أمثلة Determining Optimum Conditions for production of xylanase From Trichoderma viride Using Response Surface Methodology
الملخص
The xylanase is one of the enzymes that is characterized by various industrial applications, the most important of which are biofuels, feed, food industries, and paper. In this study, the optimal conditions for the production of xylanase by (Trichoderma viride) using response surface methodology, using an agricultural weed, (Prosopis juliflora), A Central Composite Design was used to investigate the effects of four independent variables: pH, concentration pods (w/v %), concentration sucrose(%),concentration yeast extract(%), on the response factor, xylanase activity (UI/mL), The independent variables were at three levels and their actual values selected on the basis of preliminary experimental results. A second-order polynomial model was used for predicting the response.
Regression analysis showed that the variation was explained by the model. The optimal conditions for xylanase activity were found to be pH=6.5, concentration pods 4.6 (w/v %), concentration sucrose 0.3(%),concentration yeast extract 0.4(%), Under the optimum conditions the corresponding predicted response value for xylanase activity was 122.9 UI/mL.
The good agreement between predicted and experimental values indicated suitability of the model employed and the success of response surface methodology in optimizing the xylanase activity.
References
• Anwar, Z., Gulfraz, M., and Irashad, M., (2014). Agro industrial lignocellulosic biomass a key to unlock the future bio- energy. A brief review J. Rad. Appl. 7 (2): 163–173.
• Battan, B., Sharma, J. K., and Dhiman, S. S., (2006). High level xylanase production by alkalophilic B. pumilus ASH under solid state fermentation. World Journal of Microbiology & Biotechnology, 22: 1281-1287.
• Buthelezi,S.P,,Olaniran,A.O.,Pillaay,B.,(2011) Sawdust and digestive bran as cheap alternative substrates for xylanase production. African journal microbial.5(7):742-752.
• Carmona, E. C., Fialho, M. B., and Buchgnani, E. B., (2005). Production, purification & characterization of a minor form of xylanase from A. versicolor. Process Biochemistry, 40: 359-364.
• Collins, T., Gerday, C., and Feller, G., (2005). Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiology Reviews. 29(1):3-23.
• Fortkamp,D&Knob,A.,(2014).High xylanase production by Trichoderma viride using pineapple peel as substrate and its application in pulp biobleaching. African journal of biotechnology.13(22):2248-2259.
• Goyal, M., Kalra, K. L., and Sareen, V. K., (2008). Xylanase production with xylan rich lignocellulosic wastes by a local soil isolate of T. viride. Brazilian Journal of Microbiology. 39: 535-541.
• Hoda,M.S.,Abdel-dayem,A.S., and Arafatbel,T., (2012). Production of xylanase by Aspergillus niger and Trichoderma viride using some agriculture residues. International journal of Agriculture Research.7(1):746-757.
• Holker, U., & Jurgen, A., (2005). Solid-state fermentation-are there any biotechnological advantages. Current Opinion in Microbiology. 8:301-306.
• Irfan,M., Nadeem,M., and Syed,Q.,(2014) One-factor-at-a-time (OFAT) optimization of xylanase production from Trichoderma viride-IR05 in solid-state fermentation. Journal of Radiation Research and Applied Sciences. 7:317-326.
• Jampala,P.,Tadikamalla,S.,Preethi,M.,Ramanujam,S.,and Uppuluri,K.B., (2017). Concurrent production of cellulose and exylanase from Trichoderma reesei NCIM 1186:enhancement of production by desirability-based multi-objective method.Biotech.3:7-14.
• Jun, H., Kieselbach ,T.,and Jonsson, L.J .,(2011) Enzyme production by filamentous fungi: analysis of the secretome of Trichoderma reesei grown on unconventional carbon source. Microbial Cell Factor. 10(1):1-10.
• Juturu,V&Wu,J.C., (2012). Microbial xylanases:Engineering ,production and industrial applications.Biotechnol Adv.30:1219-1227.
• Kanaga ,K., Pandey ,A., and Kumar, S., (2016) Multi-objective optimization of media nutrients for enhanced production of algae biomass and fatty acid biosynthesis from Chlorella pyrenoidosa NCIM 2738. Bioresour Technol. 200:940–950.
• Latif, F., Asgher, M., Saleem, R., Akram, A., and Legge, R., (2006). Purification and characterization of xylanase produced by C.thermophile NIBGE. World Journal of Microbiology & Biotechnology. 22:45-50.
