Abstract
Group-2 late embryogenesis abundant (LEA) proteins, also known as dehydrins, are claimed to stabilize macromolecules against damage caused by freezing, dehydration, ionic or osmotic stresses. However, their precise function remains unknown. Here, we investigated the effect of wheat dehydrin (DHN-5) protein on the activity and thermostability of two distinct enzymes, β-glucosidase (bglG) and glucose oxidase/peroxidase (GOD/POD) in vitro. The purified DHN-5 protein had the capacity to preserve and stabilize the activity of bglG subjected to heat treatment. In addition, DHN-5 stabilized oxidizing enzymes, as it improved reliability in measuring glucose concentrations with a glucose oxidase/peroxidase (GOD/POD) kit while the temperature increased from 37 to 70 °C. All together the data presented provide evidence that DHN-5 is a dehydrin able to preserve enzyme activities in vitro from adverse effects induced by heating.
| Original language | English |
|---|---|
| Pages (from-to) | 1050-1054 |
| Number of pages | 5 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 74 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2010 |
| Externally published | Yes |
Keywords
- Dehydrin
- Enzymatic activity
- Glucose oxidase/peroxidase
- Heating stress
- β-Glucosidase
ASJC Scopus subject areas
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry