Screening and evaluation of natural coagulants for water treatment

2007 ◽  
Vol 7 (5-6) ◽  
pp. 19-25 ◽  
Author(s):  
K.R. Gunaratna ◽  
B. Garcia ◽  
S. Andersson ◽  
G. Dalhammar

In developing countries many people are forced to drink turbid water and as a consequence many children are dying related to water borne diseases. Hence there is a need for inexpensive and easy methods to purify drinking water. The objective of this research is to screen different plant seeds to find a primary natural coagulant able to reduce the turbidity of the drinking water. The protein from 21 different seeds was extracted with water and salt solution and coagulation properties in synthetic clay solution were studied. The crude extract of Moringa oleifera (MO) showed the same coagulation activity as that of alum. The protein from red bean, sugar maize and red maize were promising in having coagulation activity, compared with a known coagulant protein from MO. These seeds were selected and purified to homogeneity with fast flow Sepharose ion exchange chromatography and the properties of the purified proteins were characterized. The characteristics of these coagulant proteins are different from MO protein based on molecular weight and ionic determinations. The coagulant proteins were temperature tolerant and can withstand temperature of around 85 °C and maintain the coagulation activity. The seeds identified as a coagulant source could be used as an alternative to chemicals for drinking water clarification.

2011 ◽  
Vol 74 (3-4) ◽  
pp. 209-214 ◽  
Author(s):  
Ying Wang ◽  
Peiyin Zhang ◽  
Shujun Liu ◽  
Yongsheng Zhang ◽  
Tiesuo Zhao ◽  
...  

2007 ◽  
pp. 3-10
Author(s):  
Mirjana Antov ◽  
Marina Sciban ◽  
Slavica Adamovic ◽  
Mile Klasnja

Investigation of an extraction procedure of protein coagulants from common bean seed regarding concentration of NaCl and pH was performed. High values of protein concentration and coagulation activity in crude extract (9.19 g/l and 23.9%, respectively) were obtained when the extraction was performed using 0.5 mol/l NaCl and water as solvent, which represents an advantage for economic and environmental reasons. Crude extract of common bean seed was purified by precipitation at two different percentages of (NH4)2SO4 saturation, followed by batch ion-exchange chromatography. The highest obtained coagulation activity, 45%, was determined in fraction that was eluated at 1.75 mol/l NaCl from resin loaded with proteins precipitated upon 80-100% (NH4)2SO4 saturation. High values of coagulation activity showed by some eluates suggest their application as natural coagulant for water purification. .


Proceedings ◽  
2019 ◽  
Vol 48 (1) ◽  
pp. 24
Author(s):  
Estefanía Avilés Sacoto ◽  
Paola Verlicchi

Even though Ecuador is a country with one of the highest concentration of rivers per square kilometer, its water resources are of poor quality d there is a lack of drinking water and sewage systems for its population. In 2013, only 34% of the rural population had access to drinking water and 25% to sewerage services. This is because of a lack of infrastructure and the necessary budgets allocated to them. This paper deals with a proposal for water purification that consists of the use of the Moringa olifeira plant to facilitate the flocculation process, considering that its use reduces the costs associated with the water treatment and minimizes the concentration of metals in the residual sludge. The dosage effects of the plant seeds during the flocculation processes were explored with Jar tests using a solution in doses from 250 to 350 mg per liter of water and then evaluating Chemical Oxygen Demand (COD) and turbidity as selected response variables. The COD reduction goes from the 45% to 55% while the turbidity reduction goes from the 77% to 81%, making the use of the plant possible and feasible.


1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.


1984 ◽  
Vol 51 (01) ◽  
pp. 016-021 ◽  
Author(s):  
S Birken ◽  
G Agosto ◽  
B Lahiri ◽  
R Canfield

SummaryIn order to investigate the early release of NH2-terminal plasmic fragments from the Bβ chain of fibrinogen, substantial quantities of Bβ 1-42 and Bβ 1-21 are required as immunogens, as radioimmunoassay standards and for infusion into human volunteers to determine the half-lives of these peptides. Towards this end methods that employ selective proteolytic cleavage of these fragments from fibrinogen have been developed. Both the N-DSK fragment, produced by CNBr cleavage of fibrinogen, and Bβ 1-118 were employed as substrates for plasmin with the finding of higher yields from N-DSK. Bβ 1-42 and Bβ 1-21 were purified by gel filtration and ion-exchange chromatography on SP-Sephadex using volatile buffers. When the purified preparation of Bβ 1-42 was chromatographed on reverse-phase high performance liquid chromatography, two peaks of identical amino acid composition were separated, presumably due either to pyroglutamate or to amide differences.


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