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Literature summary extracted from

  • Goldenkova-Pavlova, I.V.; Tyurin, A.A.; Mustafaev, O.N.
    The features that distinguish lichenases from other polysaccharide-hydrolyzing enzymes and the relevance of lichenases for biotechnological applications (2018), Appl. Microbiol. Biotechnol., 102, 3951-3965 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.73 food industry the enzyme is used for production and processing of alcoholic beverages Bacillus subtilis
3.2.1.73 food industry the enzyme is used for production of oligomers as prebiotics Paenibacillus barcinonensis
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Ruminococcus albus
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus altitudinis
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus amyloliquefaciens
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Brevibacillus brevis
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Niallia circulans
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus licheniformis
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus velezensis
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus sp. A3
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus sp. N137
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus sp. SJ-10
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus pumilus
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus subtilis
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Bacillus tequilensis
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production Acetivibrio thermocellus
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Fibrobacter succinogenes
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel/bioethanol production Paenibacillus barcinonensis
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Paenibacillus barengoltzii
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Paenibacillus macerans
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Paenibacillus polymyxa
3.2.1.73 additional information application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production Rhodothermus marinus
3.2.1.73 synthesis the enzyme can be used in the production of anti-hypercholesterolemic agents Niallia circulans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 gene beg1, recombinant expression in Saccharomyces cerevisiae, the enzyme is secreted Bacillus subtilis
3.2.1.73 gene bg1, recombinant expression in Escherichia coli and in Pichia pastoris Bacillus licheniformis
3.2.1.73 gene bga1, recombinant expression in Escherichia coli, the enzyme is secreted Bacillus sp. N137
3.2.1.73 gene bgc, recombinant expression in Bacillus subtilis and in Bacillus megaterium Niallia circulans
3.2.1.73 gene bgi, recombinant expression in Escherichia coli, the enzyme is secreted Bacillus sp. A3
3.2.1.73 gene bgi, recombinant expression in Escherichia coli, the enzyme is secreted Paenibacillus macerans
3.2.1.73 gene bgl, recombinant expression in Escherichia coli, the enzyme is secreted Bacillus amyloliquefaciens
3.2.1.73 gene bgl5-1, recombinant expression in Escherichia coli, the enzyme is secreted Bacillus tequilensis
3.2.1.73 gene bglA, recombinant expression in Escherichia coli Rhodothermus marinus
3.2.1.73 gene bglBB, recombinant expression in Escherichia coli, the enzyme is secreted Brevibacillus brevis
3.2.1.73 gene bglS, recombinant expression in Escherichia coli Ruminococcus albus
3.2.1.73 gene bglS, recombinant expression in Escherichia coli, in Saccharomyces cerevisiae, in plants, and in mammalian cells, the enzyme is secreted Acetivibrio thermocellus
3.2.1.73 gene bglS, recombinant expression in Saccharomyces cerevisiae Bacillus subtilis
3.2.1.73 gene FSU_0226, recombinant expression in Escherichia coli and in Pichia pastoris Fibrobacter succinogenes
3.2.1.73 gene gcs2, recombinant expression in Escherichia coli, the enzyme is secreted Bacillus velezensis
3.2.1.73 gene lic16A, recombinant expression in Escherichia coli Paenibacillus barcinonensis
3.2.1.73 gene licB, recombinant expression in Escherichia coli and in Pichia pastoris Acetivibrio thermocellus
3.2.1.73 gene US8_01508, recombinant expression in Escherichia coli, the enzyme is secreted Bacillus altitudinis
3.2.1.73 recombinant expression in Escherichia coli Bacillus sp. SJ-10
3.2.1.73 recombinant expression in Escherichia coli Bacillus subtilis
3.2.1.73 recombinant expression in Escherichia coli Paenibacillus barengoltzii
3.2.1.73 recombinant expression in Escherichia coli and in Pichia pastoris Bacillus subtilis
3.2.1.73 recombinant expression in Escherichia coli, and in Mus musculus, and in Sus scrofa parotid gland Paenibacillus polymyxa
3.2.1.73 recombinant expression, the enzyme is secreted Bacillus pumilus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 additional information end-to-end fusion by cyclization with SpyTag/SpyCatcher, and oligomerization by Foldon Bacillus subtilis
3.2.1.73 additional information rational design of disulfide bonds in the enzyme by site-directed mutagenesis Bacillus tequilensis
3.2.1.73 additional information end-to-end fusion, circular permutation, domain insertion Acetivibrio thermocellus
3.2.1.73 additional information end-to-end fusion, site-directed mutagenesis Fibrobacter succinogenes
