Literature DB >> 11297390

Thermozymes and their applications: a review of recent literature and patents.

M E Bruins1, A E Janssen, R M Boom.   

Abstract

Enzymes from thermophilic microorganisms, thermozymes, have unique characteristics such as temperature, chemical, and pH stability. They can be used in several industrial processes, in which they replace mesophilic enzymes or chemicals. Thermozymes are often used when the enzymatic process is compatible with existing (high-temperature) process conditions. The main advantages of performing processes at higher temperatures are reduced risk of microbial contamination, lower viscosity, improved transfer rates, and improved solubility of substrates. However, cofactors, substrates, or products might be unstable or other side reactions may occur. Recent developments show that thermophiles are a good source of novel catalysts that are of great industrial interest. Thermostable polymer-degrading enzymes such as amylases, pullulanases, xylanases, proteases, and cellulases are expected to play an important role in food, chemical, pharmaceutical, paper, pulp, and waste-treatment industries. Considerable research efforts have been made to better understand the stability of thermozymes. There are no major conformational differences with mesophilic enzymes, and a small number of extra salt bridges, hydrophobic interactions, or hydrogen bounds seem to confer the extra degree of stabilization. Currently, overexpression of thermozymes in standard Escherichia coli allows the production of much larger quantities of enzymes, which are easy to purify by heat treatment. With wider availability and lower cost, thermophilic enzymes will see more application in industry.

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Year:  2001        PMID: 11297390     DOI: 10.1385/abab:90:2:155

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  50 in total

1.  Draft genome sequence of Thermus sp. strain RL, isolated from a hot water spring located atop the Himalayan ranges at Manikaran, India.

Authors:  Vatsala Dwivedi; Naseer Sangwan; Aeshna Nigam; Nidhi Garg; Neha Niharika; Paramjit Khurana; Jitendra P Khurana; Rup Lal
Journal:  J Bacteriol       Date:  2012-07       Impact factor: 3.490

2.  Cloning, expression, and characterization of a thermostable glucose-6-phosphate dehydrogenase from Thermoanaerobacter tengcongensis.

Authors:  Zilong Li; Ning Jiang; Keqian Yang; Jianting Zheng
Journal:  Extremophiles       Date:  2016-02-08       Impact factor: 2.395

3.  A method of expression for an oxygen-tolerant group III alcohol dehydrogenase from Pyrococcus horikoshii OT3.

Authors:  Chikanobu Sugimoto; Kouta Takeda; Yumi Kariya; Hirotoshi Matsumura; Masafumi Yohda; Hiroyuki Ohno; Nobuhumi Nakamura
Journal:  J Biol Inorg Chem       Date:  2017-01-13       Impact factor: 3.358

4.  Prediction of protein thermostability with a direction- and distance-dependent knowledge-based potential.

Authors:  Christian Hoppe; Dietmar Schomburg
Journal:  Protein Sci       Date:  2005-09-09       Impact factor: 6.725

5.  Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability.

Authors:  Mohammad Wadud Bhuiya; Jimmy Suryadi; Zholi Zhou; Bernard Andrew Brown
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-08-19

6.  Transaldolase of Methanocaldococcus jannaschii.

Authors:  Tim Soderberg; Robert C Alver
Journal:  Archaea       Date:  2004-10       Impact factor: 3.273

7.  Thermo- and mesostabilizing protein interactions identified by temperature-dependent statistical potentials.

Authors:  Benjamin Folch; Yves Dehouck; Marianne Rooman
Journal:  Biophys J       Date:  2010-02-17       Impact factor: 4.033

8.  Conformational plasticity surrounding the active site of NADH oxidase from Thermus thermophilus.

Authors:  Teresa Miletti; Justin Di Trani; Louis-Charles Levros; Anthony Mittermaier
Journal:  Protein Sci       Date:  2015-05-29       Impact factor: 6.725

Review 9.  Thermophilic fungi in the new age of fungal taxonomy.

Authors:  Tássio Brito de Oliveira; Eleni Gomes; Andre Rodrigues
Journal:  Extremophiles       Date:  2014-11-16       Impact factor: 2.395

10.  Thermus thermophilus as a cell factory for the production of a thermophilic Mn-dependent catalase which fails to be synthesized in an active form in Escherichia coli.

Authors:  Aurelio Hidalgo; Lorena Betancor; Renata Moreno; Olga Zafra; Felipe Cava; Roberto Fernández-Lafuente; José M Guisán; José Berenguer
Journal:  Appl Environ Microbiol       Date:  2004-07       Impact factor: 4.792

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