scholarly journals Isolation of natural inhibitors of papain obtained from Carica papaya latex

2004 ◽  
Vol 47 (5) ◽  
pp. 747-754 ◽  
Author(s):  
Rubens Monti ◽  
Jonas Contiero ◽  
Antonio José Goulart
Keyword(s):  
Positive Reaction ◽  
Carica Papaya ◽  
Competitive Inhibition ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Negative Reaction ◽  
Ionic Exchange ◽  
Papaya Latex ◽  
Carica Papaya Latex ◽  
Natural Inhibitors

Studies were carried out to natural papain inhibitor from papaya latex. Fresh latex from green fruits of Carica papaya was collected and immediately transported in ice bath to the lab, from which three fractions with inhibitor effect of esterase papain activity were isolated by latex dialysis, Sephadex G-25 gel filtration and ionic exchange chromatography in SP-Sephadex C-25. The isolated fractions, identified as inhibitors I and II, showed a negative reaction with ninhydrin; however, the fraction identified as P-III showed positive reaction with ninhydrin. Kinetics data showed non-competitive inhibition (inhibitor I) and uncompetitive (inhibitors II and P-III).

scholarly journals Salivary apyrase of Rhodnius prolixus. Kinetics and purification

1986 ◽  
Vol 233 (3) ◽  
pp. 885-891 ◽  
Author(s):  
J J F Sarkis ◽  
J A Guimarães ◽  
J M C Ribeiro
Keyword(s):  
Atp Hydrolysis ◽  
Competitive Inhibition ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Rhodnius Prolixus ◽  
Exchange Chromatography ◽  
Phosphate Esters ◽  
Inorganic Pyrophosphatase ◽  
Blood Sucking ◽  
Specific Activities

The salivary apyrase activity of the blood-sucking bug Rhodnius prolixus was found to reside in a true apyrase (ATP diphosphohydrolase, EC 3.6.1.5) enzyme. The crude saliva was devoid of 5′-nucleotidase, inorganic pyrophosphatase, phosphatase and adenylate kinase activities. ATP hydrolysis proceeded directly to AMP and Pi without significant accumulation of ADP. Km values for ATP and ADP hydrolysis were 229 and 291 microM respectively. Ki values for ATP and ADP inhibition of ADP and ATP hydrolysis were not different from the Km values, and these experiments indicated competitive inhibition. Activities were purified 126-fold by combined gel filtration and ion-exchange chromatography procedures with a yield of 63%. The purified enzyme displayed specific activities of 580 and 335 mumol of Pi released/min per mg of protein for ATP and ADP hydrolysis respectively. The action of the purified enzyme on several phosphate esters indicates that Rhodnius apyrase is a non-specific nucleosidetriphosphate diphosphohydrolase.

scholarly journals Hydrolytic properties of Carica papaya latex and latex preparations

1937 ◽  
Vol 31 (11) ◽  
pp. 1926-1933 ◽  
Author(s):  
Max Frankel ◽  
Regina Maimin ◽  
Benjamin Shapiro
Keyword(s):  
Carica Papaya ◽  
Papaya Latex ◽  
Carica Papaya Latex

scholarly journals Purification of papain from fresh latex of Carica papaya

2000 ◽  
Vol 43 (5) ◽  
pp. 501-507 ◽  
Author(s):  
Rubens Monti ◽  
Carmelita A. Basilio ◽  
Henrique C. Trevisan ◽  
Jonas Contiero
Keyword(s):  
Carica Papaya ◽  
Specific Activity ◽  
Polyacrylamide Gel ◽  
Single Band ◽  
Enzymatic Assays ◽  
Papaya Latex ◽  
High Concentrations ◽  
Natural Inhibitors

