Complete genome sequence of Rhodothermaceae bacterium RA with cellulolytic and xylanolytic activities-Reference-Cited by-同舟云学术

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Complete genome sequence of Rhodothermaceae bacterium RA with cellulolytic and xylanolytic activities

Published:2018-08 Issue:8 Volume:8 Page:
ISSN:2190-572X
Container-title:3 Biotech
language:en
Short-container-title:3 Biotech

Author:

Liew Kok Jun,Teo Seng Chong,Shamsir Mohd Shahir,Sani Rajesh Kumar,Chong Chun Shiong,Chan Kok-Gan,Goh Kian Mau^ORCID

Funder

Universiti Teknologi Malaysia Research Grants

Newton Ungku Omar Fund

Zamalah Program of Universiti Teknologi Malaysia

Universiti Malaya Research Grant from JBK, NRE, and PPP

Publisher

Springer Science and Business Media LLC

Subject

Agricultural and Biological Sciences (miscellaneous),Environmental Science (miscellaneous),Biotechnology

Link

http://link.springer.com/article/10.1007/s13205-018-1391-z/fulltext.html

Reference39 articles.

1. Ahsan MM, Kimura T, Karita S, Sakka K, Ohmiya K (1996) Cloning, DNA sequencing, and expression of the gene encoding Clostridium thermocellum cellulase CelJ, the largest catalytic component of the cellulosome. J Bacteriol 178:5732–5740

2. Alfredsson GA, Kristjansson JK, Hjörleifsdottir S, Stetter KO (1988) Rhodothermus marinus, gen. nov., sp. nov., a thermophilic, halophilic bacterium from submarine hot springs in Iceland. Microbiology 134:299–306

3. Antón J, Oren A, Benlloch S, Rodríguez-Valera F, Amann R, Rosselló-Mora R (2002) Salinibacter ruber gen. nov., sp. nov., a novel, extremely halophilic member of the Bacteria from saltern crystallizer ponds. Int J Syst Evol Microbiol 52:485–491

4. Bleicher L, Prates ET, Gomes TC, Silveira RL, Nascimento AS, Rojas AL, Golubev A, Martínez L, Skaf MS, Polikarpov I (2011) Molecular basis of the thermostability and thermophilicity of laminarinases: X-ray structure of the hyperthermostable laminarinase from Rhodothermus marinus and molecular dynamics simulations. J Phys Chem B 115:7940–7949

5. Blumer-Schuette SE, Lewis DL, Kelly RM (2010) Phylogenetic, microbiological, and glycoside hydrolase diversities within the extremely thermophilic, plant biomass-degrading genus Caldicellulosiruptor. Appl Environ Microbiol 76:8084–8092

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