Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Alagoez, D.; Yildirim, D.; Guevenmez, H.K.; Sihay, D.; Tuekel, S.S.
    Covalent immobilization and characterization of a novel pullulanase from Fontibacillus sp. strain DSHK 107 onto Florisil and nano-silica for pullulan hydrolysis (2016), Appl. Biochem. Biotechnol., 179, 1262-1274 .
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.2.1.41 the pullulanases immobilized on Florisil and nano-silica protected 71% and 90% of their initial activities after 10 reuses Fontibacillus sp. DSHK 107

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.41 additional information
-
 pullulan pH 5.0, 30°C, the apparent kcat/Km-values are 1.49, 1.54, and 0.59 mg/ml pullunan, respectively, for the soluble enzyme and pullulanase immobilized on Florisil and nano-silica Fontibacillus sp. DSHK 107

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.41 Fontibacillus sp. DSHK 107
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.41 partial Fontibacillus sp. DSHK 107

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.41 pullulan + H2O
-
 Fontibacillus sp. DSHK 107 ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.41 35
-
 soluble enzyme and immobilized pullulanases on Florisil and nano-silica through glutaraldehyde spacer arm Fontibacillus sp. DSHK 107

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.41 35
-
 t1/2 of soluble enzyme: 8.9 min. Thermal stability of pullulanase immobilized on Florisil and nano-silica is enhanced 6.5- and 15.6fold Fontibacillus sp. DSHK 107
3.2.1.41 50
-
 t1/2 of soluble enzyme: 6.2 min. Thermal stability of pullulanase immobilized on Florisil and nano-silica is enhanced 6.6- and 16.0fold Fontibacillus sp. DSHK 107

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.41 5
-
 immobilized pullulanases on Florisil and nano-silica through glutaraldehyde spacer arm Fontibacillus sp. DSHK 107
3.2.1.41 6
-
 soluble enzyme Fontibacillus sp. DSHK 107

General Information

EC Number General Information Comment Organism
3.2.1.41 additional information pullulanase partially purified from Fontibacillus sp. is covalently immobilized on Florisil and nano-silica through both glutaraldehyde and (3-glycidyloxypropyl)trimethoxysilane spacer arms. The pullulanase immobilized on Florisil and nano-silica through glutaraldehyde spacer arm show 85% and 190% activity of its free form, respectively, whereas no activity is observed when it is immobilized on the same supports through (3-glycidyloxypropyl)trimethoxysilane spacer arm Fontibacillus sp. DSHK 107