3.2.1.73 additional information end-to-end fusion Paenibacillus macerans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.73 barley beta-glucan + H2O Niallia circulans
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus licheniformis
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus velezensis
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus sp. SJ-10
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus pumilus
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus subtilis
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus tequilensis
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Acetivibrio thermocellus
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Paenibacillus barcinonensis
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Paenibacillus barengoltzii
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Paenibacillus macerans
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus subtilis 168
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Niallia circulans ATCC 21367
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus subtilis MA139
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Acetivibrio thermocellus F7
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus tequilensis CGX5-1
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus subtilis SU40
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus velezensis S2
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus pumilus US570
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Bacillus subtilis NCIB 8565
-
 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O Paenibacillus barcinonensis BP-23
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Rhodothermus marinus
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Acetivibrio thermocellus
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Acetivibrio thermocellus ATCC 27405
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Acetivibrio thermocellus DSM 1237
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Acetivibrio thermocellus NBRC 103400
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Acetivibrio thermocellus NCIMB 10682
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Acetivibrio thermocellus NRRL B-4536
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Acetivibrio thermocellus VPI 7372
-
 ?
-
 ?
3.2.1.73 beta-glucan + H2O Rhodothermus marinus ITI378
-
 ?
-
 ?
3.2.1.73 laminarin + H2O Rhodothermus marinus
-
 ?
-
 ?
3.2.1.73 laminarin + H2O Rhodothermus marinus ITI378
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Ruminococcus albus
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus altitudinis
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus amyloliquefaciens
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Brevibacillus brevis
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus licheniformis
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus velezensis
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus sp. A3
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus sp. N137
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus pumilus
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus subtilis
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus tequilensis
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Acetivibrio thermocellus
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Fibrobacter succinogenes
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Paenibacillus barcinonensis
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Paenibacillus macerans
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Rhodothermus marinus
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus subtilis 168
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Ruminococcus albus 8
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus subtilis MA139
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Acetivibrio thermocellus F7
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Acetivibrio thermocellus ATCC 27405
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Fibrobacter succinogenes S85
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus amyloliquefaciens ATCC 23350
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Acetivibrio thermocellus DSM 1237
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus tequilensis CGX5-1
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus subtilis SU40
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus altitudinis YC-9
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus amyloliquefaciens ATCC 15841
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Acetivibrio thermocellus NBRC 103400
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Acetivibrio thermocellus NCIMB 10682
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Acetivibrio thermocellus NRRL B-4536
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Acetivibrio thermocellus VPI 7372
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Brevibacillus brevis ALK36
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus velezensis S2
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Bacillus pumilus US570
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Paenibacillus barcinonensis BP-23
-
 ?
-
 ?
3.2.1.73 lichenan + H2O Rhodothermus marinus ITI378
-
 ?
-
 ?
3.2.1.73 lichenin + H2O Paenibacillus barengoltzii
-
 ?
-
 ?
