ArticleSpringerPlus2013
β-galactosidase stability at high substrate concentrations.
Article in SpringerPlus, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 33 citations in OpenAlex.
- Advances in β-Galactosidase Research: A Systematic Review from Molecular Mechanisms to Enzyme Delivery Systems.Pharmaceutics · 2025Review
- Ultrasensitive and long-lasting bioluminescence immunoassay for point-of-care viral antigen detection.Nature biomedical engineering · 2025Article
- Bioconversion of Lactose into Glucose-Galactose Syrup by Two-Stage Enzymatic Hydrolysis.Foods (Basel, Switzerland) · 2022Article
- Improvement of Fucosylated Oligosaccharides Synthesis by α-L-Fucosidase from Thermotoga maritima in Water-Organic Cosolvent Reaction System.Applied biochemistry and biotechnology · 2021Article
- Bifidobacterial β-Galactosidase-Mediated Production of Galacto-Oligosaccharides: Structural and Preliminary Functional Assessments.Frontiers in microbiology · 2021Article
- Continuous Production of Galacto-Oligosaccharides by an Enzyme Membrane Reactor Utilizing Free Enzymes.Membranes · 2020Article
- The pharmacological chaperone N-n-butyl-deoxygalactonojirimycin enhances β-galactosidase processing and activity in fibroblasts of a patient with infantile GM1-gangliosidosis.Human genetics · 2020Article
- Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the β-galactosidase from Bacillus subtilis VTCC-DVN-12-01.BMC biochemistry · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymatic synthesis of galacto-oligosaccharides is usually performed at high initial substrate concentrations since higher yields are obtained. We report here on the stability of β-galactosidase from Bacillus circulans at 25, 40, and 60°C in buffer, and in systems with initially 5.0 and 30% (w/w) lactose. In buffer, the half-life time was 220 h and 13 h at 25 and 40°C, respectively, whereas the enzyme was completely inactivated after two hours at 60°C. In systems with 5.0 and 30% (w/w) lactose, a mechanistic model was used to correct the oNPG converting activity for the presence of lactose, glucose, galactose, and oligosaccharides in the activity assay. Without correction, the stability at 5.0% (w/w) lactose was overestimated, while the stability at 30% (w/w) lactose was underestimated. The inactivation constant k d was strongly dependent on temperature in buffer, whereas only a slight increase in k d was found with temperature at high substrate concentrations. The enzyme stability was found to increase strongly with the initial substrate concentrations. The inactivation energy E a appeared to be lower at high initial substrate concentrations.
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