Literature DB >> 26585268

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

Khawar Sohail Siddiqui1.   

Abstract

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.
Copyright © 2015 Elsevier Inc. All rights reserved.

Keywords:  Cold-adapted; Computational, genetic and chemical modification; Magnetic nanoparticles; Protein structure, function, stability; Psychrophilic; Thermophilic

Mesh:

Substances:

Year:  2015        PMID: 26585268     DOI: 10.1016/j.biotechadv.2015.11.001

Source DB:  PubMed          Journal:  Biotechnol Adv        ISSN: 0734-9750            Impact factor:   14.227


  30 in total

Review 1.  Role of extremophiles and their extremozymes in biorefinery process of lignocellulose degradation.

Authors:  Dixita Chettri; Ashwani Kumar Verma; Lija Sarkar; Anil Kumar Verma
Journal:  Extremophiles       Date:  2021-03-25       Impact factor: 2.395

2.  Cold active pectinase, amylase and protease production by yeast isolates obtained from environmental samples.

Authors:  Ceren Daskaya-Dikmen; Funda Karbancioglu-Guler; Beraat Ozcelik
Journal:  Extremophiles       Date:  2018-03-07       Impact factor: 2.395

3.  Cold adaptation of tRNA nucleotidyltransferases: A tradeoff in activity, stability and fidelity.

Authors:  Felix G M Ernst; Lieselotte Erber; Joana Sammler; Frank Jühling; Heike Betat; Mario Mörl
Journal:  RNA Biol       Date:  2017-11-21       Impact factor: 4.652

4.  Identification and characterization of a novel cold-tolerant extracellular protease from Planococcus sp. CGMCC 8088.

Authors:  Kun Chen; Qingshan Mo; Huan Liu; Feiyan Yuan; Haonan Chai; Fuping Lu; Huitu Zhang
Journal:  Extremophiles       Date:  2018-03-01       Impact factor: 2.395

5.  Characterization of the stereochemical configuration of lanthionines formed by the lanthipeptide synthetase GeoM.

Authors:  Neha Garg; Yuki Goto; Ting Chen; Wilfred A van der Donk
Journal:  Biopolymers       Date:  2016-11       Impact factor: 2.505

Review 6.  Cold Active Lipases: Biocatalytic Tools for Greener Technology.

Authors:  Nutan Mhetras; Vidhyashri Mapare; Digambar Gokhale
Journal:  Appl Biochem Biotechnol       Date:  2021-02-05       Impact factor: 2.926

7.  Distinct roles of an ionic interaction holding an alpha-helix with catalytic Asp and a beta-strand with catalytic His in a hyperthermophilic esterase EstE1 and a mesophilic esterase rPPE.

Authors:  VinayKumar Dachuri; Ngoc Truongvan; Quynh DangThu; Sei-Heon Jang; ChangWoo Lee
Journal:  Extremophiles       Date:  2019-07-22       Impact factor: 2.395

8.  Improving low-temperature activity and thermostability of exo-inulinase InuAGN25 on the basis of increasing rigidity of the terminus and flexibility of the catalytic domain.

Authors:  Rui Zhang; Limei He; Jidong Shen; Ying Miao; Xianghua Tang; Qian Wu; Junpei Zhou; Zunxi Huang
Journal:  Bioengineered       Date:  2020-12       Impact factor: 3.269

9.  Removal of N-terminal tail changes the thermostability of the low-temperature-active exo-inulinase InuAGN25.

Authors:  Limei He; Rui Zhang; Jidong Shen; Ying Miao; Xianghua Tang; Qian Wu; Junpei Zhou; Zunxi Huang
Journal:  Bioengineered       Date:  2020-12       Impact factor: 3.269

10.  Carbohydrate-Binding Module and Linker Allow Cold Adaptation and Salt Tolerance of Maltopentaose-Forming Amylase From Marine Bacterium Saccharophagus degradans 2-40 T.

Authors:  Ning Ding; Boyang Zhao; Xiaofeng Ban; Caiming Li; B V Venkataram Prasad; Zhengbiao Gu; Zhaofeng Li
Journal:  Front Microbiol       Date:  2021-07-14       Impact factor: 5.640

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