Cloning, Expression, Purification, and Characterization of Cold-Adapted α-Amylase from Pseudoalteromonas arctica GS230

2010 ◽  
Vol 29 (8) ◽  
pp. 591-597 ◽  
Author(s):  
Mingsheng Lu ◽  
Shujun Wang ◽  
Yaowei Fang ◽  
Huangzhong Li ◽  
Shu Liu ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Cold Adapted ◽  
Pseudoalteromonas Arctica

scholarly journals Cloning, purification, and characterization of a cold-adapted esterase produced byPsychrobacter cryohalolentisK5Tfrom Siberian cryopeg

2012 ◽  
Vol 82 (2) ◽  
pp. 367-375 ◽  
Author(s):  
Ksenia Novototskaya-Vlasova ◽  
Lada Petrovskaya ◽  
Sergey Yakimov ◽  
David Gilichinsky
Keyword(s):  
Purification And Characterization ◽  
Cold Adapted

Purification and characterization of a cold-adapted pullulanase from a psychrophilic bacterial isolate

Extremophiles ◽  
2014 ◽  
Vol 18 (6) ◽  
pp. 1095-1102 ◽  
Author(s):  
Farah Qoura ◽  
Skander Elleuche ◽  
Thomas Brueck ◽  
Garabed Antranikian
Keyword(s):  
Bacterial Isolate ◽  
Purification And Characterization ◽  
Cold Adapted

A cold-adapted esterase of a novel marine isolate, Pseudoalteromonas arctica: gene cloning, enzyme purification and characterization

Extremophiles ◽  
2010 ◽  
Vol 14 (3) ◽  
pp. 273-285 ◽  
Author(s):  
Rami Al Khudary ◽  
Ramprasath Venkatachalam ◽  
Moritz Katzer ◽  
Skander Elleuche ◽  
Garabed Antranikian
Keyword(s):  
Gene Cloning ◽  
Enzyme Purification ◽  
Purification And Characterization ◽  
Cold Adapted ◽  
Marine Isolate ◽  
Pseudoalteromonas Arctica

Purification and characterization of a psychrophilic catalase from Antarctic Bacillus

2008 ◽  
Vol 54 (10) ◽  
pp. 823-828 ◽  
Author(s):  
Wei Wang ◽  
Mi Sun ◽  
Wanshun Liu ◽  
Bin Zhang
Keyword(s):  
Activation Energy ◽  
Low Temperatures ◽  
Catalytic Efficiency ◽  
Small Subunit ◽  
Purification And Characterization ◽  
Cold Adapted ◽  
Optimal Activity ◽  
Ph Range ◽  
Antarctic Seawater

Catalase from Bacillus sp. N2a (BNC) isolated from Antarctic seawater was purified to homogeneity. BNC has a molecular mass of about 230 kDa and is composed of four identical subunits of 56 kDa. The catalase showed optimal activity at 25 °C and at a pH range of 6–11. The enzyme could be inhibited by azide, hydroxylamine, and mercaptoethanol. These characteristics suggested that BNC is a small-subunit monofunctional catalase. The activation energy of BNC was 13 kJ/mol and the apparent kcat/Km values were 3.6 × 106 and 4 × 106 L·mol–1·s–1 at 4 and 25 °C, respectively. High catalytic efficiency of BNC at low temperatures enables this bacterium to scavenge H2O2 efficiently. BNC exhibited activation energy, catalytic efficiency, and thermostability comparable with some mesophilic homologues. Such similarity of enzymatic characteristics to mesophilic homologues, although uncommon among the cold-adapted enzymes in general, has also been observed in other psychrophilic small-subunit monofunctional catalases.

Purification and characterization of two cold-adapted extracellular tannin acyl hydrolases from an Antarctic strain Verticillium sp. P9

2007 ◽  
Vol 77 (1) ◽  
pp. 77-89 ◽  
Author(s):  
Monika Kasieczka-Burnecka ◽  
Karina Kuc ◽  
Halina Kalinowska ◽  
Monika Knap ◽  
Marianna Turkiewicz
Keyword(s):  
Purification And Characterization ◽  
Cold Adapted
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