EC Number | Application | Comment | Organism |
---|---|---|---|
3.2.1.65 | food industry | the enzyme is used for enzymatic analysis of levan produced by lactic acid bacteria in fermented doughs | Paenibacillus amylolyticus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.65 | expressed in Bacillus subtilis | Paenibacillus amylolyticus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.80 | fructan + H2O | Paenibacillus amylolyticus | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.7 | Aspergillus niger | O74641 | - |
- |
3.2.1.65 | Aspergillus niger | - |
- |
- |
3.2.1.65 | Paenibacillus amylolyticus | - |
- |
- |
3.2.1.80 | Paenibacillus amylolyticus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.65 | phenyl Sepharose column chromatography and Q Sepharose chromatography | Paenibacillus amylolyticus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.65 | commercial preparation | - |
Aspergillus niger | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.65 | additional information | - |
the levanase preparation exhibits an activity of 1116 U/ml towards levan | Aspergillus niger |
3.2.1.80 | additional information | - |
the levanase preparation exhibited an activity of 1116 U/ml towards levan | Paenibacillus amylolyticus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.7 | inulin + H2O | substrate from chicory, 23% and 85% hydrolysis at 40 and 400 U/g fructan, respectively, at pH 5.0, 30°C, in 24 h | Aspergillus niger | ? | - |
? | |
3.2.1.7 | additional information | no activity on commercial Erwinia levan or levan from Leuconostoc mesenteroides strain DSM 20343 | Aspergillus niger | ? | - |
? | |
3.2.1.65 | Erwinia herbicola levan + H2O | - |
Paenibacillus amylolyticus | D-fructose + fructooligosacchrides | - |
? | |
3.2.1.65 | levan + H2O | commercial Erwinia herbicola levan and levan from Leuconostoc mesenteroides DSM 20343-fermented fava bean doughs, combined activity of exoinulinase/levanase | Aspergillus niger | ? | - |
? | |
3.2.1.65 | additional information | in order to develop a specific analysis for levan in food matrices, a Paenibacillus amylolyticus endolevanase (EC 3.2.1.65) is combined with exoinulinase (EC 3.2.1.80) for levan hydrolysis achieving about 80% hydrolysis yield, method evaluation, and modelling. The levanase preparation exhibits an activity of 1116 U/ml towards levan and no activity towards inulin as determined by the reducing value method | Aspergillus niger | ? | - |
? | |
3.2.1.80 | fructan + H2O | - |
Paenibacillus amylolyticus | ? | - |
? | |
3.2.1.80 | levan + H2O | commercial Erwinia herbicola levan and levan from Leuconostoc mesenteroides DSM 20343-fermented fava bean doughs, combined activity of exoinulinase/levanase | Paenibacillus amylolyticus | ? | - |
? | |
3.2.1.80 | additional information | exo-beta-fructosidases, including exoinulinases (EC 3.2.1.80), can nonspecifically hydrolyze both beta-(2->1) and beta-(2->6)-linkages from the non-reducing end of fructooligosaccharides and fructans. In order to develop a specific analysis for levan in food matrices, a Paenibacillus amylolyticus endolevanase (EC 3.2.1.65) is combined with exoinulinase for levan hydrolysis achieving about 80% hydrolysis yield (19.1% for exoinulinase alone), method evaluation, and modelling. The levanase preparation exhibits an activity of 1116 U/ml towards levan and no activity towards inulin as determined by the reducing value method | Paenibacillus amylolyticus | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.7 | endoinulinase | - |
Aspergillus niger |
3.2.1.65 | endolevanase | - |
Aspergillus niger |
3.2.1.65 | endolevanase | - |
Paenibacillus amylolyticus |
3.2.1.80 | exoinulinase | - |
Paenibacillus amylolyticus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.7 | 30 | - |
assay at | Aspergillus niger |
3.2.1.65 | 30 | - |
assay at | Aspergillus niger |
3.2.1.80 | 30 | - |
assay at | Paenibacillus amylolyticus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.7 | 5 | - |
- |
Aspergillus niger |
3.2.1.65 | 6 | - |
- |
Aspergillus niger |
3.2.1.80 | 4 | - |
- |
Paenibacillus amylolyticus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.1.65 | evolution | the enzyme belongs to the glycosyl hydrolase family 32, GH32 | Aspergillus niger |