Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates
Background: 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 janczewsk...
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Pontificia Universidad Católica de Valparaíso
2016
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oai:scielo:S0717-345820160005000062016-10-26Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substratesFanchini Terrasan,César RafaelGuisan,José ManuelCano Carmona,Eleonora Xylanolytic enzymes Enzyme characterization Enzyme purification Xylan hydrolysis Xylooligosaccharides hydrolysis Background: 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.19 n.5 20162016-09-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000500006en10.1016/j.ejbt.2016.08.001 |
| institution |
Scielo Chile |
| collection |
Scielo Chile |
| language |
English |
| topic |
Xylanolytic enzymes Enzyme characterization Enzyme purification Xylan hydrolysis Xylooligosaccharides hydrolysis |
| spellingShingle |
Xylanolytic enzymes Enzyme characterization Enzyme purification Xylan hydrolysis Xylooligosaccharides hydrolysis Fanchini Terrasan,César Rafael Guisan,José Manuel Cano Carmona,Eleonora Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates |
| description |
Background: 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. |
| author |
Fanchini Terrasan,César Rafael Guisan,José Manuel Cano Carmona,Eleonora |
| author_facet |
Fanchini Terrasan,César Rafael Guisan,José Manuel Cano Carmona,Eleonora |
| author_sort |
Fanchini Terrasan,César Rafael |
| title |
Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates |
| title_short |
Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates |
| title_full |
Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates |
| title_fullStr |
Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates |
| title_full_unstemmed |
Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates |
| title_sort |
xylanase and β-xylosidase from penicillium janczewskii: purification, characterization and hydrolysis of substrates |
| publisher |
Pontificia Universidad Católica de Valparaíso |
| publishDate |
2016 |
| url |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000500006 |
| work_keys_str_mv |
AT fanchiniterrasancesarrafael xylanaseand946xylosidasefrompenicilliumjanczewskiipurificationcharacterizationandhydrolysisofsubstrates AT guisanjosemanuel xylanaseand946xylosidasefrompenicilliumjanczewskiipurificationcharacterizationandhydrolysisofsubstrates AT canocarmonaeleonora xylanaseand946xylosidasefrompenicilliumjanczewskiipurificationcharacterizationandhydrolysisofsubstrates |
| _version_ |
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