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Literature summary for 4.2.2.10 extracted from

  • Sinitsyna, O.A.; Fedorova, E.A.; Semenova, M.V.; Gusakov, A.V.; Sokolova, L.M.; Bubnova, T.M.; Okunev, O.N.; Chulkin, A.M.; Vavilova, E.A.; Vinetsky, Y.P.; Sinitsyn, A.P.
    Isolation and characterization of extracellular pectin lyase from Penicillium canescens (2007), Biokhimiya, 72, 565-571.
    View publication on PubMed

Application

Application Comment Organism
food industry successfully applied to production and clarification of juice Penicillium canescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information influence of the degree of etherification on turnover numer Penicillium canescens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Penicillium canescens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ at pH values above the optimum, calcium ions can increase pectin lyase activity or even shift the pH optimum into more acidic range. No effect on enzyme activity toward highly methylated citrus pectin is displayed by CaCl2 at the salt concentration of 0-0.1 M at pH 8.0 Penicillium canescens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37546
-
x * 37546, calculated from sequence Penicillium canescens
38000
-
x * 38000, SDS-PAGE Penicillium canescens

Organism

Organism UniProt Comment Textmining
Penicillium canescens
-
PCA-10
-
Penicillium canescens PCA-10
-
PCA-10
-

Purification (Commentary)

Purification (Comment) Organism
-
Penicillium canescens

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
Penicillium canescens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pectin among pectins with different degree of substitution, the enzyme preferably hydrolyzes highly etherized substrate. The enzyme has practically no effect on completely demethylated substrate Penicillium canescens ?
-
?
pectin among pectins with different degree of substitution, the enzyme preferably hydrolyzes highly etherized substrate. The enzyme has practically no effect on completely demethylated substrate Penicillium canescens PCA-10 ?
-
?

Subunits

Subunits Comment Organism
? x * 38000, SDS-PAGE Penicillium canescens
? x * 37546, calculated from sequence Penicillium canescens

Synonyms

Synonyms Comment Organism
pectin lyase A
-
Penicillium canescens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Penicillium canescens

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 65 40°C: about 50% of maximal activity, 65°C: about 70% of maximal activity Penicillium canescens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
pH 5.0-6.0, 3 h, 20% loss of activity, pH 4.0, 30% loss of activity after 3 h Penicillium canescens
50
-
pH 5.0-6.0, 3 h, 40% loss of activity. pH 4.0, 60% loss of activity after 3 h Penicillium canescens
60
-
pH 5.0, 80% loss of activity after 1 h. pH 6.0 or pH 4.0, complete loss of activity after 1 h Penicillium canescens
70
-
half-inactivation time at pH 6.0 is 120 sec, half-inactivation time at pH 4.0 is 150 sec, half-inactivation time at pH 5.0 is 180 sec Penicillium canescens
80
-
at a humidity of 2-3%, the enzyme preserves 95% of its initial activity after incubation during 7 min. At a humidity of 15%, enzyme half-inactivation time is 120 sec Penicillium canescens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information influence of the degree of etherification on turnover numer Penicillium canescens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 5.5
-
Penicillium canescens

pH Range

pH Minimum pH Maximum Comment Organism
4.3 6.3 pH 4.3: about 50% of maximal activity, pH 6.3: about 50% of maximal activity Penicillium canescens

pH Stability

pH Stability pH Stability Maximum Comment Organism
4
-
30% loss of activity after 3 h at 40°C. 60% loss of activity after 3 h at 50°C, complete loss of activity after 30-40 min Penicillium canescens
5 6 highest stability, 20% loss of activity after 3 h at 40°C. 40% loss of activity after 3 h at 50°C Penicillium canescens
5
-
60°C, 80% loss of activity after 1 h Penicillium canescens
6
-
60°C, complete loss of activity after 30-40 min Penicillium canescens

pI Value

Organism Comment pI Value Maximum pI Value
Penicillium canescens calculated from sequence
-
6
Penicillium canescens isoelectrofocusing
-
6.7