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Literature summary extracted from

  • Miyazaki, K.
    Hyperthermophilic alpha-L-arabinofuranosidase from Thermotoga maritima MSB8: molecular cloning, gene expression, and characterization of the recombinant protein (2005), Extremophiles, 9, 399-406.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.55 biotechnology degradation of lignocellulose, hemicellulose and pectin Thermotoga maritima
3.2.1.55 nutrition clarification of fruit juices for wine industry Thermotoga maritima

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.55 expressed in Escherichia coli Thermotoga maritima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.55 332000
-
 gel filtration Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.55 Thermotoga maritima
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.55 30 min heat treatment at 80°C, hydrophobic interaction, anion exchange and gel permeation column chromatography Thermotoga maritima

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.55 additional information
-
 no activity on p-nitrophenyl-alpha-L-arabinopyranoside substrate Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
3.2.1.55 AFase
-
 Thermotoga maritima
3.2.1.55 alpha-L-arabinofuranosidase
-
 Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.55 90
-
 50% activity drop in 20 min at 100°C, thereafter reactivation occurs very slowly with half-life of 2.7 h Thermotoga maritima