Cold-adapted enzymes: from fundamentals to biotechnology

被引：487

作者：

Gerday, C ^{[1
]}

Aittaleb, M ^{[1
]}

Bentahir, M ^{[1
]}

Chessa, JP ^{[1
]}

Claverie, P ^{[1
]}

Collins, T ^{[1
]}

D'Amico, S ^{[1
]}

Dumont, J ^{[1
]}

Garsoux, G ^{[1
]}

Georlette, D ^{[1
]}

Hoyoux, A ^{[1
]}

Lonhienne, T ^{[1
]}

Meuwis, MA ^{[1
]}

Feller, G ^{[1
]}

机构：

[1] Univ Liege, Biochem Lab, Inst Chem, B-4000 Liege, Belgium

来源：

TRENDS IN BIOTECHNOLOGY | 2000年 / 18卷 / 03期

关键词：

D O I：

10.1016/S0167-7799(99)01413-4

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Psychrophilic enzymes produced by cold-adapted microorganisms display a high catalytic efficiency and are most often, if not always, associated with high thermosensitivity. Using X-ray crystallography, these properties are beginning to become understood, and the rules governing their adaptation to cold appear to be relatively diverse. The application of these enzymes offers considerable potential to the biotechnology industry, for example, in the detergent and food industries, for the production of fine chemicals and in bioremediation processes.

引用

页码：103 / 107

页数：5

共 34 条

[1] Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level [J].

Aghajari, N ;

Feller, G ;

Gerday, C ;

Haser, R .

STRUCTURE, 1998, 6 (12) :1503-1516

[2] Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor [J].

Aghajari, N ;

Feller, G ;

Gerday, C ;

Haser, R .

PROTEIN SCIENCE, 1998, 7 (03) :564-572

[3] Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23 [J].

Aghajari, N ;

Feller, G ;

Gerday, C ;

Haser, R .

PROTEIN SCIENCE, 1996, 5 (10) :2128-2129

[4] Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus -: Kinetic and structural properties [J].

Alvarez, M ;

Zeelen, JP ;

Mainfroid, V ;

Rentier-Delrue, F ;

Martial, JA ;

Wyns, L ;

Wierenga, RK ;

Maes, D .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (04) :2199-2206

[5] Comparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme [J].

Beadle, BM ;

Baase, WA ;

Wilson, DB ;

Gilkes, NR ;

Shoichet, BK .

BIOCHEMISTRY, 1999, 38 (08) :2570-2576

[6] Biocatalyst behaviour in low-water systems [J].

Bell, G ;

Halling, PJ ;

Moore, BD ;

Partridge, J ;

Rees, DG .

TRENDS IN BIOTECHNOLOGY, 1995, 13 (11) :468-473

[7]

DELILLE D, 1990, Vie et Milieu, V40, P281

[8] Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanctis [J].

Feller, G ;

d'Amico, D ;

Gerday, C .

BIOCHEMISTRY, 1999, 38 (14) :4613-4619

[9]

FELLER G, 1994, APPL MICROBIOL BIOT, V41, P477, DOI 10.1007/s002530050176

[10]

Feller G, 1997, EUR J BIOCHEM, V244, P186, DOI 10.1111/j.1432-1033.1997.00186.x

← 1 2 3 4 →