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Purification and characterization of a β-glucosidase from aspergillus niger and its application in the hydrolysis of geniposide to genipin.
- Source :
-
Journal of microbiology and biotechnology [J Microbiol Biotechnol] 2014 Jun 28; Vol. 24 (6), pp. 788-94. - Publication Year :
- 2014
-
Abstract
- An extracellular β-glucosidase from Aspergillus niger Au0847 was purified to homogeneity by precipitation with ammonium sulfate, anion exchange, and gel filtration. The purified protein was composed of two subunits with molecular masses of 110 and 120 kDa. Au0847 β-glucosidase exhibited relatively high thermostability and pH stability, and its highest activity was obtained at 65°C and pH 4.6, respectively. As a potential metalloprotein, its enzymatic activity was potently stimulated by manganese ion and DTT. The β-glucosidase displayed avid affinity and high catalytic efficiency for geniposide. Au0847 β-glucosidase has potential value as an industrial enzyme for the hydrolysis of geniposide to genipin.
- Subjects :
- Aspergillus niger chemistry
Aspergillus niger genetics
Biotransformation
Enzyme Stability
Fungal Proteins genetics
Fungal Proteins metabolism
Glucosidases genetics
Glucosidases metabolism
Kinetics
Aspergillus niger enzymology
Fungal Proteins chemistry
Fungal Proteins isolation & purification
Glucosidases chemistry
Glucosidases isolation & purification
Iridoids chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1738-8872
- Volume :
- 24
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of microbiology and biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 24608563
- Full Text :
- https://doi.org/10.4014/jmb.1401.01053