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Literature summary for 4.2.2.23 extracted from

  • Mutter, M.; Colquhoun, I.J.; Beldman, G.; Schols, H.A.; Bakx, E.J.; Voragen, A.G.
    Characterization of recombinant rhamnogalacturonan alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase from Aspergillus aculeatus. An enzyme that fragments rhamnogalacturonan I regions of pectin (1998), Plant Physiol., 117, 141-152.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
food industry rhamnogalacturonan lyase is useful in the processing of fruit, where it is important that the commercial pectolytic enzyme preparations solubilize and hydrolyze the branched RG structures, which otherwise remain as colloidally dissolved polymers in the juice and lead to problems during filtration and clarification Aspergillus aculeatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
rhamnogalacturonan I KM-values of recombinant rhamnogalacturonan lyase towards enzyme-treated saponified modified hairy regions of pectin Aspergillus aculeatus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
gel filtration Aspergillus aculeatus

Organism

Organism UniProt Comment Textmining
Aspergillus aculeatus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native and recombinant enzyme Aspergillus aculeatus

Source Tissue

Source Tissue Comment Organism Textmining
culture supernatant
-
Aspergillus aculeatus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
rhamnogalacturonan I rhamnogalacturonan I domains in saponified hairy regions of apple pectin. The enzyme fragments rhamnogalacturonan I by a multiple attack mechanism. The catalytic efficiency of recombinant rhamnogalacturonan lyase increases with decreasing degree of acetylation. Removal of arabinose side chains improves the action of recombinant rhamnogalacturonan lyase. Removal of galactose side chains decreases the catalytic efficiency of recombinant rhamnogalacturonanlyase. The average degree of multiple attack is 2.5 (the degree of multiple attack is defined as the average number of catalytic events, following the first, during the lifetime of an individual enzyme-substrate complex) Aspergillus aculeatus rhamnogalacturonan I oligosaccharides with alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the nonreducing end major oligomeric reaction products contain an alternating rhamnogalacturonan backbone with a degree of polymerization of 4, 6, 8, and 10 and with an alpha-D-(4,5)-unsaturated D-galactopyranosyluronic acid at the nonreducing end and an L-rhamnopyranose at the reducing end ?

Subunits

Subunits Comment Organism
monomer 1 * 57000, SDS-PAGE Aspergillus aculeatus

Synonyms

Synonyms Comment Organism
RG-lyase
-
Aspergillus aculeatus
rhamnogalacturonan alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase
-
Aspergillus aculeatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50 60
-
Aspergillus aculeatus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
pH 5.0, 4.5 h, stable Aspergillus aculeatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Aspergillus aculeatus

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 8 40°C, stable Aspergillus aculeatus

pI Value

Organism Comment pI Value Maximum pI Value
Aspergillus aculeatus zymography 5.3 5.1