A New Alkaliphilic Cold-Active Esterase from the Psychrophilic Marine Bacterium Rhodococcus sp.: Functional and Structural Studies and Biotechnological Potential

2014 ◽  
Vol 172 (6) ◽  
pp. 3054-3068 ◽  
Author(s):  
Concetta De Santi ◽  
Pietro Tedesco ◽  
Luca Ambrosino ◽  
Bjørn Altermark ◽  
Nils-Peder Willassen ◽  
...  
3 Biotech ◽  
2021 ◽  
Vol 11 (11) ◽  
Author(s):  
Megha Kumari ◽  
Srichandan Padhi ◽  
Swati Sharma ◽  
Loreni Chiring Phukon ◽  
Sudhir P. Singh ◽  
...  

Author(s):  
Hubert Cieśliński ◽  
Marta Wanarska ◽  
Anna Pawlak-Szukalska ◽  
Ewelina Krajewska ◽  
Monika Wicka ◽  
...  

2010 ◽  
Vol 162 (8) ◽  
pp. 2136-2148 ◽  
Author(s):  
Xiaoxia Mao ◽  
Yuzhi Hong ◽  
Zongze Shao ◽  
Yan Zhao ◽  
Ziduo Liu
Keyword(s):  

2017 ◽  
Vol 5 (15) ◽  
Author(s):  
Purnima Singh ◽  
Neelam Kapse ◽  
Utpal Roy ◽  
Shiv Mohan Singh ◽  
P. K. Dhakephalkar

ABSTRACT Nesterenkonia sp. strain PF2B19, a psychrophilic bacterium, was isolated from 44,800-year-old permafrost. The draft genome sequence of this strain revealed the presence of genes involved in the production of cold active enzymes, carotenoid biosynthesis, fatty acid biosynthesis, and resistance to heavy metals. These results show the immense potential of the strain.


2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Mei-Ling Sun ◽  
Fang Zhao ◽  
Mei Shi ◽  
Xi-Ying Zhang ◽  
Bai-Cheng Zhou ◽  
...  

Marine Drugs ◽  
2020 ◽  
Vol 18 (5) ◽  
pp. 245
Author(s):  
Jianlong He ◽  
Le Liu ◽  
Xiaoyan Liu ◽  
Kai Tang

We cloned a xylanase gene (xynT) from marine bacterium Echinicola rosea sp. nov. JL3085T and recombinantly expressed it in Escherichia coli BL21. This gene encoded a polypeptide with 379 amino acid residues and a molecular weight of ~43 kDa. Its amino acid sequence shared 45.3% similarity with an endoxylanase from Cellvibrio mixtus that belongs to glycoside hydrolases family 10 (GH10). The XynT showed maximum activity at 40 °C and pH 7.0, and a maximum velocity of 62 μmoL min−1 mg−1. The XynT retained its maximum activity by more than 69%, 51%, and 26% at 10 °C, 5 °C, and 0 °C, respectively. It also exhibited the highest activity of 135% in the presence of 4 M NaCl and retained 76% of its activity after 24 h incubation with 4 M NaCl. This novel xylanase, XynT, is a cold-active and halotolerant enzyme that may have promising applications in drug, food, feed, and bioremediation industries.


Author(s):  
John Fahim ◽  
Yasmin Elsayed ◽  
Usama Abdelmohsen ◽  
Mostafa Fouad

3 Biotech ◽  
2021 ◽  
Vol 11 (2) ◽  
Author(s):  
Yingying He ◽  
Changfeng Qu ◽  
Liping Zhang ◽  
Jinlai Miao

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