Molecular-level insight into the effects of low moisture and trehalose on the thermostability of ß-glucosidase.
Food Chem
; 460(Pt 2): 140607, 2024 Jul 24.
Article
em En
| MEDLINE
| ID: mdl-39068804
ABSTRACT
The high temperature induces conformational changes in ß-glucosidase, making it inactive and limiting its application field. In this paper, the effect of trehalose on the thermostability of ß-glucosidase from low-moisture Hevea brasiliensis seeds was investigated. The results showed that the residual enzyme activities of ß-glucosidase supplemented with trehalose after high-temperature treatment were significantly higher than that of the control group. The improvement of thermostability could be explained by low-field nuclear magnetic resonance (LF-NMR) and molecular dynamics (MD) simulations at the molecular level. Moreover, adding trehalose increased the water activity and water content of ß-glucosidase, leading to a more stable conformation. Trehalose replaced some water and formed a stable network of hydrogen bonds with protein and surrounding water. The glass formed by trehalose also reduced molecular movement, thus providing good protection for enzymes.
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01-internacional
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MEDLINE
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article