• Lo, C-M., Zhang ,Q., Callow, N.V.,and Ju, L-K., (2010) Cellulase production by continuous culture of Trichoderma reesei Rut C30 using acid hydrolysate prepared to retain more oligosaccharides for induction. Bioresour Technol .101(2):717–723.
• Longo, M.A., & Sanromán, M.N.,(2006). Production of food aroma compounds: Microbial and enzymatic methodologies. Food Technol Biotechnol .44:335–353..
• Manivannan, A.,& Narendhirakannan, R., (2014) Response surface optimization for co-production of cellulase and xylanase enzymes by Trichoderma reesei NRRL–3652. Int J ChemTech Res .6(7):3883.
• Millar,G.L.,(1959). use of dinitrosalicylic and reagent for determination of reducing sugar. Analytical chemistry.31:426-428.
• Nathan,V.K.,Rani, M.E., Rathinasamy,G., and Dhiraviam,K.N.,(2017). Low molecular weight xylanase from Trichoderma viride VKF3 for Bio-bleaching of newspaper pulp. Bio Resources.12(3):5264-5278.
• Pandey, A., (2003). Solid-state fermentation. BioChemical Engineering Journal. 13: 81-84.
• Pirota,R.D.P.B.;Delabona,P.S.,Farinas,C.S.,(2014).Simplification of the biomass to ethanol conversation process by using the whole medium of filamentous fungi cultivated under solid-state fermentation. Bioenergy Res.7:744-752.
• Ramasamy, S., Balakrishna, H.S., Selvaraj, U.,and Uppuluri, K.B., (2014) Production and statistical optimization of oxytetracycline from Streptomyces rimosus NCIM 2213 using a new cellulosic substrate, Prosopis juliflora. BioResources 9(4):7209–7221.
• Srikanth, R., Siddartha, G., Reddy, C.H.S., Harish, B., Ramaiah, M.J.,and Uppuluri, K.B., (2015) Antioxidant and anti-inflammatory levan produced from Acetobacter xylinum NCIM2526 and its statistical optimization. Carbohydr Polym. 123:8–16.
• Taibi,Z.,Saoudi,B.,Boudelaa,M.,Trigui,H.,Belghith,H., Gargouri,A.,and Ladjama,A., (2012). Purification and biochemical characterizationof a highly thermostable xylanase from Actinomadura sp. Strain Cpt20 isolated from poultry compost. Appl Biochem Biotechnol.166(3):663–679.
• Venkatesh,M., & Girija,D.,(2009). Micrbial pectinase from tropical fruit Wastes. Journul of Tropical Agriculture. 47(1):67-69.
• Walia,A.,Guleria,S.,Mehta,P.,Chauhan,A., and Prakash,J.,(2017). Microbial xylanases and their industrial application in pulp and paper biobleaching:a review.Biotech.7(11):1-12.
• Walter,M.,Jaklitsc,G.J.,Sarah,L.M., and Bing,S.L.,(2006). Hypocrearufa/ Trichoderma viride: a reassessment and description of five closely related specieswith and without warted condidia. Stud Mycol USA .56(1):135-177.
• Zhang, L., Wang, X., Ruan, Z., Liu, Y., Niu, X., Yue, Z., Li, Z., Liao, W.,and Liu, Y.,(2014) Fungal cellulase/xylanase production and corresponding hydrolysis using pretreated corn stover as substrates. Appl Biochem Biotechnol. 172(2):1045–1054.
• Kachlishvili, E., Penninckx, M.J., Tsiklauri, N., and Elisashvili, V., (2006). Effect of nitrogen source on lignocellulolytic enzyme production by white-rot basidiomycetes under solid-state cultivation. World Journal Microbiol Biotechnol .22(4):391–397.
• Gautam, S.P., Bundela, P.S., Pandey, A.K., Khan, J., Awasthi, M.K.,and Sarsaiya, S., (2011) Optimization for the production of cellulase enzyme from municipal solid waste residue by two novel cellulolytic fungi. Biotechnol Res Int.2011:1-8. doi:10.4061/2011/810425.
• Sun, X., Zhang, R.,and Zhang, Y. (2004) Production of lignocellulolytic enzymes by Trametes gallica and detection of polysaccharide hydrolase and laccase activities in polyacrylamide gels. J Basic Microbiol. 44(3):220–231.
• Kapich, A., Prior, B., Botha, A., Galkin, S., Lundell ,T., and Hatakka, A., (2004). Effect of lignocellulose-containing substrates on production of ligninolytic peroxidases in submerged cultures of Phanerochaete chrysosporium ME-446. Enzyme Microb Technol. 34(2):187–195.