Changes in Soil Protease Activity and Numbers of Culturable Bacteria in Upland Fields by the Application of Liquid Livestock Feces

2005 ◽  
Vol 51 (4) ◽  
pp. 491-496 ◽  
Author(s):  
Katsuji Watanabe ◽  
Hiroshi Niimi
Keyword(s):  
Protease Activity ◽  
Culturable Bacteria ◽  
Soil Protease ◽  
Livestock Feces

scholarly journals Synthesis of methods used to assess soil protease activity

2021 ◽  
Vol 158 ◽  
pp. 108277
Author(s):  
Lucy M. Greenfield ◽  
Jérémy Puissant ◽  
Davey L. Jones
Keyword(s):  
Protease Activity ◽  
Soil Protease

Azocoll protease activity assay

2007 ◽  
Author(s):  
Naxin Jiang ◽  
Nguan Soon Tan ◽  
Bow Ho ◽  
Jeak Ling Ding
Keyword(s):  
Protease Activity ◽  
Activity Assay

Extraction and Partial Purification of Protease from Bilimbi (Averrhoa bilimbi L.)

2013 ◽  
Vol 10 (2) ◽  
pp. 29
Author(s):  
Normah Ismail ◽  
Nur' Ain Mohamad Kharoe
Keyword(s):  
Molecular Weight ◽  
Protein Content ◽  
Ammonium Sulfate ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Protease Activity ◽  
Protein Concentration ◽  
Temperature Stability ◽  
Partial Purification ◽  
Ammonium Sulfate Precipitation

Unripe and ripe bilimbi (Averrhoa bilimbi L.) were ground and the extracted juices were partially purified by ammonium sulfate precipitation at the concentrations of 40 and 60% (w/v). The collected proteases were analysed for pH, temperature stability, storage stability, molecular weight distribution, protein concentration and protein content. Protein content of bilimbi fruit was 0.89 g. Protease activity of both the unripe and ripe fruit were optimum at pH 4 and 40°C when the juice were purified at 40 and 60% ammonium sulfate precipitation. A decreased in protease activity was observed during the seven days of storage at 4°C. Molecular weight distribution indicated that the proteases protein bands fall between IO to 220 kDa. Protein bands were observed at 25, 50 and 160 kDa in both the unripe and ripe bilimbi proteases purified with 40% ammonium sulfate, however, the bands were more intense in those from unripe bilimbi. No protein bands were seen in proteases purified with 60% ammonium sulfate. Protein concentration was higher for proteases extracted with 40% ammonium sulfate at both ripening stages. Thus, purification using 40% ammonium sulfate precipitation could be a successful method to partially purify proteases from bilimbi especially from the unripe stage. 

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