ArticleBiotechnology reports (Amsterdam, Netherlands)2021
Investigating thermal stability based on the structural changes of lactase enzyme by several orthogonal methods.
Article in Biotechnology reports (Amsterdam, Netherlands), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Advances in β-Galactosidase Research: A Systematic Review from Molecular Mechanisms to Enzyme Delivery Systems.Pharmaceutics · 2025Review
- Hot Melt Extrusion as Continuous Manufacturing Technique to Produce Bilayer Films Loaded with Paracetamol or Lactase.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Study on Lyophilised Orodispersible Tablets from Plant-Based Drinks as Bulking Agents.Pharmaceutics · 2025Article
- Optimization of solid-state fermentation conditions for high β-galactosidase-producing lactic acid bacteria and its application in low-lactose dairy products.Frontiers in bioengineering and biotechnology · 2025Article
- Development and Dissolution Study of a β-Galactosidase Containing Drinking Straw.Pharmaceutics · 2022Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermal stability of lactase (β-galactosidase) enzyme has been studied by a variety of physico-chemical methods. β-galactosidase is the main active ingredient of medications for lactose intolerance. It is typically produced industrially by the Aspergillus oryzae filamentous fungus. Lactase was used as a model to help understand thermal stability of enzyme-type biopharmaceuticals. Enzyme activity (hydrolyzation of lactose) of β-galactosidase was determined after storing the solid enzyme substance at various temperatures. For a better understanding of the relationship between structure and activity changes we determined the mass and size of the molecules with gel electrophoresis and dynamic light scattering and detected aggregation processes. A bottom-up proteomic procedure was used to determine the primary amino acid sequence and to investigate changes in the N-glycosylation pattern of the protein. NMR and CD spectroscopic methods were used to observe changes in higher order structures and to reveal relationships between structural and functional changes.
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