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Novel thermodynamics of xylanase formation by a 2-deoxy-d-glucose resistant mutant of Thermomyces lanuginosus and its xylanase potential for biobleachability. | LitMetric

AI Article Synopsis

  • The study examined how well xylanases are produced by both the wild type and a mutant strain (M7) of the fungus Thermomyces lanuginosus using various substrates.
  • M7 showed significantly increased xylanase production on glucose-based media, producing 8.8 times more than the wild type, with optimal results seen using a mix of corncob and corn steep liquor.
  • In biobleaching tests, enzymes from the mutant reduced the kappa number and chlorine demand more effectively than those from the wild type, suggesting that the mutant's enzymes have promising potential for industrial applications.

Article Abstract

Production of xylanases by Thermomyces lanuginosus wild type and its deoxyglucose resistant mutant M7 on different substrates was investigated. The mutation conferred catabolite repression resistance as M7 supported xylanase production on glucose-based medium that was 8.8-fold higher than that of wild type. Product formation parameters were highest in media containing a combination of corncob and corn steep liquor. Among the soluble substrates, xylose was the best inducer. In the presence of glucose, the wild type produced 26 IU of xylanase per g of glucose while the xylanase yield of the mutant was 224 IU per g of glucose. Thermodynamic studies showed that M7 required lower Gibbs free energy, enthalpy and entropy for product formation than the wild type. In biobleaching studies an 18.6% decrease in kappa number and 2.63% increase in brightness for enzyme-treated pulp was observed. Moreover prebleaching with M7-derived enzyme resulted in a 27.3% reduction in chlorine demand as compared with that of 18.5% decrease when wild organism-derived enzyme was employed. These improvements indicate that the mutant-derived enzymes possessed a useful prebleaching potential and could be exploited for large-scale application.

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Source
http://dx.doi.org/10.1016/j.biortech.2009.10.072DOI Listing

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