3.2.1.73 additional information Ruminococcus albus lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus altitudinis lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus amyloliquefaciens lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Brevibacillus brevis lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Niallia circulans lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus licheniformis lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus velezensis lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus sp. A3 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus sp. N137 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus sp. SJ-10 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus pumilus lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus subtilis lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus tequilensis lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Acetivibrio thermocellus lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Fibrobacter succinogenes lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Paenibacillus barcinonensis lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Paenibacillus barengoltzii lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Paenibacillus macerans lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Paenibacillus polymyxa lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Rhodothermus marinus lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus subtilis 168 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Ruminococcus albus 8 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Niallia circulans ATCC 21367 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus subtilis MA139 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Acetivibrio thermocellus F7 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Acetivibrio thermocellus ATCC 27405 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Fibrobacter succinogenes S85 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus amyloliquefaciens ATCC 23350 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Acetivibrio thermocellus DSM 1237 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus tequilensis CGX5-1 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus subtilis SU40 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus altitudinis YC-9 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus amyloliquefaciens ATCC 15841 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Acetivibrio thermocellus NBRC 103400 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Acetivibrio thermocellus NCIMB 10682 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Acetivibrio thermocellus NRRL B-4536 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Acetivibrio thermocellus VPI 7372 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Brevibacillus brevis ALK36 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus velezensis S2 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus pumilus US570 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Bacillus subtilis NCIB 8565 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Paenibacillus barcinonensis BP-23 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Paenibacillus polymyxa CP7 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 additional information Rhodothermus marinus ITI378 lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan ?
-
 ?
3.2.1.73 oat beta-glucan + H2O Bacillus amyloliquefaciens
-
 ?
-
 ?
3.2.1.73 oat beta-glucan + H2O Bacillus tequilensis
-
 ?
-
 ?
3.2.1.73 oat beta-glucan + H2O Paenibacillus barengoltzii
-
 ?
-
 ?
3.2.1.73 oat beta-glucan + H2O Bacillus amyloliquefaciens ATCC 23350
-
 ?
-
 ?
3.2.1.73 oat beta-glucan + H2O Bacillus tequilensis CGX5-1
-
 ?
-
 ?
3.2.1.73 plant beta-glucan + H2O Paenibacillus polymyxa
-
 ?
-
 ?
3.2.1.73 plant beta-glucan + H2O Paenibacillus polymyxa CP7
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Acetivibrio thermocellus Q84C00 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Acetivibrio thermocellus A3DBX3 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Acetivibrio thermocellus ATCC 27405 A3DBX3 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Acetivibrio thermocellus DSM 1237 A3DBX3 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Acetivibrio thermocellus F7 Q84C00 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Acetivibrio thermocellus NBRC 103400 A3DBX3 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Acetivibrio thermocellus NCIMB 10682 A3DBX3 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Acetivibrio thermocellus NRRL B-4536 A3DBX3 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Acetivibrio thermocellus VPI 7372 A3DBX3 i.e. Ruminiclostridium thermocellum
-
3.2.1.73 Bacillus altitudinis
-
-
-
3.2.1.73 Bacillus altitudinis YC-9
-
-
-
3.2.1.73 Bacillus amyloliquefaciens
-
-
-
3.2.1.73 Bacillus amyloliquefaciens P07980 i.e. Bacillus velezensis
-
3.2.1.73 Bacillus amyloliquefaciens ATCC 15841 P07980 i.e. Bacillus velezensis
-
3.2.1.73 Bacillus amyloliquefaciens ATCC 23350
-
-
-
3.2.1.73 Bacillus licheniformis P27051
-
-
3.2.1.73 Bacillus pumilus A0A0F6QU36
-
-
3.2.1.73 Bacillus pumilus US570 A0A0F6QU36
-
-
3.2.1.73 Bacillus sp. A3 Q6YAT3
-
-
3.2.1.73 Bacillus sp. N137 Q45648
-
-
3.2.1.73 Bacillus sp. SJ-10 I1W007
-
-
3.2.1.73 Bacillus subtilis A8CGP1
-
-
3.2.1.73 Bacillus subtilis G0YW23
-
-
3.2.1.73 Bacillus subtilis P04957
-
-
3.2.1.73 Bacillus subtilis Q45691
-
-
3.2.1.73 Bacillus subtilis 168 P04957
-
-
3.2.1.73 Bacillus subtilis MA139 A8CGP1
-
-
3.2.1.73 Bacillus subtilis NCIB 8565 Q45691
-
-
3.2.1.73 Bacillus subtilis SU40 G0YW23
-
-
3.2.1.73 Bacillus tequilensis K0A689
-
-
3.2.1.73 Bacillus tequilensis CGX5-1 K0A689
-
-
3.2.1.73 Bacillus velezensis A0A0M4NIK2 i.e. Bacillus amyloliquefaciens subsp. plantarum or Bacillus velezensis
-
3.2.1.73 Bacillus velezensis S2 A0A0M4NIK2 i.e. Bacillus amyloliquefaciens subsp. plantarum or Bacillus velezensis
