ArticleISRN biotechnology2013
Macromolecular Crowding Enhances Catalytic Efficiency and Stability of α-Amylase.
Article in ISRN biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Aggregation of Phosphates Enhances Enzyme Activity in Aqueous Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- HCR-Proxy resolves site-specific proximal RNA microenvironments at subcompartmental resolution.Nucleic acids research · 2026Article
- Understanding the Impacts of Molecular and Macromolecular Crowding Agents on Protein-Polymer Complex Coacervates.Biomacromolecules · 2023Article
- Crowding-induced morphological changes in synthetic lipid vesicles determined using smFRET.Frontiers in bioengineering and biotechnology · 2022Article
- Particle-Based Simulation Reveals Macromolecular Crowding Effects on the Michaelis-Menten Mechanism.Biophysical journal · 2019Article
- Large cosolutes, small cosolutes, and dihydrofolate reductase activity.Protein science : a publication of the Protein Society · 2017Article
- β-galactosidase stability at high substrate concentrations.SpringerPlus · 2013Article
Corrections and comments
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Authors and funding
1 author.
Funding
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Abstract
In the present study an attempt was made to investigate the macromolecular crowding effect on functional attributes of α-amylase. High concentrations of sugar based cosolvents, (e.g., trehalose, sucrose, sorbitol, and glycerol) were used to mimic the macromolecular crowding environment (of cellular milieu) under in vitro conditions. To assess the effect of macromolecular crowding, the activity and structural properties of the enzyme were evaluated in the presence of different concentrations of the above cosolvents. Based on the results it is suggested that the macromolecular crowding significantly improves the catalytic efficiency of the enzyme with marginal change in the structure. Out of four cosolvents examined, trehalose was found to be the most effective in consistently enhancing thermal stability of the enzyme. Moreover, the relative effectiveness of the above cosolvents was found to be dependent on their concentration used.
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Registered trials
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