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Literature summary for 3.2.1.14 extracted from

  • Garcia-Fraga, B.; da Silva, A.F.
    Lopez-Seijas, J.; Sieiro, C.: Functional expression and characterization of a chitinase from the marine archaeon Halobacterium salinarum CECT 395 in Escherichia coli (2013), Appl. Microbiol. Biotechnol., 98, 2133-2143.
    View publication on PubMed
Search for more literature for 3.2.1.14

Application

Application Comment Organism
degradation exo-acting enzyme with potential interest regarding the biodegradation of chitin waste or its bioconversion into biologically active products Halobacterium salinarum

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Halobacterium salinarum

Inhibitors

Inhibitors Comment Organism Structure
Mn2+ 5 mM, 40°C, pH 7.3, 81% loss of activity Halobacterium salinarum

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 5 mM, 40°C, pH 7.3, 1.18fold activation Halobacterium salinarum
K+ 5 mM, 40°C, pH 7.3, 1.21fold activation Halobacterium salinarum
Mg2+ 5 mM, 40°C, pH 7.3, 1.32fold activation Halobacterium salinarum
NaCl the enzyme is salt-dependent with its highest activity in the presence of 1.5 M of NaCl, but retains 20% of its activity in the absence of salt Halobacterium salinarum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66500
-
-
 Halobacterium salinarum

Organism

Organism UniProt Comment Textmining
Halobacterium salinarum
-
-
-
Halobacterium salinarum CECT 395
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Halobacterium salinarum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.513
-
 pH 7.3, 40°C Halobacterium salinarum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-N,N',N''-triacetylchitotrioside + H2O
-
 Halobacterium salinarum 4-nitrophenol + N,N',N''-triacetylchitotriose
-
 ?
4-nitrophenyl beta-N,N',N''-triacetylchitotrioside + H2O
-
 Halobacterium salinarum CECT 395 4-nitrophenol + N,N',N''-triacetylchitotriose
-
 ?
4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
-
 Halobacterium salinarum p-nitrophenol + N-acetyl-D-glucosamine
-
 ?
4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
-
 Halobacterium salinarum CECT 395 p-nitrophenol + N-acetyl-D-glucosamine
-
 ?
colloidal chitin + H2O
-
 Halobacterium salinarum ?
-
 ?
colloidal chitin + H2O
-
 Halobacterium salinarum CECT 395 ?
-
 ?
crystalline chitin + H2O
-
 Halobacterium salinarum ?
-
 ?
crystalline chitin + H2O
-
 Halobacterium salinarum CECT 395 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 66500, SDS-PAGE Halobacterium salinarum

Synonyms

Synonyms Comment Organism
HschiA1
-
 Halobacterium salinarum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 purified recombinant enzyme, determined in 50 mM Tris–HCl buffer at pH 8 with 1.5 M NaCl Halobacterium salinarum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 45 30°C: about 50% of maximal activity, 45°C: about 70% of maximal activity Halobacterium salinarum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
 40 min, 10% loss of activity Halobacterium salinarum
45
-
 40 min, 35% loss of activity Halobacterium salinarum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 purified recombinant enzyme Halobacterium salinarum

pH Range

pH Minimum pH Maximum Comment Organism
6 8 pH 6.0: about 40% of maximal activity, pH 8.0: about 70% of maximal activity Halobacterium salinarum

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.5 8.5 the enzyme maintains over 90% of its activity after 40 min Halobacterium salinarum