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dc.creatorFanchini Terrasan,César Rafael
dc.creatorGuisan,José Manuel
dc.creatorCano Carmona,Eleonora
dc.date2016-09-01
dc.date.accessioned2019-05-03T12:45:26Z
dc.date.available2019-05-03T12:45:26Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000500006
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/85570
dc.descriptionBackground: Xylanases and β-D-xylosidases are the most important enzymes responsible for the degradation of xylan, the second main constituent of plant cell walls. Results: In this study, the main extracellular xylanase (XYL I) and p-xylosidase (BXYL I) from the fungus Penicillium janczewskii were purified, characterized and applied for the hydrolysis of different substrates. Their molecular weights under denaturing and non-denaturing conditions were, respectively, 30.4 and 23.6 kDa for XYL I, and 100 and 200 kDa for BXYL I, indicating that the latter is homodimeric. XYL I is highly glycosylated (78%) with optimal activity in pH 6.0 at 65°C, while BXYL I presented lower sugar content (10.5%) and optimal activity in pH 5.0 at 75°C. The half-lives of XYL I at 55, 60 and 65°C were 125,16 and 6 min, respectively. At 60°C, BXYL I retained almost 100% of the activity after 6 h. NH4+,Na+, DTT and β-mercaptoethanol stimulated XYL I, while activation of BXYL I was not observed. Interestingly, XYL I was only partially inhibited by Hg2+, while BXYL I was completely inhibited. Xylobiose, xylotriose and larger xylooligosaccharides were the main products from xylan hydrolysis by XYL I. BXYL I hydrolyzed xylobiose and larger xylooligosaccharides with no activity against xylans. Conclusion: The enzymes act synergistically in the degradation of xylans, and present industrial characteristics especially in relation to optimal activity at high temperatures, prolonged stability of BXYL I at 60°C, and stability of XYL I in wide pH range.
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dc.languageen
dc.publisherPontificia Universidad Católica de Valparaíso
dc.relation10.1016/j.ejbt.2016.08.001
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceElectronic Journal of Biotechnology v.19 n.5 2016
dc.subjectXylanolytic enzymes
dc.subjectEnzyme characterization
dc.subjectEnzyme purification
dc.subjectXylan hydrolysis
dc.subjectXylooligosaccharides hydrolysis
dc.titleXylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates


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