Production and characterization of Trichoderma reesei and Thermomyces lanuginosus xylanases

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en Xiong, Hairong 2012-02-13T13:00:29Z 2012-02-13T13:00:29Z 2004-10-30
dc.identifier.isbn 951-22-7318-7
dc.identifier.issn 0359-6621
dc.description.abstract This thesis describes the production and properties of xylanases from Trichoderma reesei Rut C-30 and Thermomyces lanuginosus DSM 10635. The thermostability of several T. reesei xylanase II mutants was also studied. T. reesei Rut C-30 responds to the pH of the growth environment by modifying its enzyme production patterns. The production of the xylanases I, II and III by T. reesei at different pH conditions correlates with the pH-dependent activity pattern of the enzymes. The xylanase was preferentially produced when it is most active in that particular pH environment. The highest total xylanase production with T. reesei Rut C-30 was achieved at pH 6 on a lactose-based medium. Among the pentoses and hexoses tested, L-arabinose was the most effective inducer of the xylanases. Furthermore, in co-metabolism of L-arabinose and D-glucose, the addition of the former relieved the repression of D-glucose on xylanase production. The replacement of part lactose with L-arabinose resulted in significant improvement in xylanase production. Small amounts of bulky L-arabinose-rich plant materials, such as sugar beet pulp and oat husk hydrolysates, stimulated the xylanase production. While xylanase production was improved by these approaches, the cellulase production was not enhanced. In addition, the stability and activity of T. reesei xylanase II mutants containing different combinations of disulphide bridges were studied. The most stable combination mutant showed about 5000-fold half-life at 65 °C compared to the wild type xylanase II. The molecular system controlling xylanase induction was fundamentally different in T. reesei and T. lanuginosus. Unlike T. reesei Rut C-30, T. lanuginosus DSM 10635 xylanase was not induced by L-arabinose or lactose. The amino acid sequence of DSM 10635 xylanase was most likely the same as that of T. lanuginosus DSM 5826 xylanase. The temperature-dependent inactivation curve of the DSM 10635 xylanase decreased slowly at neutral or slightly alkaline pH, whereas at low pH, the inactivation was fast. The thermostabilizing effect of the substrate, birchwood xylan, on DSM 10635 xylanase was observed to be significant only under acidic conditions. en
dc.format.extent 46, [33]
dc.format.mimetype application/pdf
dc.language.iso en en
dc.publisher Helsinki University of Technology en
dc.publisher Teknillinen korkeakoulu fi
dc.relation.ispartofseries Technical biochemistry report en
dc.relation.ispartofseries Teknillisen biokemian tiedote fi
dc.relation.ispartofseries 9 en
dc.relation.haspart Xiong H., von Weymarn N., Leisola M. and Turunen O., 2004. Influence of pH on the production of xylanases by Trichoderma reesei Rut C-30. Process Biochemistry 39, number 6, pages 729-733.
dc.relation.haspart Xiong H., Turunen O., Pastinen O., Leisola M. and von Weymarn N., 2004. Improved xylanase production by Trichoderma reesei grown on L-arabinose and lactose or D-glucose mixtures. Applied Microbiology and Biotechnology 64, number 3, pages 353-358.
dc.relation.haspart Xiong H., von Weymarn N., Turunen O., Leisola M. and Pastinen O., Xylanase production by Trichoderma reesei Rut C-30 grown on L-arabinose-rich plant hydrolysates. Bioresource Technology, in press.
dc.relation.haspart Xiong H., Fenel F., Leisola M. and Turunen O., 2004. Engineering the thermostability of Trichoderma reesei endo-1,4-β-xylanase II by combination of disulphide bridges. Extremophiles 8, number 5, pages 393-400.
dc.relation.haspart Xiong H., Nyyssölä A., Jänis J., Pastinen O., von Weymarn N., Leisola M. and Turunen O., 2004. Characterization of the xylanase produced by submerged cultivation of Thermomyces lanuginosus DSM 10635. Enzyme and Microbial Technology 35, number 1, pages 93-99.
dc.subject.other Chemistry en
dc.title Production and characterization of Trichoderma reesei and Thermomyces lanuginosus xylanases en
dc.type G5 Artikkeliväitöskirja fi
dc.description.version reviewed en
dc.contributor.department Department of Chemical Technology en
dc.contributor.department Kemian tekniikan osasto fi
dc.subject.keyword xylanase en
dc.subject.keyword cellulase en
dc.subject.keyword Trichoderma reesei en
dc.subject.keyword Thermomyces lanuginosus en
dc.subject.keyword pH en
dc.subject.keyword L-arabinose en
dc.subject.keyword oligosaccharides en
dc.subject.keyword characterization en
dc.subject.keyword cultivation en
dc.subject.keyword induction en
dc.subject.keyword purification en
dc.subject.keyword thermostability en
dc.identifier.urn urn:nbn:fi:tkk-004295
dc.type.dcmitype text en
dc.type.ontasot Väitöskirja (artikkeli) fi
dc.type.ontasot Doctoral dissertation (article-based) en
dc.contributor.lab Laboratory of Bioprocess Engineering en
dc.contributor.lab Bioprosessitekniikan laboratorio fi

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