Purification and Characterization of 56 kDa cold active Protease from Serratia marcescens

2011 ◽  
Vol 5 (32) ◽  
Author(s):  
A.L. TARIQ
Keyword(s):  
Serratia Marcescens ◽  
Purification And Characterization ◽  
Cold Active ◽  
Active Protease

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 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.

scholarly journals Isolation and characterization of a new cold-active protease from psychrotrophic bacteria of Western Himalayan glacial soil

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Saleem Farooq ◽  
Ruqeya Nazir ◽  
Shabir Ahmad Ganai ◽  
Bashir Ahmad Ganai
Keyword(s):  
Specific Activity ◽  
Temperature Range ◽  
Psychrotrophic Bacteria ◽  
Isolation And Characterization ◽  
Cold Active ◽  
Active Protease ◽  
Quantitative Screening ◽  
First Time ◽  
Low K

AbstractAs an approach to the exploration of cold-active enzymes, in this study, we isolated a cold-active protease produced by psychrotrophic bacteria from glacial soils of Thajwas Glacier, Himalayas. The isolated strain BO1, identified as Bacillus pumilus, grew well within a temperature range of 4–30 °C. After its qualitative and quantitative screening, the cold-active protease (Apr-BO1) was purified. The Apr-BO1 had a molecular mass of 38 kDa and showed maximum (37.02 U/mg) specific activity at 20 °C, with casein as substrate. It was stable and active between the temperature range of 5–35 °C and pH 6.0–12.0, with an optimum temperature of 20 °C at pH 9.0. The Apr-BO1 had low Km value of 1.0 mg/ml and Vmax 10.0 µmol/ml/min. Moreover, it displayed better tolerance to organic solvents, surfactants, metal ions and reducing agents than most alkaline proteases. The results exhibited that it effectively removed the stains even in a cold wash and could be considered a decent detergent additive. Furthermore, through protein modelling, the structure of this protease was generated from template, subtilisin E of Bacillus subtilis (PDB ID: 3WHI), and different methods checked its quality. For the first time, this study reported the protein sequence for psychrotrophic Apr-BO1 and brought forth its novelty among other cold-active proteases.

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 highly active protease from Bacillus subtilis-150

2010 ◽  
Vol 46 (5) ◽  
pp. 833-834
Author(s):  
K. T. Normurodova ◽  
A. A. Makhsumkhanov ◽  
B. Kh. Alimova ◽  
O. M. Pulatova ◽  
N. I. Bozorov
Keyword(s):  
Bacillus Subtilis ◽  
Purification And Characterization ◽  
Highly Active ◽  
Active Protease

scholarly journals Purification and characterization of a Serratia marcescens nuclease produced by Escherichia coli

1989 ◽  
Vol 54 (1) ◽  
pp. 17-27 ◽  
Author(s):  
Kirsten Biedermann ◽  
Pia Knak Jepsen ◽  
Erik Riise ◽  
Ib Svendsen
Keyword(s):  
Escherichia Coli ◽  
Serratia Marcescens ◽  
Purification And Characterization
Sign in / Sign up

Export Citation Format

Share Document