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Literature summary for 4.2.2.14 extracted from

  • Tavernier, M.L.; Petit, E.; Delattre, C.; Courtois, B.; Courtois, J.; Strancar, A.; Michaud, P.
    Production of oligoglucuronans using a monolithic enzymatic microreactor (2008), Carbohydr. Res., 343, 2687-2691.
    View publication on PubMed

Application

Application Comment Organism
biotechnology a glucuronan lyase is immobilized on a monolithic Convective Interaction Media disk. Degradations of three glucuronans with various O-acetylation degrees is investigated and compared with degradations using free enzyme. The immobilized glucuronan lyase is inhibited by the O-acetylation degree like the free enzyme. 1H NMR analyses are used to study the O-acetylation degree of oligoglucuronans and demonstrate that the average degrees of polymerization are inclusive between 4 and 13 after 24 h of degradation. This first immobilization of a glucuronan lyase constitutes a tool to produce oligoglucuronans Trichoderma sp.

Organism

Organism UniProt Comment Textmining
Trichoderma sp.
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-
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Purification (Commentary)

Purification (Comment) Organism
gel filtration and anion-exchange chromatography Trichoderma sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
immobilized glucuronan lyase activity is calculated for deacetylated glucuronan. The activity is 1300times less than the theoretical immobilized activity. Activity decreases 4times and 14times for native and highly acetylated glucuronans, respectively Trichoderma sp.

Synonyms

Synonyms Comment Organism
glucuronan lyase
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Trichoderma sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
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assay at Trichoderma sp.