In the present study we wish to report a method of crystallizing papain from fresh papaya latex which gave higher yields than previously reported. This method does not involve the use of sulphydryl reagents. The papain thus obtained is practically pure and shows a single band when submitted to electrophoresis on polyacrylamide gel, and is identical to the papain obtained by other methods. In routine enzymatic assays, specific activity was measured using Z-gly-pNP and BAEE as substrates. Papain crystallized by this method, without the use of high concentrations of salts or thiol-containing substances such as cysteine and dithiothreitol, is obtained in the form of a complex with natural inhibitors existent in latex which can be removed by dialysis.

scholarly journals Physico-Chemical Treatment of a Wastewater Collector Loaded with Metals and Suspension Material by The Solution of Raw Carica papaya Latex

2020 ◽  
pp. 42-49
Author(s):  
Togbe Finagnon Crépin Alexis ◽  
Yete Pélagie ◽  
Yovo Franck ◽  
Wotto Valentin
Keyword(s):  
Suspended Matter ◽  
Water Samples ◽  
Carica Papaya ◽  
Metal Removal ◽  
Tropical Plant ◽  
Iron Copper ◽  
Physico Chemical ◽  
Copper Zinc ◽  
Papaya Latex ◽  
Carica Papaya Latex

The papaya (Carica papaya), of the family Caricaceae, is a tree-like tropical plant, native to Central and South America. Papaya cultivation extends to all warm and humid countries. The present study consists in using the solution of raw Carica papaya latex (SLCP) cultivated in Benin as a natural biodegradable flocculant in a physico-chemical process to treat liquid discharges loaded with metals including iron, copper, zinc, and manganese; and suspended matter, and also to test its efficiency against other products commonly used in wastewater treatment. The tests were carried out on water samples from the wastewater collector that runs through the Agla district in Cotonou. The comparative study with a commonly used flocculant, aluminium sulphate, showed outstanding competitiveness with a high flocculation power for the solution of Carica papaya raw latex. In six water samples from the collector with average concentrations of iron, copper, zinc and manganese of 18.20 mg/L ; 2.50mg/L ; 3.80 mg/L and 3.70 mg/L respectively, the percentages of metal removal exceeded 90% for iron and manganese and around 85% for copper and zinc with the combination FeCl3 + SLCP. The NaOH + SLCP combination showed a very significant effect on the removal of metals (96% reduction) and suspended matter.

scholarly journals PURIFICATION AND CHARACTERIZATION OF SALIVARY AMYLASE INHIBITOR EXTRACTED FROM BARLEY

2016 ◽  
Vol 47 (4) ◽  
Author(s):  
Abood & Hakeem
Keyword(s):  
Ammonium Sulfate ◽  
Specific Activity ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Exchange Chromatography ◽  
Alpha Amylase ◽  
Ionic Exchange ◽  
Inhibition Activity ◽  
Amylase Inhibitors

Amylase inhibitors were purified by many sequential steps included concentration by gradual addition of ammonium sulfate at  saturation ratios. ranged from 0 to 90% . The best ratio of saturation was found to be 70% as the specific activity and inhibition activity toward Human alpha-amylase(HAS)  were the highest ( 8 U/mg and 6 U/ml respectively as compared to those of the rest ratios, the ratio of saturation with ammonium sulfate 60 % and then 50%, (5.8 ,5.5  )U/ml and( 7.7 ،7 )U/mg respectively for inhibition activity and specific activity and for  40% ,30%20%  saturation  the inhibition activity and specific activity were(5 ،4.8 ،4 ) u/ml (6.6 ،6 ،5.8) u/mg respectively .The precepitation step was followed by ionic exchange chromatography technique by DEAE-cellulose column( 3×11 )cm and the results showed that there was one peak with inhibition activity toward (HAS). Further  purification steps were conducted using gel filtration on Sephacryl S-200 column    (1.5  ×  60)cm; the purification folds was5.59 times with outcome of 46.5%.The results of alpha-amylase inhibitors characterization showed that the molecular weight was about 23.44 and 22.9  kDa  as determined by electrophoresis and gel filteration respectively.                                         

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