Isolation and characterization of a flocculating protein from Moringa oleifera Lam

Gassenschmidt, U.; Jany, Klaus‐Dieter; Tauscher, B.; Niebergall, H

doi:10.1016/0304-4165(94)00176-x

Cited by 297 publications

(195 citation statements)

References 9 publications

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“…These results suggest that the active molecule is water soluble and has a low molecular weight (< 12 kDa). Considering that hemagglutination activity was observed in this fraction (Table 1), a strong candidate for ovicidal activity is a flocculation protein from M. oleifera with a molecular mass of 6.5 kDa (GASSENSCHMIDT et al, 1995;NDABIGENGESERE et al, 1995), which has reportedly shown larvicidal activity (COELHO et al, 2009) andovicidal activity against A. aegypti (SANTOS et al, 2012). However, the CENR fraction from M. oleifera showed other protein activities that cannot be ignored, such as hemolysin and protease inhibitors (Table 1).…”

Section: Discussionmentioning

confidence: 99%

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus

Salles

Braga

Nascimento³

et al. 2014

Rev. Bras. Parasitol. Vet.

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Bioactive molecules of plant species are promising alternatives for the chemical control of gastrointestinal nematodes in ruminants. Extracts of native and exotic seed species from Brazil's semi-arid region were tested in vitro in an egg hatch assay and the bioactivity of their proteins was investigated. Each seed species was subjected to three extractions with three types of solvents. All the seeds showed ovicidal activity, which varied according to the solvents. Higher ovicidal activity was found in the molecule fractions of low molecular weight (<12 kDa) for Albizia lebbeck, Ipomoea asarifolia, Jatropha curcas, Libidibia ferrea, Moringa oleifera and Ricinus communis (P<0.05, Bonferroni test). The two fractions of Crotalaria spectabilis showed the same ovicidal activity (P>0.05, Bonferroni test). Hemagglutinating activity was detected in the fractions of C. spectabilis and M. oleifera fractions, hemolysin activity in the A. lebbeck and M. oleifera fractions, serine protease inhibitory activity in the A. lebbeck, I. asarifolia, J. curcas, M. oleifera and R. communis fractions, cysteine protease inhibitor activity in the M. oleifera fraction, and no protein activity in the L. ferrea fraction. The results of this work reveal new plant species with a potential for use in controlling nematode parasites in goats, thus opening a new field of research involving plant protein molecules with ovicidal properties.Keywords: Goats, nematodes, egg hatch assay, lectin, protease inhibitors, hemolysin. ResumoMoléculas bioativas de espécies vegetais são alternativas promissoras ao controle químico dos nematoides gastrintestinais em ruminantes. Extratos de sementes de espécies nativas e exóticas do Semiárido Brasileiro foram testados in vitro em ensaio de eclosão de ovos e investigada a natureza proteica da bioatividade. Três extrações com três solventes foram feitas para cada semente estudada. Todas as sementes apresentaram atividade ovicida, variando com o solvente utilizado. Maior taxa de inibição da eclosão concentrou-se nas frações de moléculas de baixa massa molecular (<12 kDa) para Albizia lebbeck, Ipomoea asarifolia, Jatropha curcas, Libidibia ferrea, Moringa oleifera e Ricinus communis (P<0,05, teste de Bonferroni). Crotalaria spectabilis mostrou atividade nas duas frações, sem diferença entre elas (P>0,05, teste de Bonferroni). Observou-se atividade hemaglutinante nas frações de C. spectabilis e M. oleifera, de hemolisina em A. lebbeck e M. oleifera, de atividade inibidora de protease da serina em A. lebbeck, I. asarifolia, J. curcas, M. oleifera

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Section: Discussionmentioning

confidence: 99%

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus

Salles

Braga

Nascimento³

et al. 2014

Rev. Bras. Parasitol. Vet.

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“…Ongoing research is attempting to characterize and purify the coagulant components of Moringa seeds (Ndabigengesere et al, 1995;Gassenschmidt et al, 1995). It is believed that the seed is an organic natural polymer (Jahn, 1984).…”

Section: Moringa Seeds As Coagulantmentioning

confidence: 99%

“…It has been described as adsorption and charge neutralization (Ndabigengesere et al, 1995;Gassenschmidt et al, 1995) and interparticle bridging (Muyibi and Evison, 1995a). Flocculation by inter-particle bridging is mainly characteristic of high molecular weight polyelectrolytes.…”

Section: Moringa Seeds As Coagulantmentioning

confidence: 99%

Moringa oleifera: a food plant with multiple medicinal uses

Anwar

Latif

Ashraf

et al. 2006

Phytotherapy Research

1,496

1,048

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“…MC is a heterogeneous, cationic biopolymer of molecular weight 6-12 kDa and isoelectric point between 10 and 11, obtained by aqueous extraction of Moringa seeds belonging to family Moringaceae, which has been used for the purification of water since time immemorial (7,23). Structural and amino acid analysis of MC has revealed a total of 60 residues having high contents of glutamine, arginine, and proline in the sequence; "QGPGRQPDFQRCGQQLRNISPPQRCPSLRQAVQLTH-QQQGQVGPQQVRQMYRVASNIPST" (8). Spray drying being expensive and non-green limits the complete exploitation of solid dispersion technology.…”

Section: Introductionmentioning

confidence: 99%

Solid-State Characterization and Dissolution Properties of Meloxicam–Moringa Coagulant–PVP Ternary Solid Dispersions

et al. 2013

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Abstract. The effect of ternary solid dispersions of poor water-soluble NSAID meloxicam with moringa coagulant (obtained by salt extraction of moringa seeds) and polyvinylpyrrolidone on the in vitro dissolution properties has been investigated. Binary (meloxicam-moringa and meloxicam-polyvinylpyrrolidone (PVP)) and ternary (meloxicam-moringa-PVP) systems were prepared by physical kneading and ball milling and characterized by Fourier transform infrared spectroscopy, differential scanning calorimetry, and X-ray diffractometry. The in vitro dissolution behavior of meloxicam from the different products was evaluated by means of United States Pharmacopeia type II dissolution apparatus. The results of solid-state studies indicated the presence of strong interactions between meloxicam, moringa, and PVP which were of totally amorphous nature. All ternary combinations were significantly more effective than the corresponding binary systems in improving the dissolution rate of meloxicam. The best performance in this respect was given by the ternary combination employing meloxicam-moringa-PVP ratio of [1:(3:1)] prepared by ball milling, with about six times increase in percent dissolution rate, whereas meloxicam-moringa (1:3) and meloxicam-PVP (1:4) prepared by ball milling improved dissolution of meloxicam by almost 3-and 2.5-folds, respectively. The achieved excellent dissolution enhancement of meloxicam in the ternary systems was attributed to the combined effects of impartation of hydrophilic characteristic by PVP, as well as to the synergistic interaction between moringa and PVP.

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Isolation and characterization of a flocculating protein from Moringa oleifera Lam

Cited by 297 publications

References 9 publications

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus

Lectin, hemolysin and protease inhibitors in seed fractions with ovicidal activity against Haemonchus contortus

Moringa oleifera: a food plant with multiple medicinal uses

Solid-State Characterization and Dissolution Properties of Meloxicam–Moringa Coagulant–PVP Ternary Solid Dispersions

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