Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 74, Issue 5, Pages 1050-1054Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.90949
Keywords
dehydrin; heating stress; enzymatic activity; beta-glucosidase; glucose oxidase/peroxidase
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Funding
- Ministry of Higher Education, Scientific Research, and Technology of Tunisia
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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, beta-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 degrees 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.
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