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Literature summary extracted from

  • Baffa Junior, J.; Viana, P.; de Rezende, S.; Soares, N.; Guimaraes, V.
    Immobilization of an alpha-galactosidase from Debaryomyces hansenni UFV-1 in cellulose film and its application in oligosaccharides hydrolysis (2018), Food Bioprod. Process., 111, 30-36 .
No PubMed abstract available

General Stability

EC Number General Stability Organism
3.2.1.22 enzyme immobilization in a cellulose film preserves 97% of the initial enzyme activity. The enzyme maintains above 80% of its original activity after 10 consecutive reuses of the film Debaryomyces hansenii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.22 0.47
-
 4-nitrophenyl alpha-D-galactopyranoside immobilized enzyme, at pH 5.0 and 40°C Debaryomyces hansenii
3.2.1.22 9.13
-
 stachyose immobilized enzyme, at pH 5.0 and 40°C Debaryomyces hansenii
3.2.1.22 20.1
-
 raffinose immobilized enzyme, at pH 5.0 and 40°C Debaryomyces hansenii

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.22 Debaryomyces hansenii
-
-
-
3.2.1.22 Debaryomyces hansenii UFV-1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.22 partial purification by DEAE-Sepharose column chromatography Debaryomyces hansenii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.22 3.03
-
 lyophilized extract, at pH 5.0 and 40°C Debaryomyces hansenii
3.2.1.22 87.52
-
 after 28.88fold purification, at pH 5.0 and 40°C Debaryomyces hansenii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.22 4-nitrophenyl alpha-D-galactopyranoside + H2O
-
 Debaryomyces hansenii 4-nitrophenol + alpha-D-galactopyranose
-
 ?
3.2.1.22 4-nitrophenyl alpha-D-galactopyranoside + H2O
-
 Debaryomyces hansenii UFV-1 4-nitrophenol + alpha-D-galactopyranose
-
 ?
3.2.1.22 raffinose + H2O best substrate Debaryomyces hansenii sucrose + D-galactose
-
 ?
3.2.1.22 raffinose + H2O best substrate Debaryomyces hansenii UFV-1 sucrose + D-galactose
-
 ?
3.2.1.22 stachyose + H2O
-
 Debaryomyces hansenii 2 D-galactose + sucrose
-
 ?
3.2.1.22 stachyose + H2O
-
 Debaryomyces hansenii UFV-1 2 D-galactose + sucrose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.22 Alpha-D-galactoside galactohydrolase
-
 Debaryomyces hansenii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.22 60
-
 free enzyme Debaryomyces hansenii
3.2.1.22 85
-
 immobilized enzyme Debaryomyces hansenii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.22 65 85 about 65% of the maximal activity of the immobilized enzyme is detected between 65 and 85°C. At temperatures above 90°C, a sharp decrease in the enzymatic activity is observed Debaryomyces hansenii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.22 45 95 the immobilized enzyme retains 100% of its activity when incubated at 45 and 65°C for 24 h. The half-lifes of the immobilized enzyme at 45, 65, 85 and 95°C are 4.4 h, 4.2 h, 3.9 h and 0.12 h, respectively. The enzyme has 75% of its activity after pre-incubation at 85°C for 30 h Debaryomyces hansenii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.22 4
-
 immobilized enzyme Debaryomyces hansenii
3.2.1.22 5
-
 free enzyme Debaryomyces hansenii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.22 4 6.5 over 60% activity of the immobilized enzyme is determined between 4.0 and 6.5 Debaryomyces hansenii