Valorization of corn cob for the obtention and purification of endoglucanase produced by SSF |
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Affiliation: | 1. IPROByQ-CONICET, Faculty of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 531, 2000, Rosario, Argentina;2. Area of Statistics and Data Processing, Faculty of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 531, 2000, Rosario, Argentina;3. Food Research Department, School of Chemistry, Universidad Autónoma de Coahuila, Blvd. Venustiano Carranza and J. Cárdenas s/n, ZIP 25280, Saltillo, Coahuila, Mexico;1. Faculty of Applied Life Science, Nippon Veterinary and Life Science University, Musashino, Tokyo, Japan;2. Graduate School of Agriculture, Ibaraki University, Inashiki, Ibaraki, Japan;1. Key Laboratory of Textile Fibers and Products, Ministry of Education, P. R. C, College of Materials Science and Engineering, Wuhan Textile University, Wuhan 430073, China;2. Third Institute of Oceanography, Ministry of Natural Resources, P. R. C, Xiamen 361005, China;3. High-Tech Organic Fibers Key Laboratory of Sichuan Province, Sichuan Textile Research Institute, Chengdu 610072, China;1. Department of Pharmaceutical Biotechnology, School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran;2. Pharmaceutical Sciences Research Center, Shiraz University of Medical Science, Shiraz, Iran;3. Biotechnology Research Center, Shiraz University of Medical Sciences, Shiraz, Iran |
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Abstract: | Agro-food by-products contain valuable nutrients which are wasted. In this work, solid-state fermentation (SSF) was carried out using corn cob as substrate for endoglucanase production. The radial growth of three fungal strains -Trichoderma harzianum T104, Aspergillus niger GH1 and Aspergillus niger NRRL3- was analyzed in order to select the most appropriate. Radial growth data were analyzed with a mixed linear model for longitudinal data and no statistically significant differences were found between both A. niger strains.Endoglucanase was separated from the extract of A. niger GH1 by fast protein liquid chromatography (FPLC).The highest endoglucanase activity was detected in fraction number three collected from FPLC corresponding to 72 h of SSF. Seven bands in a range from 24 to 50 kDa, which correspond to endoglucanase from fungal extract, were detected by zymogram analysis. According to protein quantification performed by the ImageJ software, 85% of the proteins present in the samples collected by FPLC corresponded to endoglucanase proteins. The purified endoglucanase retained about 100% of its catalytic activity at 30 °C and 50 °C and was stable in a pH range between 4.00-6.00. These properties make this isolated enzyme suitable for industrial applications such as the saccharification process for bioethanol production. |
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Keywords: | Radial growth Endoglucanase SSF Corn cob Purification |
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