” Food Technology and Biotechnology, vol. 44, no. 2, pp. 221–227, 2006.
[43]  H. Vahidi, F. Kobarfard, and F. Namjoyan, “Effect of cultivation conditions on growth and antifungal activity of Mycena leptocephala,” African Journal of Biotechnology, vol. 3, no. 11, pp. 606–609, 2004.

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