Purification and characterization of an extracellular serine protease from Clonostachys rosea and its potential as a pathogenic factor

2006 ◽  
Vol 41 (4) ◽  
pp. 925-929 ◽  
Author(s):  
Jun Li ◽  
Jinkui Yang ◽  
Xiaowei Huang ◽  
Ke-Qin Zhang
Archaea ◽  
2006 ◽  
Vol 2 (1) ◽  
pp. 51-57 ◽  
Author(s):  
Malashetty Vidyasagar ◽  
S. Prakash ◽  
Carol Litchfield ◽  
K. Sreeramulu

A novel haloalkaliphilic, thermostable serine protease was purified from the extreme halophilic archaeon,Halogeometricum borinquensestrain TSS101. The protease was isolated from a stationary phase culture, purified 116-fold with 18% yield and characterized biochemically. The molecular mass of the purified enzyme was estimated to be 86 kDa. The enzyme showed the highest activity at 60 °C and pH 10.0 in 20% NaCl. The enzyme had high activity over the pH range from 6.0 to 10.0. Enzymatic activity was strongly inhibited by 1 mM phenyl methylsulfonyl fluoride, but activity was increased 59% by 0.1% cetyltrimethylammonium bromide. The enzyme exhibited relatively high thermal stability, retaining 80% of its activity after 1 h at 90 °C. Thermostability increased in the presence of Ca2+. The stability of the enzyme was maintained in 10% sucrose and in the absence of NaCl.


2011 ◽  
Vol 46 (9) ◽  
pp. 1711-1716 ◽  
Author(s):  
Mitsuhiro Ueda ◽  
Takayuki Yamashita ◽  
Masami Nakazawa ◽  
Kazutaka Miyatake ◽  
Satoshi Ohki ◽  
...  

2004 ◽  
Vol 27 (5) ◽  
pp. 311-318 ◽  
Author(s):  
Andreina Cesari ◽  
Claudio Santiago Cacciato ◽  
Rosana Esther De Castro ◽  
Jorge Julian Sanchez

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