Flow curve-molecular weight distribution: Is the solution of the inverse problem possible?

1991 ◽  
Vol 31 (22) ◽  
pp. 1590-1596 ◽  
Author(s):  
Alexander Ya. Malkin ◽  
Albert E. Teishev
Keyword(s):  
Molecular Weight ◽  
Inverse Problem ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Flow Curve

Obtaining the kinetic function of depolymerization from evolving molecular weight distribution data-an inverse problem

AIChE Journal ◽  
2012 ◽  
Vol 59 (3) ◽  
pp. 912-922 ◽  
Author(s):  
Y. Leong Yeow ◽  
Bifei Guan ◽  
Liang Wu ◽  
Tze-Ming Yap ◽  
Jong-Leng Liow ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Inverse Problem ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Distribution Data ◽  
Kinetic Function

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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