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Literature summary for 4.2.2.2 extracted from

  • Zhang, C.; Yao, J.; Zhou, C.; Mao, L.; Zhang, G.; Ma, Y.
    The alkaline pectate lyase PEL168 of Bacillus subtilis heterologously expressed in Pichia pastoris is more stable and efficient for degumming ramie fiber (2013), BMC Biotechnol., 13, 26.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
DMSO 24% activation at 0.5% Bacillus subtilis
additional information no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5% Bacillus subtilis

Application

Application Comment Organism
environmental protection the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption Bacillus subtilis
industry the conventional degumming process of ramie with alkaline treatment at high temperature causes severe environmental pollution. Pectate lyases can be used to remove pectin from ramie in a degumming process with reduced environmental pollution and energy consumption Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
gene pel168, enzyme expression in Pichia pastoris strain and in Escherichia coli, the latter shows less glycosylation and thermostability Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
Co2+ 53% inhibition at 5 mM Bacillus subtilis
Cu2+ 93% inhibition at 5 mM Bacillus subtilis
EDTA complete inhibition at 5 mM Bacillus subtilis
Fe3+ 41% inhibition at 5 mM Bacillus subtilis
Hg2+ complete inhibition at 5 mM Bacillus subtilis
Mg2+ 64.5% inhibition at 5 mM Bacillus subtilis
Mn2+ 91.5% inhibition at 5 mM Bacillus subtilis
additional information no or poor effect by Tween-80, methanol, ethanol, isopropyl alcohol at 0.5% Bacillus subtilis
Ni2+ 18% inhibition at 5 mM Bacillus subtilis
SDS complete inhibition at 0.5% Bacillus subtilis
Zn2+ 63.5% inhibition at 5 mM Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required, activates the recombinant enzyme from Pichia pastoris by 26% Bacillus subtilis
additional information no or poor effect on the recombinant enzyme from Pichia pastoris by Sr2+, K+, and Li+ Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
x * 48600-51400, recombinant enzyme from Pichia pastoris, SDS-PAGE, x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P39116 gene pel168
-
Bacillus subtilis 168 P39116 gene pel168
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme has five putative N-glycosylation sites (Asn-X-Thr/Ser), three near to the N-terminus (N-48, N-127, N-184), and the other two near the C-terminus (N-345, N-351) Bacillus subtilis

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1320
-
purified recombinant enzyme from Pichia pastoris, pH 9.5, 50°C Bacillus subtilis

Subunits

Subunits Comment Organism
? x * 48600-51400, recombinant enzyme from Pichia pastoris, SDS-PAGE, x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE Bacillus subtilis

Synonyms

Synonyms Comment Organism
alkaline pectate lyase
-
Bacillus subtilis
PEL168
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
purified enzyme, 20 min, recombinant enzyme from Pichia pastoris retaines 26% activity, recombinant enzyme from Escherichia coli is inactivated Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
-
Bacillus subtilis