Effect of Dextran and its Derivatives on Thermal Tnactivation of Glucoamylase

Moriyama, Shigeru; Matsuno, Ryuichi; Nakanishi, Kotoyoshi; Kamikubo, Tadashi

doi:10.1080/00021369.1980.10864429

Cited by 1 publication

(2 citation statements)

References 6 publications

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“…14,15 However, not all polymers increase the protein stability. Despite evidence suggesting protein−polymer repulsion, 16 studies revealed that poly(sulfobetaine) can destabilize proteins in bulk polymer solutions. 17 A few studies have explored the influence of alginate on the thermodynamic stability, diffusion, or activity of encapsulated proteins.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Numerous studies have analyzed how polyelectrolytes and water-soluble polymers can alter the stability of biomolecules such as enzymes. − Complex coacervates also form as a result of protein–polymer interactions. , Other studies exploited protein–polymer interactions to increase protein stability in organic solvents or to mimic protein mixtures. , However, not all polymers increase the protein stability. Despite evidence suggesting protein–polymer repulsion, studies revealed that poly(sulfobetaine) can destabilize proteins in bulk polymer solutions …”

Section: Introductionmentioning

confidence: 99%

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Protein Folding Stability and Kinetics in Alginate Hydrogels

Chang,

Gruebele,

Leckband

2023

Biomacromolecules

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Proteins are commonly encapsulated in alginate gels for drug delivery and tissue-engineering applications. However, there is limited knowledge of how encapsulation impacts intrinsic protein properties such as folding stability or unfolding kinetics. Here, we use fast relaxation imaging (FReI) to image protein unfolding in situ in alginate hydrogels after applying a temperature jump. Based on changes in the Förster resonance energy transfer (FRET) response of FRET-labeled phosphoglycerate kinase (PGK), we report the quantitative impact of multiple alginate hydrogel concentrations on protein stability and folding dynamics. The gels stabilize PGK by increasing its melting temperature up to 18.4 °C, and the stabilization follows a nonmonotonic dependence on the alginate density. In situ kinetic measurements also reveal that PGK deviates more from two-state folding behavior in denser gels and that the gel decreases the unfolding rate and accelerates the folding rate of PGK, compared to buffer. Phi-value analysis suggests that the folding transition state of an encapsulated protein is structurally similar to that of folded protein. This work reveals both beneficial and negative impacts of gel encapsulation on protein folding, as well as potential mechanisms contributing to altered stability.

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