Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
Differently activated agarose-based supports were evaluated for co-immobilization of a crude extract from Penicillium janczewskii containing xylanase, β-xylosidase and α-l-arabinofuranosidase activities. Adequately selecting support and immobilization conditions (8 h, using agarose with 10% crosslinking) increased enzyme levels substantially, mainly in relation to the xylanase (2-fold). A coating with dextran aldehyde MW 6000 Da, partially oxidized, covalently attached the enzymes to the support. Optimum activity was verified in the pH range 2-4, and at 50, 65 and 80 °C for the xylanase, α-l-arabinofuranosidase and β-xylosidase, respectively. The xylanase was highly thermostable retaining more than 70% of activity even after 24 h incubation at 60 and 70 °C; and at 80 °C its half-life was 1.7 h. The half-lives of the β-xylosidase and α-l-arabinofuranosidase at 50 °C were 2.3 and 3.8 h, respectively. The co-immobilization of the enzymes on a single support give raise to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the α-l-arabinofuranosidase presented high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles.
Saved in:
| Main Authors: | , , , , , |
|---|---|
| Format: | artículo biblioteca |
| Published: |
Elsevier
2016
|
| Subjects: | Xylanase, Xylan hydrolysis, β-xylosidase, α-l-arabinofuranosidase, Enzyme co-immobilization, Penicillium janczewskii, |
| Online Access: | http://hdl.handle.net/10261/150099 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| id |
dig-cial-es-10261-150099 |
|---|---|
| record_format |
koha |
| spelling |
dig-cial-es-10261-1500992020-01-15T09:26:30Z Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis Fanchini Terrasan, César Rafael Trobo-Maseda, Lara Moreno-Pérez, Sonia Cano Carmona, Eleonora Pessela, Benevides C. Guisán, José Manuel Xylanase Xylan hydrolysis β-xylosidase α-l-arabinofuranosidase Enzyme co-immobilization Penicillium janczewskii Differently activated agarose-based supports were evaluated for co-immobilization of a crude extract from Penicillium janczewskii containing xylanase, β-xylosidase and α-l-arabinofuranosidase activities. Adequately selecting support and immobilization conditions (8 h, using agarose with 10% crosslinking) increased enzyme levels substantially, mainly in relation to the xylanase (2-fold). A coating with dextran aldehyde MW 6000 Da, partially oxidized, covalently attached the enzymes to the support. Optimum activity was verified in the pH range 2-4, and at 50, 65 and 80 °C for the xylanase, α-l-arabinofuranosidase and β-xylosidase, respectively. The xylanase was highly thermostable retaining more than 70% of activity even after 24 h incubation at 60 and 70 °C; and at 80 °C its half-life was 1.7 h. The half-lives of the β-xylosidase and α-l-arabinofuranosidase at 50 °C were 2.3 and 3.8 h, respectively. The co-immobilization of the enzymes on a single support give raise to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the α-l-arabinofuranosidase presented high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles. Peer Reviewed 2017-05-22T11:37:18Z 2017-05-22T11:37:18Z 2016 2017-05-22T11:37:18Z artículo http://purl.org/coar/resource_type/c_6501 doi: 10.1016/j.procbio.2016.02.014 issn: 1359-5113 e-issn: 1873-3298 Process Biochemistry 51(5): 614-623 (2016) http://hdl.handle.net/10261/150099 10.1016/j.procbio.2016.02.014 Postprint https://doi.org/10.1016/j.procbio.2016.02.014 Sí open Elsevier |
| institution |
CIAL ES |
| collection |
DSpace |
| country |
España |
| countrycode |
ES |
| component |
Bibliográfico |
| access |
En linea |
| databasecode |
dig-cial-es |
| tag |
biblioteca |
| region |
Europa del Sur |
| libraryname |
Biblioteca del CIAL España |
| topic |
