Wheat Dehydrin DHN-5 Exerts a Heat-Protective Effect on β-Glucosidase and Glucose Oxidase Activities

被引:66
作者
Brini, Faical [1 ]
Saibi, Walid [2 ]
Amara, Imen [1 ]
Gargouri, Ali [2 ]
Masmoudi, Khaled [1 ]
Hanin, Moez [1 ]
机构
[1] CBS, Plant Mol Genet Lab, Sfax 3018, Tunisia
[2] CBS, Mol Genet Eukaryotes Lab, Sfax 3018, Tunisia
关键词
dehydrin; heating stress; enzymatic activity; beta-glucosidase; glucose oxidase/peroxidase; CRYOPROTECTIVE ACTIVITY; WATER-STRESS; IN-VITRO; COLD; DEHYDRATION; PROTEIN; TOLERANCE; BINDING; PHOSPHORYLATION; PURIFICATION;
D O I
10.1271/bbb.90949
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1050 / 1054
页数:5
相关论文
共 40 条
[1]   Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation [J].
Alsheikh, MK ;
Heyen, BJ ;
Randall, SK .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (42) :40882-40889
[2]   PROTECTIVE EFFECT OF LOW AND HIGH MOLECULAR-WEIGHT COMPOUNDS ON STABILITY OF CATALASE SUBJECTED TO FREEZING AND THAWING [J].
ASHWOODSMITH, MJ ;
WARBY, C .
CRYOBIOLOGY, 1972, 9 (02) :137-+
[3]   Stabilization of immobilized glucose oxidase against thermal inactivation by silanization for biosensor applications [J].
Babu, VRS ;
Kumar, MA ;
Karanth, NG ;
Thakur, MS .
BIOSENSORS & BIOELECTRONICS, 2004, 19 (10) :1337-1341
[4]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[5]   Cryoprotective activity of a cold-induced dehydrin purified from barley [J].
Bravo, LA ;
Gallardo, J ;
Navarrete, A ;
Olave, N ;
Martínez, J ;
Alberdi, M ;
Close, TJ ;
Corcuera, LJ .
PHYSIOLOGIA PLANTARUM, 2003, 118 (02) :262-269
[6]   Hydrolysis of oleuropein by recombinant β-glycosidase from hyperthermophilic archaeon Sulfolobus solfataricus immobilised on chitosan matrix [J].
Briante, R ;
La Cara, F ;
Febbraio, F ;
Barone, R ;
Piccialli, G ;
Carolla, R ;
Mainolfi, P ;
De Napoli, L ;
Patumi, M ;
Fontanazza, G ;
Nucci, R .
JOURNAL OF BIOTECHNOLOGY, 2000, 77 (2-3) :275-286
[7]   Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana [J].
Brini, Faical ;
Hanin, Moez ;
Lumbreras, Victoria ;
Amara, Imen ;
Khoudi, Habib ;
Hassairi, Afif ;
Pages, Montserrat ;
Masmoudi, Khaled .
PLANT CELL REPORTS, 2007, 26 (11) :2017-2026
[8]   Functional characterization of DHN-5, a dehydrin showing a differential phosphorylation pattern in two Tunisian durum wheat (Triticum durum Desf.) varieties with marked differences in salt and drought tolerance [J].
Brini, Faical ;
Hanin, Moez ;
Lumbreras, Victoria ;
Irar, Sami ;
Pages, Montserrat ;
Masmoudi, Khaled .
PLANT SCIENCE, 2007, 172 (01) :20-28
[9]   Hydrophilic protein associated with desiccation tolerance exhibits broad protein stabilization function [J].
Chakrabortee, Sohini ;
Boschetti, Chiara ;
Walton, Laura J. ;
Sarkar, Sovan ;
Rubinsztein, David C. ;
Tunnacliffe, Alan .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (46) :18073-18078
[10]   A CDNA-BASED COMPARISON OF DEHYDRATION-INDUCED PROTEINS (DEHYDRINS) IN BARLEY AND CORN [J].
CLOSE, TJ ;
KORTT, AA ;
CHANDLER, PM .
PLANT MOLECULAR BIOLOGY, 1989, 13 (01) :95-108