A novel and efficient and low-cost methodology for purification of Macrotyloma axillare (Leguminosae) seed lectin

Santana, Marcos Aurélio de; Santos, Alexandre Martins Costa; Oliveira, Marcelo Elias de; Oliveira, Jamil S.; Baba, Elio H.; Santoro, Marcelo M.; Andrade, Milton Hércules Guerra de

doi:10.1016/j.ijbiomac.2008.07.011

Cited by 11 publications

(7 citation statements)

References 28 publications

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“…Ethylenediaminetetraacetic acid (EDTA) is a divalent metal ion-chelating agent. When the lectin fully reacted with EDTA, the hemagglutinating activity of lectin was lost, and the reaction was generally reversible [35].…”

Section: Resultsmentioning

confidence: 99%

“…Compared with the results of antibacterial experiments, the Zihua snap bean lectin can inhibit the growth of P. infestans at a high concentration. According to de Santana [35], only a few lectins had significant antifungal activity. In addition, lectins from kidney beans have inhibitory effects on four harmful fungi ( Helminthosporium maydis , Sclerotinia sclerotiorum , Gibberalla sanbinetti, and Rhizoctonia solani ) in agriculture [52].…”

Section: Resultsmentioning

confidence: 99%

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Two-Step Isolation, Purification, and Characterization of Lectin from Zihua Snap Bean (Phaseolus vulgaris) Seeds

Jiang

Wang

et al. 2019

Polymers

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A two-step method based on an aqueous two-phase system and Sephadex G-75 was used to separate and purify lectin from the seeds of the Zihua snap bean. The preliminary properties and bioactivity of the Zihua snap bean lectin were characterized by different instrumental methods, such as sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE), liquid chromatography-nano electrospray ionization mass spectrometry (Nano LC-ESI-MS/MS), and Fourier transform infrared spectroscopy (FTIR). The hemagglutinating activity of the Zihua snap bean lectin could not be inhibited by glucose, N-acetyl-d-glucosamine, d-galactose, N-acetyl-d-galactosamine, fructose, sucrose, d-maltose, d-trehalose, and lactose. It was found that the hemagglutinating activity of the lectin showed strong dependence on Mn2+ and Ca2+. The thermal and pH stability of the Zihua snap bean lectin was studied by FTIR and fluorescence spectroscopy. Relatively good stability was observed when the temperature was not higher than 70 °C, as well as in the pH range of 2.0 to 10.0. Digestive stability in vitro was investigated. The untreated lectin was relatively stable to pepsin and trypsin activity, but heat treatment could significantly reduce the digestive stability in vitro. Moreover, the lectin showed an inhibitory effect on the tested bacteria (Staphylococcus aureus (S. aureus), Escherichia coli (E. coli), Bacillus subtilis (B. subtilis)), and it also showed a certain inhibitory effect on the growth of Phytophthora infestans (P. infestans) at higher concentrations.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Two-Step Isolation, Purification, and Characterization of Lectin from Zihua Snap Bean (Phaseolus vulgaris) Seeds

Jiang

Wang

et al. 2019

Polymers

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“…Chromatographic methods can be time-consuming and expensive, leading to the loss of biological activity and a poor yield of the entire process. The affinity chromatography maintenance is a hardy task when plant crude extracts are loaded into columns because such samples contain pigments, oily components, proteolytic enzymes, and other complex substances that could damage the column and impair the purification (Santana et al, 2008). Therefore, due to the great importance of the lectins in the biological and medical field, it is essential to develop new purification methods that are not only more economical and selective but can also handle high contents of solids and complex substances and also allow for process integration.…”

Section: Introductionmentioning

confidence: 99%

An overview of lectins purification strategies

Nascimento

Cunha

Nascimento

et al. 2012

J of Molecular Recognition

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Lectins hold great promise not only as reagents for diagnostics and drug discovery but also as a novel class of biopharmaceutical products. In fact, new research directions in the last years have led to major developments in the uses of plant lectins as therapeutic agents against numerous diseases in an ageing society. It is even expected that lectins may occupy an important place in the biopharmaceutical industry next to monoclonal antibodies. All these new trends are placing a tremendous emphasis on the development of new approaches for faster lectins development, selection, and optimization, including alternatives methods of purification. This article reviews the isolation and purification methods used for lectins purification. Origins and applications of lectins are described, highlighting the special features of this class of proteins, such as the carbohydrated-binding domains and their importance in the development of affinity methodologies to increase and facilitate lectins purification. Published strategies for the purification of lectins from different sources are analyzed in relation to the purification methods used, their sequence, and the number of times they are used in a purification procedure. The purity of lectins is analyzed in relation to the average overall yield and purification factors obtained for each purification scheme for these proteins and the purification steps necessary. New directions are described for improving lectins separation and purification.

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“…Lectin solubility and stability vary with the sequence of amino acids in the polypeptide chain, and such structural features can be exploited to provide concentrated lectin preparations. Lectins can be precipitated from extracts by adding ammonium sulfate at high concentration (salting out method) or organic solvents (Santana et al, 2008;Napoleão et al, 2011). Heat-stable lectins can be partially purified by submitting the extract to high temperature for removal of other proteins (Santana et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

“…Lectins can be precipitated from extracts by adding ammonium sulfate at high concentration (salting out method) or organic solvents (Santana et al, 2008;Napoleão et al, 2011). Heat-stable lectins can be partially purified by submitting the extract to high temperature for removal of other proteins (Santana et al, 2008). Lectins are purified by ion exchange, molecular exclusion and/or affinity chromatography that rely on characteristics like charge, size and biological affinity of lectin for solid phases, respectively.…”

Section: Introductionmentioning

confidence: 99%