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β-Galactosidase hydrolyses terminal β(1,4)-Galactose linkages


Item Id: FSB5001
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100 Units [$99]
500 Units [$279]
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β(1,4)-Galactosidase From Aspergillus oryzae 

High-grade enzyme optimized for glycobiology applications

Multiple chromatography steps yield an exceptionally high grade product form of β-galactosidase from Aspergillus oryzae for glycobiology applications. The enzyme catalyzes the rapid hydrolysis of terminal β(1,4)-galactoside linkages biantennary type N-glycans, but displays no activity towards β(1,3) linked terminal galactoside equivalents, a characteristic uncommon to other commercially available β-galactosidases. β-galactosidase is also a proven catalyst for the hydrolysis of plant polysaccharides (e.g. galactomannan) and catalyzes the reverse reaction to form polymers of galactose and synthetic conjugates under specific conditions. 


Quantity100 Units
Specific Activity>170 U/mg
Purity>95% by SDS-PAGE
Molecular Weight109.9 kDaltons (Calculated)
Extinction coefficient1 mg/ml = 1.75/cm path length (Calculated) at 280 nm
Theoretical pI5.33
Storage Format: Lyophilized powder
Temperature: 2-8C.
Stability: 1 year
Units One unit is defined as the quantity of enzyme that will hydrolyze one μmole of an ο-nitrophenol-β-D-galactopyranoside to o-nitrophenol and D-galactose per minute at 37C and a pH 4.5. This unit is based on a 15-minute assay.


1. Tanaka, Y, Kagamiishi, A, Kiuchi, A, Horiuchi, T.J (1975) Purification and properties of beta-galactosidase from Aspergillus oryzae. Biochem. 1;77(1?):241-7 

2. Zeleny, R., Altmann, F., Praznik, W. (1997) A Capillary Electrophoretic Study on the Specificity of β-Galactosidases from Aspergillus oryzae, Escherichia coli, Streptococcus pneumoniae,and Canavalia ensiformis (Jack Bean). Anal. Biochem., 246(1):96-101 

3. Miller, J. (1972) Experiments in Molecular Genetics, p. 352-355. Cold Spring Harbor Laboratory, NY.

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