Purification and characterization of the cold-active killer toxin from the psychrotolerant yeast Mrakia frigida isolated from sea sediments in Antarctica

2012 ◽  
Vol 47 (5) ◽  
pp. 822-827 ◽  
Author(s):  
Guang-Lei Liu ◽  
Ke Wang ◽  
Ming-Xia Hua ◽  
Muhammad Aslam Buzdar ◽  
Zhen-Ming Chi
Keyword(s):  
Killer Toxin ◽  
Purification And Characterization ◽  
Cold Active ◽  
Psychrotolerant Yeast

Purification and characterization of a cold-active protease from psychrotrophicSerratia marcescensAP3801

1997 ◽  
Vol 74 (11) ◽  
pp. 1377-1383 ◽  
Author(s):  
Yasutaka Morita ◽  
Kenji Kondoh ◽  
Quamrul Hasan ◽  
Toshifumi Sakaguchi ◽  
Yuji Murakami ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Cold Active ◽  
Active Protease

Purification and characterization of cold-active endo-1,4-β-glucanase produced by Pseudoalteromonas sp. AN545 from Antarctica

2011 ◽  
Vol 29 (5) ◽  
pp. 1086-1092
Author(s):  
Jihong Shen ◽  
Guangfeng Kan ◽  
Cuijuan Shi ◽  
Zhenhuan Lei ◽  
Qiuju Xie ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Cold Active

Isolation, Purification, and Characterization of a Cold-Active Lipase fromAspergillus nidulans

2000 ◽  
Vol 48 (1) ◽  
pp. 105-109 ◽  
Author(s):  
Isabel Mayordomo ◽  
Francisca Randez-Gil ◽  
Jose A. Prieto
Keyword(s):  
Purification And Characterization ◽  
Cold Active ◽  
Active Lipase

Purification and Characterization of an Extracellular Cold-Active Protease Produced by the Psychrotrophic Bacterium serratia Sp. WJ39

2014 ◽  
Vol 618 ◽  
pp. 330-334 ◽  
Author(s):  
Xiu Ling Ji ◽  
Muhammad Kamran Taj ◽  
Xiao Bo Lu ◽  
Lian Bing Lin ◽  
Qi Zhang ◽  
...  
Keyword(s):  
Residual Activity ◽  
Leather Industry ◽  
Purification And Characterization ◽  
Suitable Candidate ◽  
Optimal Activity ◽  
Sds Page ◽  
Cold Active ◽  
Active Protease ◽  
Ph Range

Proteases have diverse applications in a wide variety of industries, such as in detergent, leather, food, pharmaceutical and silk. The extracellular cold-active protease was purified from the psychrotrophic bacteriumSerratiasp. WJ39 from a meat factory. The protease was cold-active with a molecular mass of 47.6 kDa estimated on SDS-PAGE. It showed an optimal activity at pH of 8 and was stable at pH 6 to 10, while its optimal temperature was 37°C and it was stable at 0-25°C, even remained 35% residual activity at 0°C. The protease was totally inhibited by PMSF which was telling that the purified enzyme was a serine protease. The properties like moderate thermostability, activity in a broad pH range and resistance to metal ions make this enzyme a suitable candidate for the possible use in food and leather industry.

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