ArticleJournal of biosciences2009
Thermal stability of alpha-amylase in aqueous cosolvent systems.
Article in Journal of biosciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Effect of Replacing Conventional Corn with Corn Containing Thermostable α-Amylase Enzyme (AMY797E) in Standard and Low-Energy Diets in Laying Hens.Animals : an open access journal from MDPI · 2026Article
- Influence of Supercritical Carbon Dioxide on the Activity and Conformational Changes ofFoods (Basel, Switzerland) · 2023Article
- Self-Organization of Enzyme-Catalyzed Reactions Studied by the Maximum Entropy Production Principle.International journal of molecular sciences · 2023Article
- Detrimental Effects of Elevated Temperatures on the Structure and Activity of Phenylalanine Ammonia Lyase-Bovine Serum Albumin Mixtures and the Stabilizing Potential of Surfactant and Sugars.AAPS PharmSciTech · 2022Article
- Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens.The protein journal · 2020Article
- Understanding the Role of Preferential Exclusion of Sugars and Polyols from Native State IgG1 Monoclonal Antibodies and its Effect on Aggregation and Reversible Self-Association.Pharmaceutical research · 2019Article
- Reaction and diffusion thermodynamics explain optimal temperatures of biochemical reactions.Scientific reports · 2018Article
- Thermal adaptation of dihydrofolate reductase from the moderate thermophile Geobacillus stearothermophilus.Biochemistry · 2014Article
- Macromolecular Crowding Enhances Catalytic Efficiency and Stability of α-Amylase.ISRN biotechnology · 2013Article
- Honey-induced protein stabilization as studied by fluorescein isothiocyanate fluorescence.TheScientificWorldJournal · 2013Article
- Stabilizing effect of various polyols on the native and the denatured states of glucoamylase.TheScientificWorldJournal · 2013Article
- Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.Protein science : a publication of the Protein Society · 2010Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity and thermal stability of alpha-amylase were studied in the presence of different concentrations of trehalose, sorbitol, sucrose and glycerol. The optimum temperature of the enzyme was found to be 50 +/- 2 degrees C. Further increase in temperature resulted in irreversible thermal inactivation of the enzyme. In the presence of cosolvents, the rate of thermal inactivation was found to be significantly reduced. The apparent thermal denaturation temperature (Tm) app and activation energy (Ea) of alpha-amylase were found to be significantly increased in the presence of cosolvents in a concentration-dependent manner. In the presence of 40% trehalose, sorbitol, sucrose and glycerol, increments in the (Tm)app were 20 degrees C, 14 degrees C, 13 degrees C and 9 degrees C, respectively. The Ea of thermal denaturation of alpha-amylase in the presence of 20% (w/v) trehalose, sorbitol, sucrose and glycerol was found to be 126, 95, 90 and 43 kcal/mol compared with a control value of 40 kcal/mol. Intrinsic and 8-anilinonaphathalene-1-sulphonic acid (ANS) fluorescence studies indicated that thermal denaturation of the enzyme was accompanied by exposure of the hydrophobic cluster on the protein surface. Preferential interaction parameters indicated extensive hydration of the enzyme in the presence of cosolvents.
Indexed as
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.