-
3.2.1.73 Brevibacillus brevis P37073
-
-
3.2.1.73 Brevibacillus brevis ALK36 P37073
-
-
3.2.1.73 Fibrobacter succinogenes P17989
-
-
3.2.1.73 Fibrobacter succinogenes S85 P17989
-
-
3.2.1.73 Niallia circulans P19254
-
-
3.2.1.73 Niallia circulans ATCC 21367 P19254
-
-
3.2.1.73 Paenibacillus barcinonensis A0A097QQT4
-
-
3.2.1.73 Paenibacillus barcinonensis BP-23 A0A097QQT4
-
-
3.2.1.73 Paenibacillus barengoltzii A0A0K1P4J7
-
-
3.2.1.73 Paenibacillus macerans Q846Q0
-
-
3.2.1.73 Paenibacillus polymyxa A9Z0X6
-
-
3.2.1.73 Paenibacillus polymyxa CP7 A9Z0X6
-
-
3.2.1.73 Rhodothermus marinus P45798 i.e. Rhodothermus obamensis
-
3.2.1.73 Rhodothermus marinus ITI378 P45798 i.e. Rhodothermus obamensis
-
3.2.1.73 Ruminococcus albus E9SCT3
-
-
3.2.1.73 Ruminococcus albus 8 E9SCT3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 barley beta-glucan + H2O
-
 Niallia circulans ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus licheniformis ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus velezensis ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus sp. SJ-10 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus pumilus ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus subtilis ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus tequilensis ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Acetivibrio thermocellus ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Paenibacillus barcinonensis ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Paenibacillus barengoltzii ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Paenibacillus macerans ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus subtilis 168 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Niallia circulans ATCC 21367 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus subtilis MA139 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Acetivibrio thermocellus F7 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus tequilensis CGX5-1 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus subtilis SU40 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus velezensis S2 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus pumilus US570 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Bacillus subtilis NCIB 8565 ?
-
 ?
3.2.1.73 barley beta-glucan + H2O
-
 Paenibacillus barcinonensis BP-23 ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Rhodothermus marinus ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Acetivibrio thermocellus ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Acetivibrio thermocellus ATCC 27405 ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Acetivibrio thermocellus DSM 1237 ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Acetivibrio thermocellus NBRC 103400 ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Acetivibrio thermocellus NCIMB 10682 ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Acetivibrio thermocellus NRRL B-4536 ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Acetivibrio thermocellus VPI 7372 ?
-
 ?
3.2.1.73 beta-glucan + H2O
-
 Rhodothermus marinus ITI378 ?
-
 ?
3.2.1.73 carboxymethylcellulose + H2O
-
 Bacillus velezensis ?
-
 ?
3.2.1.73 carboxymethylcellulose + H2O
-
 Bacillus velezensis S2 ?
-
 ?
3.2.1.73 laminarin + H2O
-
 Rhodothermus marinus ?
-
 ?
3.2.1.73 laminarin + H2O
-
 Rhodothermus marinus ITI378 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Ruminococcus albus ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus altitudinis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus amyloliquefaciens ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Brevibacillus brevis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus licheniformis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus velezensis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus sp. A3 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus sp. N137 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus pumilus ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus subtilis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus tequilensis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Fibrobacter succinogenes ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Paenibacillus barcinonensis ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Paenibacillus macerans ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Rhodothermus marinus ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus subtilis 168 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Ruminococcus albus 8 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus subtilis MA139 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus F7 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus ATCC 27405 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Fibrobacter succinogenes S85 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus amyloliquefaciens ATCC 23350 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus DSM 1237 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus tequilensis CGX5-1 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus subtilis SU40 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus altitudinis YC-9 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus amyloliquefaciens ATCC 15841 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus NBRC 103400 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus NCIMB 10682 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus NRRL B-4536 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus VPI 7372 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Brevibacillus brevis ALK36 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus velezensis S2 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus pumilus US570 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Paenibacillus barcinonensis BP-23 ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Rhodothermus marinus ITI378 ?
