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Literature summary for 3.2.1.55 extracted from

  • Jia, L.; Budinova, G.; Takasugi, Y.; Noda, S.; Tanaka, T.; Ichinose, H.; Goto, M.; Kamiya, N.
    Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase (2016), Biochem. Eng. J., 114, 268-275.
No PubMed abstract available
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Application

Application Comment Organism
degradation hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilized on commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed Acetivibrio thermocellus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Acetivibrio thermocellus

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
wheat arabinoxylan + H2O
-
 Acetivibrio thermocellus L-arabinose + ?
-
 ?

Synonyms

Synonyms Comment Organism
Araf51A
-
 Acetivibrio thermocellus