Purification and biochemical characterization of a cold-active lipase from Antarctic sea ice bacteria Pseudoalteromonas sp. NJ 70

2012 ◽  
Vol 39 (9) ◽  
pp. 9233-9238 ◽  
Author(s):  
Quanfu Wang ◽  
Yanhua Hou ◽  
Yu Ding ◽  
Peisheng Yan
Keyword(s):  
Sea Ice ◽  
Biochemical Characterization ◽  
Antarctic Sea Ice ◽  
Cold Active ◽  
Active Lipase

High-level expression and biochemical characterization of a novel cold-active lipase from Rhizomucor endophyticus

2016 ◽  
Vol 38 (12) ◽  
pp. 2127-2135 ◽  
Author(s):  
Xiaojie Duan ◽  
Mingming Zheng ◽  
Yu Liu ◽  
Zhengqiang Jiang ◽  
Shaoqing Yang
Keyword(s):  
Biochemical Characterization ◽  
High Level Expression ◽  
Cold Active ◽  
High Level ◽  
Active Lipase

scholarly journals Cloning, Expression, Purification, and Characterization of Glutaredoxin from Antarctic Sea-Ice BacteriumPseudoalteromonassp. AN178

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Quanfu Wang ◽  
Yanhua Hou ◽  
Yonglei Shi ◽  
Xiao Han ◽  
Qian Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sea Ice ◽  
Amino Acid Residues ◽  
E Coli ◽  
Antarctic Sea Ice ◽  
Apparent Homogeneity ◽  
Cold Active ◽  
Catalytic Motif ◽  
Protein Disulfide

Glutaredoxins (Grxs) are small ubiquitous redox enzymes that catalyze glutathione-dependent reactions to reduce protein disulfide. In this study, a full-length Grx gene (PsGrx) with 270 nucleotides was isolated from Antarctic sea-ice bacteriumPseudoalteromonassp. AN178. It encoded deduced 89 amino acid residues with the molecular weight 9.8 kDa. Sequence analysis of the amino acid sequence revealed the catalytic motif CPYC. RecombinantPsGrx (rPsGrx) stably expressed inE. coliBL21 was purified to apparent homogeneity by Ni-affinity chromatography. rPsGrx exhibited optimal activity at 30°C and pH 8.0 and showed 25.5% of the activity at 0°C. It retained 65.0% of activity after incubation at 40°C for 20 min and still exhibited 37.0% activity in 1.0 M NaCl. These results indicated that rPsGrx was a typical cold active protein with low thermostability.

Characterization of a cold-active lipase from Psychrobacter cryohalolentis K5T and its deletion mutants

2013 ◽  
Vol 78 (4) ◽  
pp. 385-394 ◽  
Author(s):  
K. A. Novototskaya-Vlasova ◽  
L. E. Petrovskaya ◽  
E. M. Rivkina ◽  
D. A. Dolgikh ◽  
M. P. Kirpichnikov
Keyword(s):  
Deletion Mutants ◽  
Cold Active ◽  
Active Lipase

Cloning and characterization of a new cold-active lipase from a deep-sea sediment metagenome

2009 ◽  
Vol 81 (5) ◽  
pp. 865-874 ◽  
Author(s):  
Jeong Ho Jeon ◽  
Jun-Tae Kim ◽  
Yun Jae Kim ◽  
Hyung-Kwoun Kim ◽  
Hyun Sook Lee ◽  
...  
Keyword(s):  
Deep Sea ◽  
Deep Sea Sediment ◽  
Cold Active ◽  
Active Lipase

scholarly journals A Novel Cold-Active Lipase from Candida albicans: Cloning, Expression and Characterization of the Recombinant Enzyme

2011 ◽  
Vol 12 (6) ◽  
pp. 3950-3965 ◽  
Author(s):  
Dong-Ming Lan ◽  
Ning Yang ◽  
Wen-Kai Wang ◽  
Yan-Fei Shen ◽  
Bo Yang ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Recombinant Enzyme ◽  
Cold Active ◽  
Active Lipase

scholarly journals Molecular and biochemical characterization of a novel cold-active and metal ion-tolerant GH10 xylanase from frozen soil

2017 ◽  
Vol 31 (5) ◽  
pp. 955-963 ◽  
Author(s):  
Haiyan Qiu ◽  
Zhongyuan Li ◽  
Hui Wang ◽  
Haiying Zhang ◽  
Shuang Li ◽  
...  
Keyword(s):  
Metal Ion ◽  
Biochemical Characterization ◽  
Frozen Soil ◽  
Cold Active ◽  
Gh10 Xylanase
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