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Literature summary for 4.2.2.10 extracted from

  • Bibi, F.; Irshad, M.; Anwar, Z.; Bhatti, K.; Raza, A.
    Improved catalytic functionalities of purified pristine and chitosan-immobilized polygalacturonase, and pectin lyase (2017), Chem. Eng. Res. Des., 128, 146-154 .
No PubMed abstract available
Search for more literature for 4.2.2.10

Application

Application Comment Organism
synthesis purification and surface immobilization using various concentrations of chitosan and glutaraldehyde as cross-linking agent. The immobilized fractions are highly stable over a pH and temperature range from 4-9 and 45-85°C, respectively. Chitosan-immobilized enzyme fractions retain more than 75% of their operational activities even after seven consecutive cycles Neurospora crassa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 apple pectin Km value 0.13 mg/ml for free enzyme, 0.10 mg/ml for chitosan-immobilized enzyme, respectively, 40°C, pH not specified in the publication Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Neurospora crassa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
377
-
 40°C, pH not specified in the publication Neurospora crassa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
apple pectin
-
 Neurospora crassa ?
-
 ?

Expression

Organism Comment Expression
Neurospora crassa isolation after fermentation citrus peel waste additional information