Literature DB >> 16232960

Enzymes which are stable in the presence of organic solvents.

H Ogino1, H Ishikawa.   

Abstract

There are numerous advantages of employing enzymes as catalysts in organic solvents or aqueous solutions containing organic solvents instead of water. A few natural enzymes which are stable in the presence of organic solvents have been discovered. However, almost all natural enzymes are easily denatured and inactivated in the presence of organic solvents. Therefore, several physical and chemical methods, such as immobilization, modification, and entrapment, for stabilizing enzymes in the presence of organic solvents were developed. Protein engineering using site directed mutagenesis and directed evolution are useful for clarifying why organic solvent-stable enzymes are stable in the presence of organic solvents and for developing organic solvent-stable mutant enzymes.

Entities:  

Year:  2001        PMID: 16232960     DOI: 10.1263/jbb.91.109

Source DB:  PubMed          Journal:  J Biosci Bioeng        ISSN: 1347-4421            Impact factor:   2.894


  38 in total

1.  Purification and characterization of an organic-solvent-tolerant cellulase from a halotolerant isolate, Bacillus sp. L1.

Authors:  Xin Li; Hui-Ying Yu
Journal:  J Ind Microbiol Biotechnol       Date:  2012-03-22       Impact factor: 3.346

2.  A novel xylanase with tolerance to ethanol, salt, protease, SDS, heat, and alkali from actinomycete Lechevalieria sp. HJ3.

Authors:  Junpei Zhou; Yajie Gao; Yanyan Dong; Xianghua Tang; Junjun Li; Bo Xu; Yuelin Mu; Qian Wu; Zunxi Huang
Journal:  J Ind Microbiol Biotechnol       Date:  2012-03-20       Impact factor: 3.346

3.  Purification and characterization of a halophilic α-amylase with increased activity in the presence of organic solvents from the moderately halophilic Nesterenkonia sp. strain F.

Authors:  Mohammad Shafiei; Abed-Ali Ziaee; Mohammad Ali Amoozegar
Journal:  Extremophiles       Date:  2012-05-17       Impact factor: 2.395

4.  Protein engineering by random mutagenesis and structure-guided consensus of Geobacillus stearothermophilus Lipase T6 for enhanced stability in methanol.

Authors:  Adi Dror; Einav Shemesh; Natali Dayan; Ayelet Fishman
Journal:  Appl Environ Microbiol       Date:  2013-12-20       Impact factor: 4.792

5.  Filling the Void: Introducing Aromatic Interactions into Solvent Tunnels To Enhance Lipase Stability in Methanol.

Authors:  Shalev Gihaz; Margarita Kanteev; Yael Pazy; Ayelet Fishman
Journal:  Appl Environ Microbiol       Date:  2018-11-15       Impact factor: 4.792

6.  Calcium-ion-induced stabilization of the protease from Bacillus cereus WQ9-2 in aqueous hydrophilic solvents: effect of calcium ion binding on the hydration shell and intramolecular interactions.

Authors:  Jiaxing Xu; Yu Zhuang; Bin Wu; Long Su; Bingfang He
Journal:  J Biol Inorg Chem       Date:  2013-01-16       Impact factor: 3.358

7.  Biochemical characterization of a halophilic, alkalithermophilic protease from Alkalibacillus sp. NM-Da2.

Authors:  Asmaa R Abdel-Hamed; Dina M Abo-Elmatty; Juergen Wiegel; Noha M Mesbah
Journal:  Extremophiles       Date:  2016-10-18       Impact factor: 2.395

8.  Purification and biochemical characterization of a protease secreted by the Salinivibrio sp. strain AF-2004 and its behavior in organic solvents.

Authors:  Hamid Reza Karbalaei-Heidari; Abed-Ali Ziaee; Mohammad Ali Amoozegar
Journal:  Extremophiles       Date:  2006-10-27       Impact factor: 2.395

9.  Purification and characterization of extracellular lipases from Pseudomonas monteilii TKU009 by the use of soybeans as the substrate.

Authors:  San-Lang Wang; Yu-Ting Lin; Tzu-Wen Liang; Sau-Hua Chio; Li-June Ming; Pei-Chen Wu
Journal:  J Ind Microbiol Biotechnol       Date:  2008-09-23       Impact factor: 3.346

10.  Evolving thermostability in mutant libraries of ligninolytic oxidoreductases expressed in yeast.

Authors:  Eva García-Ruiz; Diana Maté; Antonio Ballesteros; Angel T Martinez; Miguel Alcalde
Journal:  Microb Cell Fact       Date:  2010-03-18       Impact factor: 5.328

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