Production, Purification, and Characterization of a Cellulase from Paenibacillus elgii .

Autor: Doan CT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Tran TN; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Pham TP; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Tran TTT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Truong BP; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Nguyen TT; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Nguyen TM; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Bui TQH; Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Nguyen AD; Institute of Biotechnology and Environment, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam., Wang SL; Department of Chemistry, Tamkang University, New Taipei City 25137, Taiwan.; Life Science Development Center, Tamkang University, New Taipei City 25137, Taiwan.
Jazyk: angličtina
Zdroj: Polymers [Polymers (Basel)] 2024 Jul 17; Vol. 16 (14). Date of Electronic Publication: 2024 Jul 17.
DOI: 10.3390/polym16142037
Abstrakt: Cellulases are one of the most essential natural factors for cellulose degradation and, thus, have attracted significant interest for various applications. In this study, a cellulase from Paenibacillus elgii TKU051 was produced, purified, and characterized. The ideal fermentation conditions for cellulase productivity were 2% carboxymethyl cellulose (CMC) as the growth substrate, pH = 8, temperature of 31 °C, and 4 days of culturing. Accordingly, a 45 kDa cellulase (PeCel) was successfully purified in a single step using a High Q column with a recovery yield of 35% and purification of 42.2-fold. PeCel has an optimal activity at pH 6 and a temperature of 60 °C. The activity of cellulase was significantly inhibited by Cu 2+ and enhanced by Mn 2+ . The PeCel-catalyzed products of the CMC hydrolysis were analyzed by high-performance liquid chromatography, which revealed chitobiose and chitotriose as the major products. Finally, the clarity of apple juice was enhanced when treated with PeCel.
Databáze: MEDLINE
Nepřihlášeným uživatelům se plný text nezobrazuje