Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability-Reference-Cited by-同舟云学术

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Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability

Published:2019-06-27 Issue:1 Volume:9 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Akanuma Satoshi,Bessho Mizumo,Kimura Hikono,Furukawa Ryutaro,Yokobori Shin-ichi,Yamagishi Akihiko

Funder

Japan Society for the Promotion of Science London

MEXT | National Institutes of Natural Sciences

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-019-45560-x.pdf

Reference51 articles.

1. Sterner, R. & Liebl, W. Thermophilic adaptation of proteins. Crit Rev Biochem Mol Biol 36, 39–106, https://doi.org/10.1080/20014091074174 (2001).

2. Sarmiento, F., Peralta, R. & Blamey, J. M. Cold and Hot Extremozymes: Industrial Relevance and Current Trends. Front Bioeng Biotechnol 3, 148, https://doi.org/10.3389/fbioe.2015.00148 (2015).

3. Siddiqui, K. S. Some like it hot, some like it cold: Temperature dependent biotechnological applications and improvements in extremophilic enzymes. Biotechnol Adv 33, 1912–1922, https://doi.org/10.1016/j.biotechadv.2015.11.001 (2015).

4. Habbeche, A. et al. Purification and biochemical characterization of a detergent-stable keratinase from a newly thermophilic actinomycete Actinomadura keratinilytica strain Cpt29 isolated from poultry compost. J Biosci Bioeng 117, 413–421, https://doi.org/10.1016/j.jbiosc.2013.09.006 (2014).

5. Aqvist, J. Cold Adaptation of Triosephosphate Isomerase. Biochemistry 56, 4169–4176, https://doi.org/10.1021/acs.biochem.7b00523 (2017).

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