-
 ?
3.2.1.73 lichenin + H2O
-
 Paenibacillus barengoltzii ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Ruminococcus albus ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus altitudinis ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus amyloliquefaciens ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Brevibacillus brevis ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Niallia circulans ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus licheniformis ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus velezensis ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus sp. A3 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus sp. N137 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus sp. SJ-10 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus pumilus ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus subtilis ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus tequilensis ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Acetivibrio thermocellus ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Fibrobacter succinogenes ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Paenibacillus barcinonensis ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Paenibacillus barengoltzii ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Paenibacillus macerans ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Paenibacillus polymyxa ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Rhodothermus marinus ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Ruminococcus albus ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus altitudinis ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus amyloliquefaciens ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Brevibacillus brevis ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Niallia circulans ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus licheniformis ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus velezensis ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus sp. A3 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus sp. N137 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus sp. SJ-10 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus pumilus ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus subtilis ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus tequilensis ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Acetivibrio thermocellus ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Fibrobacter succinogenes ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Paenibacillus barcinonensis ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Paenibacillus barengoltzii ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Paenibacillus macerans ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Paenibacillus polymyxa ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Rhodothermus marinus ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus subtilis 168 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus subtilis 168 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Ruminococcus albus 8 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Ruminococcus albus 8 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Niallia circulans ATCC 21367 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Niallia circulans ATCC 21367 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus subtilis MA139 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus subtilis MA139 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Acetivibrio thermocellus F7 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Acetivibrio thermocellus F7 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Acetivibrio thermocellus ATCC 27405 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Acetivibrio thermocellus ATCC 27405 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Fibrobacter succinogenes S85 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Fibrobacter succinogenes S85 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus amyloliquefaciens ATCC 23350 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus amyloliquefaciens ATCC 23350 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Acetivibrio thermocellus DSM 1237 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Acetivibrio thermocellus DSM 1237 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus tequilensis CGX5-1 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus tequilensis CGX5-1 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus subtilis SU40 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus subtilis SU40 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus altitudinis YC-9 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus altitudinis YC-9 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus amyloliquefaciens ATCC 15841 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus amyloliquefaciens ATCC 15841 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Acetivibrio thermocellus NBRC 103400 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Acetivibrio thermocellus NBRC 103400 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Acetivibrio thermocellus NCIMB 10682 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Acetivibrio thermocellus NCIMB 10682 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Acetivibrio thermocellus NRRL B-4536 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Acetivibrio thermocellus NRRL B-4536 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Acetivibrio thermocellus VPI 7372 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Acetivibrio thermocellus VPI 7372 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Brevibacillus brevis ALK36 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Brevibacillus brevis ALK36 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus velezensis S2 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus pumilus US570 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus pumilus US570 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Bacillus subtilis NCIB 8565 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Bacillus subtilis NCIB 8565 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Paenibacillus barcinonensis BP-23 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Paenibacillus barcinonensis BP-23 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Paenibacillus polymyxa CP7 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Paenibacillus polymyxa CP7 ?
-
 ?
3.2.1.73 additional information lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan Rhodothermus marinus ITI378 ?
-
 ?
3.2.1.73 additional information beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds Rhodothermus marinus ITI378 ?
-
 ?
3.2.1.73 oat beta-glucan + H2O
-
 Bacillus amyloliquefaciens ?
-
 ?
3.2.1.73 oat beta-glucan + H2O
-
 Bacillus tequilensis ?
-
 ?
