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Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Thermal destabilization of stem bromelain by trehalose
1Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.hinayounus@rediffmail.com
The Protein Journal
|January 5, 2007
Summary
Trehalose and sucrose surprisingly destabilized bromelain protein, reducing its thermal stability and accelerating inactivation. This study challenges trehalose
Area of Science:
- Biochemistry
- Protein chemistry
- Enzyme kinetics
Background:
- Trehalose is recognized as a universal protein stabilizer.
- Osmoytes like trehalose and sucrose are commonly used to protect proteins.
Purpose of the Study:
- To investigate the impact of trehalose and sucrose on the thermal stability and conformation of bromelain.
- To understand the interaction between these disaccharides and the enzyme.
Main Methods:
- UV spectroscopy and CD spectropolarimetry were used to determine thermal stability (Tm values).
- Enzyme inactivation rates were measured at 60°C.
- Differential scanning calorimetry (DSC) was employed to study protein-osmolyte interactions.
Main Results:
- Bromelain in 1 M trehalose or sucrose showed decreased thermal stability, with Tm values dropping by 5-7°C.
- The enzyme exhibited faster inactivation at 60°C in the presence of these osmolytes.
- Preferential hydration of denatured bromelain by sucrose/trehalose was observed, stabilizing the denatured state.
Conclusions:
- Contrary to expectations, trehalose and sucrose destabilized bromelain under thermal stress.
- These osmolytes preferentially stabilize the denatured conformation of bromelain.
- This finding represents a novel observation of protein destabilization by trehalose.
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