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

β(1,4)-Galactosidase

Item Id: FSB5001
Your Price:
$99.00
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Amount
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. 


Properties

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.



References

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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