3.2.1.73 oat beta-glucan + H2O
-
 Paenibacillus barengoltzii ?
-
 ?
3.2.1.73 oat beta-glucan + H2O
-
 Bacillus amyloliquefaciens ATCC 23350 ?
-
 ?
3.2.1.73 oat beta-glucan + H2O
-
 Bacillus tequilensis CGX5-1 ?
-
 ?
3.2.1.73 oat gum + H2O
-
 Bacillus velezensis ?
-
 ?
3.2.1.73 oat gum + H2O
-
 Bacillus velezensis S2 ?
-
 ?
3.2.1.73 plant beta-glucan + H2O
-
 Paenibacillus polymyxa ?
-
 ?
3.2.1.73 plant beta-glucan + H2O
-
 Paenibacillus polymyxa CP7 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 Beg1
-
 Bacillus subtilis
3.2.1.73 beta-1,3-1,4-glucanase
-
 Ruminococcus albus
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus altitudinis
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus amyloliquefaciens
3.2.1.73 beta-1,3-1,4-glucanase
-
 Brevibacillus brevis
3.2.1.73 beta-1,3-1,4-glucanase
-
 Niallia circulans
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus licheniformis
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus velezensis
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus sp. A3
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus sp. N137
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus sp. SJ-10
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus pumilus
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus subtilis
3.2.1.73 beta-1,3-1,4-glucanase
-
 Bacillus tequilensis
3.2.1.73 beta-1,3-1,4-glucanase
-
 Acetivibrio thermocellus
3.2.1.73 beta-1,3-1,4-glucanase
-
 Fibrobacter succinogenes
3.2.1.73 beta-1,3-1,4-glucanase
-
 Paenibacillus barcinonensis
3.2.1.73 beta-1,3-1,4-glucanase
-
 Paenibacillus barengoltzii
3.2.1.73 beta-1,3-1,4-glucanase
-
 Paenibacillus macerans
3.2.1.73 beta-1,3-1,4-glucanase
-
 Paenibacillus polymyxa
3.2.1.73 beta-1,3-1,4-glucanase
-
 Rhodothermus marinus
3.2.1.73 beta-glucanase
-
 Acetivibrio thermocellus
3.2.1.73 BG1
-
 Bacillus licheniformis
3.2.1.73 Bga1
-
 Bacillus sp. N137
3.2.1.73 bgc
-
 Niallia circulans
3.2.1.73 bgi
-
 Bacillus sp. A3
3.2.1.73 bgi
-
 Paenibacillus macerans
3.2.1.73 Bgl
-
 Bacillus amyloliquefaciens
3.2.1.73 Bgl
-
 Bacillus licheniformis
3.2.1.73 bgl5-1
-
 Bacillus tequilensis
3.2.1.73 BglA
-
 Bacillus amyloliquefaciens
3.2.1.73 BglA
-
 Rhodothermus marinus
3.2.1.73 BglBB
-
 Brevibacillus brevis
3.2.1.73 bglBC1
-
 Niallia circulans
3.2.1.73 BglS
-
 Ruminococcus albus
3.2.1.73 BglS
-
 Bacillus subtilis
3.2.1.73 BglS
-
 Paenibacillus macerans
3.2.1.73 BglT
-
 Bacillus tequilensis
3.2.1.73 CP7 beta-1,3-1,4-glucanase
-
 Paenibacillus polymyxa
3.2.1.73 Cthe_0211
-
 Acetivibrio thermocellus
3.2.1.73 CtLic16A
-
 Acetivibrio thermocellus
3.2.1.73 E-LICHN
-
 Bacillus subtilis
3.2.1.73 Fisuc_2961
-
 Fibrobacter succinogenes
3.2.1.73 FSU_0226
-
 Fibrobacter succinogenes
3.2.1.73 Gcs2
-
 Bacillus velezensis
3.2.1.73 GluUS570
-
 Bacillus pumilus
