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Literature summary for 3.2.1.132 extracted from

  • Kobayashi, T.; Koide, O.; Deguchi, S.; Horikoshi, K.
    Characterization of chitosanase of a deep biosphere Bacillus strain (2011), Biosci. Biotechnol. Biochem., 75, 669-673.
    View publication on PubMed
Search for more literature for 3.2.1.132

Cloned(Commentary)

Cloned (Comment) Organism
-
 Bacillus thuringiensis

Inhibitors

Inhibitors Comment Organism Structure
2-Hydroxy-5-nitrobenzyl bromide 69% inhibition at 5 mM, 33% inhibition at 1 mM Bacillus thuringiensis
Co2+ 60% inhibition at 1 mM Bacillus thuringiensis
Cu2+ 70% inhibition at 1 mM Bacillus thuringiensis
Fe3+ 35% inhibition at 1 mM Bacillus thuringiensis
Hg2+ 98% inhibition at 1 mM Bacillus thuringiensis
KCl complete inhibition at 100 mM Bacillus thuringiensis
additional information the enzyme is very stable under incubation with EDTA, EGTA, o-phenanthroline, N-ethylmaleimide, monoiodoacetate and EDAC (5 mM each), beta-mercaptoethanol and dithiothreitol (2 mM each), N-bromosuccinimide (1 mM) and p-chloromercuribenzoate (0.1 mM) Bacillus thuringiensis
Na2SO4 complete inhibition at 100 mM Bacillus thuringiensis
NaCl complete inhibition at 100 mM Bacillus thuringiensis
Ni2+ 25% inhibition at 1 mM Bacillus thuringiensis
Pd2+ 96% inhibition at 1 mM Bacillus thuringiensis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information not affected by Ca2+, Sr2+, Mn2+, Fe2+, Sn2+, and Zn2+ Bacillus thuringiensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
 gel filtration Bacillus thuringiensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
-
-
-
Bacillus thuringiensis JAM-GG01
-
-
-

Purification (Commentary)

Purification (Comment) Organism
SuperQ column chromatography and CM Toyopearl column chromatography Bacillus thuringiensis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
17.1
-
 culture broth, pH 6.0, 50°C Bacillus thuringiensis
412
-
 after 24.1fold purification, pH 6.0, 50°C Bacillus thuringiensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chitosan + H2O
-
 Bacillus thuringiensis chitotriose + chitotetraose
-
 ?
chitosan + H2O
-
 Bacillus thuringiensis JAM-GG01 chitotriose + chitotetraose
-
 ?
additional information the enzyme does not hydrolyze glycolchitosan, chitin, carboxymethyl cellulose, barley beta-glucan or phosphoric acid swollen cellulose (0.2% each) Bacillus thuringiensis ?
-
 ?
additional information the enzyme does not hydrolyze glycolchitosan, chitin, carboxymethyl cellulose, barley beta-glucan or phosphoric acid swollen cellulose (0.2% each) Bacillus thuringiensis JAM-GG01 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 43000, SDS-PAGE Bacillus thuringiensis

Synonyms

Synonyms Comment Organism
Cho-GG
-
 Bacillus thuringiensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 in acetate buffer (pH 5.6) Bacillus thuringiensis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 70
-
 Bacillus thuringiensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45 55 the enzyme is gradually inactivated during incubation at temperature above 45°C and is completely inactivated at 55°C after 15 min, at 55°C this instability is abolished in the presence of reaction products chitotriose and chitotetraose (2.5 mM each). The residual activities of the enzyme after 1 h of incubation at 60°C with 10 mM chitotriose or chitotetraose are 35.5% and 59.5%, respectively Bacillus thuringiensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Bacillus thuringiensis