Statistical Optimization of Cellulase Production by Thermomyces dupontii
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RESEARCH PAPER
Statistical Optimization of Cellulase Production by Thermomyces dupontii Kinza Nisar1 • Roheena Abdullah1 • Afshan Kaleem1 • Mehwish Iqtedar1 Received: 27 May 2019 / Accepted: 11 July 2020 Ó Shiraz University 2020
Abstract In the present investigation, significant physical parameters such as incubation time, temperature and pH were optimized for cellulase production by wild and mutant strains of thermophilic Thermomyces dupontii. For a comparative analysis, three independent variables which were selected from OVAT were subjected to RSM. As per response surface methodology (RSM) model, central composite design was used in order to analyze the interactive effects of significant physical factors on cellulase productivity. The second polynomial regression model with a determination coefficient R2 value 0.9503 and 0.9711 was found to be adequate and significant. 3D response surface plots and contours showed interaction among three variables. In contrast to wild T. dupontii, mutant strain showed 1.7-fold increase in FPase activity (43 U/ml/min) at 55 °C and pH 5.5 in 72 h. The result indicates thermophilic mutant T. dupontii has a potential for industrial use, because enzyme obtained from thermophile is more appropriate for industrial process where high temperature is involved. Keywords Submerged Temperature FPase Coefficient Contour
1 Introduction Lignocellulosic material is mainly composed of hemicellulose, cellulose, and lignin. Cellulose is composed of linear polymer of D-glucose units that are linked by b-1, 4 glycosidic bonds, whereas dimers of glucose units form cellobiose. Basically, cellulose exists in two forms including crystalline and amorphous (Priyanka et al. 2017). The lignocellulosic waste can be converted into simple sugars with the aid of cellulases. Cellulases belong to the group of glycoside hydrolases which catalyzes the hydrolysis of cellulose. Cellulose degradation is a complex process that involves coordination of different cellulolytic enzymes. These enzymes act synergistically to degrade cellulose, i.e., the endo-1,4-glucanases (EC 3.2.1.4), which randomly hydrolyze the glycosidic bonds; the exo-1,4glucanases or cellobiohydrolases (EC 3.2.1.91) act on the non-reducing and reducing ends of polysaccharides to give cellobiose units; and the b-1,4-glucosidases (EC 3.2.1.21) & Roheena Abdullah [email protected] 1
Department of Biotechnology, Lahore Collage for Women University, Lahore, Pakistan
degraded cellobiose to release glucose (Alvarez-Cervantes et al. 2016; Saroj et al. 2017). In many industrial processes, high temperature is required. In recent years, cellulase production by thermophilic fungi has received greater attention in many biotechnological applications including pulp and paper, detergent, food, animal feed and textile industries (Hebeish et al. 2009). The greater stability of thermostable enzymes at high-temperature and extreme operative conditions leads to better performance of hydrolysis making the p
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