3.2.1.73 lam1
-
 Acetivibrio thermocellus
3.2.1.73 Lic16A
-
 Paenibacillus barcinonensis
3.2.1.73 LicA
-
 Bacillus licheniformis
3.2.1.73 LicB
-
 Acetivibrio thermocellus
3.2.1.73 Lichenase
-
 Ruminococcus albus
3.2.1.73 Lichenase
-
 Bacillus altitudinis
3.2.1.73 Lichenase
-
 Bacillus amyloliquefaciens
3.2.1.73 Lichenase
-
 Brevibacillus brevis
3.2.1.73 Lichenase
-
 Niallia circulans
3.2.1.73 Lichenase
-
 Bacillus licheniformis
3.2.1.73 Lichenase
-
 Bacillus velezensis
3.2.1.73 Lichenase
-
 Bacillus sp. A3
3.2.1.73 Lichenase
-
 Bacillus sp. N137
3.2.1.73 Lichenase
-
 Bacillus sp. SJ-10
3.2.1.73 Lichenase
-
 Bacillus pumilus
3.2.1.73 Lichenase
-
 Bacillus subtilis
3.2.1.73 Lichenase
-
 Bacillus tequilensis
3.2.1.73 Lichenase
-
 Acetivibrio thermocellus
3.2.1.73 Lichenase
-
 Fibrobacter succinogenes
3.2.1.73 Lichenase
-
 Paenibacillus barcinonensis
3.2.1.73 Lichenase
-
 Paenibacillus barengoltzii
3.2.1.73 Lichenase
-
 Paenibacillus macerans
3.2.1.73 Lichenase
-
 Paenibacillus polymyxa
3.2.1.73 Lichenase
-
 Rhodothermus marinus
3.2.1.73 licM
-
 Paenibacillus macerans
3.2.1.73 LicS
-
 Bacillus subtilis
3.2.1.73 PbBglu16A
-
 Paenibacillus barengoltzii
3.2.1.73 Ra0505
-
 Ruminococcus albus
3.2.1.73 TF-glu
-
 Fibrobacter succinogenes
3.2.1.73 US8_01508
-
 Bacillus altitudinis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.73 35
-
-
 Bacillus velezensis
3.2.1.73 40
-
-
 Bacillus licheniformis
3.2.1.73 40
-
-
 Bacillus subtilis
3.2.1.73 40 55
-
 Paenibacillus polymyxa
3.2.1.73 45 60
-
 Bacillus tequilensis
3.2.1.73 50
-
-
 Bacillus amyloliquefaciens
3.2.1.73 50
-
-
 Bacillus sp. SJ-10
3.2.1.73 50
-
-
 Bacillus subtilis
3.2.1.73 50
-
-
 Fibrobacter succinogenes
3.2.1.73 55
-
-
 Bacillus pumilus
3.2.1.73 55
-
-
 Bacillus velezensis
3.2.1.73 55
-
-
 Paenibacillus barcinonensis
3.2.1.73 55
-
-
 Paenibacillus barengoltzii
3.2.1.73 60
-
-
 Bacillus subtilis
3.2.1.73 65
-
-
 Bacillus altitudinis
3.2.1.73 65 70
-
 Bacillus sp. N137
3.2.1.73 65 70
-
 Brevibacillus brevis
3.2.1.73 65
-
-
 Niallia circulans
3.2.1.73 65
-
-
 Paenibacillus macerans
3.2.1.73 70
-
-
 Acetivibrio thermocellus
3.2.1.73 70
-
-
 Bacillus amyloliquefaciens
3.2.1.73 80
-
-
 Acetivibrio thermocellus
3.2.1.73 85
-
-
 Rhodothermus marinus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.73 25 55 activity range Bacillus velezensis
3.2.1.73 30 70 activity range Bacillus sp. SJ-10
3.2.1.73 30 80 activity range Bacillus pumilus
3.2.1.73 40 80 activity range Acetivibrio thermocellus
3.2.1.73 40 70 activity range Bacillus licheniformis
3.2.1.73 45 70 activity range Bacillus velezensis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.73 30
-
 12 h, 50% activity remaining Bacillus licheniformis
3.2.1.73 30 70 80% activity remaining Bacillus sp. SJ-10
3.2.1.73 40 55 24 h, completely stable Bacillus velezensis
