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Literature summary extracted from

  • Borriss, R.; Olsen, O.; Thomsen, K.K.; von Wettstein, D.
    Hybrid Bacillus endo-(1-3,1-4)-beta-glucanases: construction of recombinant genes and molecular properties of the gene products (1989), Carlsberg Res. Commun., 54, 41-54.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, expression in Escherichia coli Bacillus amyloliquefaciens
3.2.1.73 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, expression in Escherichia coli Paenibacillus macerans

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 additional information construction of hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens. Hybrid enzyme H1 exhibits increased thermostability especially in an acidic environment compared to both parental enzymes. Hybrid enzyme H2 is more thermolabile than the naturally occuring beta-glucanases Bacillus amyloliquefaciens
3.2.1.73 additional information construction of hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens. Hybrid enzyme H1 exhibits increased thermostability especially in an acidic environment compared to both parental enzymes. Hybrid enzyme H2 is more thermolabile than the naturally occuring beta-glucanases Paenibacillus macerans

General Stability

EC Number General Stability Organism
3.2.1.73 Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation Bacillus amyloliquefaciens
3.2.1.73 Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation Paenibacillus macerans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.73 additional information
-
 additional information
-
 Bacillus amyloliquefaciens
3.2.1.73 additional information
-
 additional information
-
 Paenibacillus macerans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Bacillus amyloliquefaciens
-
 parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
3.2.1.73 Paenibacillus macerans
-
 parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.73 parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens Bacillus amyloliquefaciens
3.2.1.73 parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens Paenibacillus macerans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.73 10.4
-
 hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens Bacillus amyloliquefaciens
3.2.1.73 10.4
-
 hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens Paenibacillus macerans
3.2.1.73 1330
-
-
 Bacillus amyloliquefaciens
3.2.1.73 3722
-
 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase Bacillus amyloliquefaciens
3.2.1.73 3722
-
 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase Paenibacillus macerans
3.2.1.73 5030
-
-
 Paenibacillus macerans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 beta-D-glucan + H2O beta-D-glucan from barley Bacillus amyloliquefaciens additional information
-
 ?
3.2.1.73 beta-D-glucan + H2O beta-D-glucan from barley Paenibacillus macerans additional information
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus amyloliquefaciens ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Paenibacillus macerans ?
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.73 additional information
-
 Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation Bacillus amyloliquefaciens
3.2.1.73 additional information
-
 Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation Paenibacillus macerans
3.2.1.73 65
-
 half-life: 25 min Bacillus amyloliquefaciens
3.2.1.73 65
-
 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase is stable for more than 1 h at pH 5.5. The 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens irreversible thermoinactivated within 20-25 min Bacillus amyloliquefaciens
3.2.1.73 65
-
 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase is stable for more than 1 h at pH 5.5. The 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens irreversible thermoinactivated within 20-25 min Paenibacillus macerans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 5.6 6.6
-
 Bacillus amyloliquefaciens
3.2.1.73 5.6 6.6 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase Paenibacillus macerans
3.2.1.73 6 7
-
 Bacillus amyloliquefaciens
3.2.1.73 6 7.5
-
 Paenibacillus macerans

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.73 3.5 7 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase, stable Bacillus amyloliquefaciens
3.2.1.73 3.5 7 hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase, stable Paenibacillus macerans
3.2.1.73 4.8 6 stable Bacillus amyloliquefaciens
3.2.1.73 4.8 6.4 stable Paenibacillus macerans
3.2.1.73 5.6 6 hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, stable Bacillus amyloliquefaciens
3.2.1.73 5.6 6 hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, stable Paenibacillus macerans