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Literature summary extracted from

  • Shi, Q.; Hou, Y.; Xu, Y.; Moerkeberg Krogh, K.B.R.; Tenkanen, M.
    Enzymatic analysis of levan produced by lactic acid bacteria in fermented doughs (2019), Carbohydr. Polym., 208, 285-293 .
    View publication on PubMed

Application

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.65 expressed in Bacillus subtilis Paenibacillus amylolyticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.80 fructan + H2O Paenibacillus amylolyticus
-
?
-
?

Organism

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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.65 phenyl Sepharose column chromatography and Q Sepharose chromatography Paenibacillus amylolyticus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.65 commercial preparation
-
Aspergillus niger
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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 ?
-
?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

EC Number General Information Comment Organism
3.2.1.65 evolution the enzyme belongs to the glycosyl hydrolase family 32, GH32 Aspergillus niger