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Literature summary for 3.2.1.8 extracted from

  • Fanchini Terrasan, C.; Trobo-Maseda, L.; Moreno-Perez, S.; Carmona, E.; Pessela, B.; Guisan, J.
    Co-immobilization and stabilization of xylanase, beta-xylosidase and alpha-L--arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis (2016), Process Biochem., 51, 614-623.
No PubMed abstract available

Application

Application Comment Organism
degradation co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads 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 alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles Penicillium janczewskii

Organism

Organism UniProt Comment Textmining
Penicillium janczewskii
-
-
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Penicillium janczewskii CRM 1348
-
-
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Penicillium janczewskii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
24 h, more than 70% residual activity Penicillium janczewskii
80
-
half-life 1.7 h Penicillium janczewskii

pH Range

pH Minimum pH Maximum Comment Organism
2 4
-
Penicillium janczewskii