Sorbitol prevents the self-aggregation of unfolded lysozyme leading to an up to 13°C stabilisation of the folded form-Reference-Cited by-同舟云学术

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Sorbitol prevents the self-aggregation of unfolded lysozyme leading to an up to 13°C stabilisation of the folded form

Published:2004-11 Issue:3 Volume:114 Page:269-278
ISSN:0168-1656
Container-title:Journal of Biotechnology
language:en
Short-container-title:Journal of Biotechnology

Author:

Petersen Steffen B.,Jonson Virpi,Fojan Peter,Wimmer Reinhard,Pedersen Shona

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology,Bioengineering

Reference31 articles.

1. Pressure-induced changes in the folded structure of lysozyme;Akasaka;J. Mol. Biol.,1997

2. Increased thermal stability of proteins in the presence of sugars and polyols;Back;Biochemistry,1979

3. Thermal unfolding and refolding of β-lactoglobulin: an intrinsic and extrinsic fluorescence study;Bhattacharjee;Eur. J. Biochem.,2000

4. Calorimetric titration of lysozyme;Bjurulf;Eur. J. Biochem.,1972

5. Mechanism of enzyme stabilisation;Combes;Ann. N.Y. Acad. Sci.,1987

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