Some like it hot, some like it cold: Temperature dependent biotechnological applications and improvements in extremophilic enzymes

被引:100
|
作者
Siddiqui, Khawar Sohail [1 ]
机构
[1] King Fahd Univ Petr & Minerals, Dept Life Sci, Dhahran 31261, Saudi Arabia
关键词
Psychrophilic; Cold-adapted; Thermophilic; Protein structure; function; stability; Computational; genetic and chemical modification; Magnetic nanoparticles; ITERATIVE SATURATION MUTAGENESIS; ANTARCTICA LIPASE-B; DIRECTED EVOLUTION; ALPHA-AMYLASE; THERMAL-STABILITY; BIOCHEMICAL-CHARACTERIZATION; PSYCHROPHILIC ENZYMES; CHEMICAL-MODIFICATION; COMPUTATIONAL DESIGN; ENHANCED STABILITY;
D O I
10.1016/j.biotechadv.2015.11.001
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
The full biotechnological exploitation of enzymes is still hampered by their low activity, low stability and high cost. Temperature-dependent catalytic properties of enzymes are a key to efficient and cost-effective translation to commercial applications. Organisms adapted to temperature extremes are a rich source of enzymes with broad ranging thermal properties which, if isolated, characterized and their structure-function-stability relationship elucidated, could underpin a variety of technologies. Enzymes from thermally-adapted organisms such as psychrophiles (low-temperature) and thermophiles (high-temperature) are a vast natural resource that is already under scrutiny for their biotechnological potential. However, psychrophilic and thermophilic enzymes show an activity-stability trade-off that necessitates the use of various genetic and chemical modifications to further improve their properties to suit various industrial applications. This review describes in detail the properties and biotechnological applications of both cold-adapted and thermophilic enzymes. Furthermore, the review critically examines ways to improve their value for biotechnology, concluding by proposing an integrated approach involving thermally-adapted, genetically and magnetically modified enzymes to make biocatalysis more efficient and cost-effective. (C) 2015 Elsevier Inc. All rights reserved.
引用
收藏
页码:1912 / 1922
页数:11
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