3.2.1.73 55
-
 3 h, 85% activity remaining Paenibacillus barcinonensis
3.2.1.73 55
-
 stable up to Paenibacillus barengoltzii
3.2.1.73 60
-
 2 h, 90% activity remaining Bacillus altitudinis
3.2.1.73 60
-
 1 h, 50% activity remaining Bacillus amyloliquefaciens
3.2.1.73 70
-
 4 h, 60% activity remaining Bacillus velezensis
3.2.1.73 70
-
 1 h, 80% activity remaining Bacillus sp. N137
3.2.1.73 70
-
 2 h, 70% activity remaining Bacillus pumilus
3.2.1.73 75
-
 1 h, 75% activity remaining Brevibacillus brevis
3.2.1.73 80
-
 30 min, 50% activity remaining Bacillus amyloliquefaciens
3.2.1.73 80
-
 10 min, 60% activity remaining Bacillus subtilis
3.2.1.73 80
-
 1 h, 54% activity remaining Bacillus subtilis
3.2.1.73 80
-
 4 h, 80% activity remaining Acetivibrio thermocellus
3.2.1.73 80
-
 16 h, completely stable Rhodothermus marinus
3.2.1.73 90
-
 10 min, 80% activity remaining Bacillus sp. A3

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 5
-
-
 Bacillus velezensis
3.2.1.73 5.6
-
-
 Bacillus licheniformis
3.2.1.73 6
-
-
 Bacillus altitudinis
3.2.1.73 6
-
-
 Bacillus amyloliquefaciens
3.2.1.73 6
-
-
 Niallia circulans
3.2.1.73 6
-
-
 Bacillus sp. SJ-10
3.2.1.73 6
-
-
 Bacillus pumilus
3.2.1.73 6
-
-
 Bacillus subtilis
3.2.1.73 6
-
-
 Bacillus tequilensis
3.2.1.73 6
-
-
 Fibrobacter succinogenes
3.2.1.73 6
-
-
 Paenibacillus barcinonensis
3.2.1.73 6
-
-
 Paenibacillus barengoltzii
3.2.1.73 6
-
-
 Acetivibrio thermocellus
3.2.1.73 6.4
-
-
 Bacillus subtilis
3.2.1.73 6.5
-
-
 Bacillus amyloliquefaciens
3.2.1.73 7
-
-
 Bacillus subtilis
3.2.1.73 7
-
-
 Paenibacillus macerans
3.2.1.73 7
-
-
 Rhodothermus marinus
3.2.1.73 7.5
-
-
 Bacillus velezensis
3.2.1.73 8
-
-
 Bacillus subtilis
3.2.1.73 8
-
-
 Acetivibrio thermocellus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.73 2 10 activity range Bacillus pumilus
3.2.1.73 3 6 activity range Paenibacillus polymyxa
3.2.1.73 3 10 activity range Fibrobacter succinogenes
3.2.1.73 3.5 9 activity range Paenibacillus barengoltzii
3.2.1.73 4 8 activity range Bacillus velezensis
3.2.1.73 4 9 activity range Bacillus sp. SJ-10
3.2.1.73 4 11 activity range Acetivibrio thermocellus
3.2.1.73 4.5 8 activity range Bacillus tequilensis
3.2.1.73 5 7 activity range Bacillus licheniformis
3.2.1.73 5 8 activity range Bacillus amyloliquefaciens
3.2.1.73 6 10 activity range Bacillus velezensis
3.2.1.73 6 12 activity range Bacillus sp. N137
3.2.1.73 8 10 activity range Brevibacillus brevis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.73 3.5 9 stable at Paenibacillus barengoltzii
3.2.1.73 4 9 80% activity remaining Bacillus sp. SJ-10

General Information

EC Number General Information Comment Organism
3.2.1.73 physiological function the enzyme protects plants against pathogenic fungi Bacillus velezensis