A Statistical Approach for Production of Pectinase through Optimization of Process Factors Using Mutant Strain of Bacillus subtilis
DOI:
https://doi.org/10.48165/Keywords:
Taguchi methodology, optimization, pectinase, mutant, process factorsAbstract
The optimization of the various process parameters including nutritional and physiochemical factors was carried out for production of pectinase using from mutant strain of Bacillus subtilis using Taguchi methodology. In the entire optimization study, mutant UV-20- 11/NTG-1-5/EMS-1-2 was used. The experimental work was performed using shake flask experiments. In this study, ten factors including, orange peel, ammonium sulfate, magnesium sulfate, phosphate ion, sodium chloride, inoculum percentage, temperature, pH, agitation speed, and incubation time were considered for their effect on pectinase production. It was evident from Taguchi methodology that agitation speed contributed the maximum impact (26.51%) on pectinase productivity followed by ammonium sulfate (13.77%), incubation time (12.77%), temperature (12.36%), pH (V%), orange peel (9.64%), inoculum percentage (5.61%), and sodium chloride (5.467%). The results showed that a higher level of pectinase productivity (630.58 U) was achieved with orange peel (5 g/L), ammonium sulfate (1.5 g/L), magnesium sulfate (0.5 g/L), phosphate ion (0.5 g/L), sodium chloride (0.5 g/L), inoculum percentage (1%), temperature (37oC), pH (7), agitation speed (140 rpm), and incubation time (96 h).
Downloads
References
Bhunia, B., Basak, B., Bhattacharya, P., Dey, A. 2012. Kinetic studies of alkaline protease from Bacillus licheniformis NCIM-2042. J Microbiol Biotechnol, 22(12), 1758-66.
Bhunia, B., Basak, B., Bhattacharya, P., Dey, A. 2013. Process engineering studies to investigate the effect of temperature and pH on kinetic parameters of alkaline protease production. Journal of bioscience and bioengineering, 115(1), 86-89.
Bhunia, B., Dutta, D., Chaudhuri, S. 2011. Extracellular alkaline protease from Bacillus licheniformis NCIM-2042: Improving enzyme activity assay and characterization. Engineering in Life Sciences, 11(2), 207-215.
Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem, 72, 248-54. 5. Çalik, P., Bilir, E., Çalik, G., Özdamar, T.H. 2003. Bioreactor operation parameters as tools for metabolic regulations in fermentation processes: influence of pH conditions. Chemical Engineering Science, 58(3-6), 759-766.
Dehnad, K. 1989. Quality control, robust design, and the Taguchi method. Pacific Grove, CA: Wadsworth and Brooks.
Dixon, M., Webb, E.C. 1979. Enzymes. 3rd ed. Academic Press, New York. 8. Dutta, S., Basak, B., Bhunia, B., Sinha, A., Dey, A. 2017. Approaches towards the enhanced production of Rapamycin by Streptomyces hygroscopicus MTCC 4003 through mutagenesis and optimization of process parameters by Taguchi orthogonal array methodology. World Journal of Microbiology and Biotechnology, 33(5), 90.
Kaur, G., Kumar, S., Satyanarayana, T. 2004. Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile Apinis. Bioresour Technol, 94(3), 239-43.
Kumar, A., Bhunia, B., Dasgupta, D., Mandal, T., Dey, A., Datta, S., Bhattacharya, P. 2013. Optimization of culture condition for growth and phenol degradation by Alcaligenes faecalis JF339228 using Taguchi Methodology. Desalination and Water Treatment, 51(16-18), 3153-3163.
Mitra, A. 1998. Fundamentals of Quality Control and Improvement. Pearson Educational Asia, Delhi.
Nakagawa, T., Yamada, K., Miyaji, T., Tomizuka, N. 2002. Cold-active pectinolytic activity of psychrophilic-basidiomycetous yeast Cystofilobasidium capitatum strain PPY-1. J Biosci Bioeng, 94(2), 175-7.
Rüdiger, A., Ogbonna, J.C., Märkl, H., Antranikian, G. 1992. Effect of gassing, agitation, substrate supplementation and dialysis on the growth of an extremely thermophilic archaeon Pyrococcus woesei. Applied microbiology and biotechnology, 37(4), 501-504.
Sadana, A., Henley, J.P. 1988. Influence of pH on enzyme stabilization:an analysis using a series-type mechanism. Journal of Biotechnology, 7, 95-112.
Sode, K., Ito, K., Witarto, A.B., Watanabe, K., Yoshida, H., Postma, P. 1996. Increased production of recombinant pyrroloquinoline quinone (PQQ) glucose dehydrogenase by metabolically
engineered Escherichia coli strain capable of PQQ biosynthesis. J Biotechnol, 49(1-3), 239-43.
Taguchi, G. 1986. Introduction to Quality Engineering. Asian Productivity Organization. American supplier institute Inc., Dearborn, MI.
Tanford, C. 1968. Protein denaturation. Adv Prot Chem, 23, 121-282.
Tong, L., Wang, C., Chen, C., Chen, C. 2004. Dynamic multiple responses by ideal solution analysis. Euro J Operational Res, 156, 433–444.
Uday, U.S.P., Goswami, S., Gopikrishna, K., Bandyopadhyay, T.K., Bhunia, B. 2018. Identification of markers at various stages of batch fermentation and improved production of xylanase using Aspergillus niger (KP874102. 1). 3 Biotech, 8(8), 337.
Yadav, P., Garg, N., Kumar, S. 2015. Improved shelf stability of mulberry juice by combination of preservatives. Indian Journal of Natural Products and Resources (IJNPR)[Formerly Natural Product Radiance (NPR)], 5(1), 62-66.
Ying-xian, Y. 2005. The Status Quo and Strategy of Hemp Bast Degumming. Shandong Textile Science & Technology, 1, 51-54.
Zhou, J., Wu, D., Guo, D. 2010. Optimization of the production of thiocarbohydrazide using the Taguchi method. J Chem Technol Biotechnol, 85, 1402-1406.