Xylanase Xylan hydrolysis β-xylosidase α-l-arabinofuranosidase Enzyme co-immobilization Penicillium janczewskii Xylanase Xylan hydrolysis β-xylosidase α-l-arabinofuranosidase Enzyme co-immobilization Penicillium janczewskii |
| spellingShingle |
Xylanase Xylan hydrolysis β-xylosidase α-l-arabinofuranosidase Enzyme co-immobilization Penicillium janczewskii Xylanase Xylan hydrolysis β-xylosidase α-l-arabinofuranosidase Enzyme co-immobilization Penicillium janczewskii Fanchini Terrasan, César Rafael Trobo-Maseda, Lara Moreno-Pérez, Sonia Cano Carmona, Eleonora Pessela, Benevides C. Guisán, José Manuel Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis |
| description |
Differently activated agarose-based supports were evaluated for co-immobilization of a crude extract from Penicillium janczewskii containing xylanase, β-xylosidase and α-l-arabinofuranosidase activities. Adequately selecting support and immobilization conditions (8 h, using agarose with 10% crosslinking) increased enzyme levels substantially, mainly in relation to the xylanase (2-fold). A coating with dextran aldehyde MW 6000 Da, partially oxidized, covalently attached the enzymes to the support. Optimum activity was verified in the pH range 2-4, and at 50, 65 and 80 °C for the xylanase, α-l-arabinofuranosidase and β-xylosidase, respectively. The xylanase was highly thermostable retaining more than 70% of activity even after 24 h incubation at 60 and 70 °C; and at 80 °C its half-life was 1.7 h. The half-lives of the β-xylosidase and α-l-arabinofuranosidase at 50 °C were 2.3 and 3.8 h, respectively. The co-immobilization of the enzymes on a single support give raise to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the α-l-arabinofuranosidase presented high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles. |
| format |
artículo |
| topic_facet |
Xylanase Xylan hydrolysis β-xylosidase α-l-arabinofuranosidase Enzyme co-immobilization Penicillium janczewskii |
| author |
Fanchini Terrasan, César Rafael Trobo-Maseda, Lara Moreno-Pérez, Sonia Cano Carmona, Eleonora Pessela, Benevides C. Guisán, José Manuel |
| author_facet |
Fanchini Terrasan, César Rafael Trobo-Maseda, Lara Moreno-Pérez, Sonia Cano Carmona, Eleonora Pessela, Benevides C. Guisán, José Manuel |
| author_sort |
Fanchini Terrasan, César Rafael |
| title |
Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis |
| title_short |
Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis |
| title_full |
Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis |
| title_fullStr |
Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis |
| title_full_unstemmed |
Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis |
| title_sort |
co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from penicillium janczewskii for arabinoxylan hydrolysis |
| publisher |
Elsevier |
| publishDate |
2016 |
| url |
http://hdl.handle.net/10261/150099 |
| work_keys_str_mv |
AT fanchiniterrasancesarrafael coimmobilizationandstabilizationofxylanasebxylosidaseandalarabinofuranosidasefrompenicilliumjanczewskiiforarabinoxylanhydrolysis AT trobomasedalara coimmobilizationandstabilizationofxylanasebxylosidaseandalarabinofuranosidasefrompenicilliumjanczewskiiforarabinoxylanhydrolysis AT morenoperezsonia coimmobilizationandstabilizationofxylanasebxylosidaseandalarabinofuranosidasefrompenicilliumjanczewskiiforarabinoxylanhydrolysis AT canocarmonaeleonora coimmobilizationandstabilizationofxylanasebxylosidaseandalarabinofuranosidasefrompenicilliumjanczewskiiforarabinoxylanhydrolysis AT pesselabenevidesc coimmobilizationandstabilizationofxylanasebxylosidaseandalarabinofuranosidasefrompenicilliumjanczewskiiforarabinoxylanhydrolysis AT guisanjosemanuel coimmobilizationandstabilizationofxylanasebxylosidaseandalarabinofuranosidasefrompenicilliumjanczewskiiforarabinoxylanhydrolysis |
| _version_ |
1777671254097002496 |