History of Plant Lectin Research

Damme, Els J.M. Van

doi:10.1007/978-1-4939-1292-6_1

Cited by 57 publications

(56 citation statements)

References 19 publications

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“…It not was found on the gel electrophoresis SDS-PAGE molecular mass protein Pequi between 30 and 35 kDa that is typical of the structure of lectins (Sharon & Lis, 1995;Devi et al, 2014;Van Damme, 2014). Technically, the protein bands present in the range of 5-25 kDa suggest the presence of inhibitors of serine peptidases type Kunitz, Bowman-Birk and 2S albumin which has been reported in the scientific literature (Carlini & Grossi-de-Sá, 2002;Ruan et al, 2011).…”

Section: Electrophoresis Of Isolated Fractions Of Pequi Seedsmentioning

confidence: 86%

“…Lectins can act as non-nutritional factors with the capacity to combine with sugars and glycoconjugates, inducing erythrocyte agglutination Van Damme, 2014). The consumption of power by lectins, can lead to gross changes of various animal organs and even lead to hyperplasia and hypertrophy of the pancreas and intestine and may lead to various adverse health effects, by decreasing the absorption of nutrients (Seena & Sridhar, 2004;Pompeu et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

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Anti-nutritional factors and digestibility of protein in Cayocar brasiliense seeds

et al. 2017

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The Brazilian Cerrado presents a wide variety of natural products, including the Pequi (Caryocar brasiliense). The important factor that determines the dietary and nutritional ideality of protein is degestitibility. This work aims to evaluate the protein digestibility of Pequi seeds and the presence of anti-nutritional factors. The protein Pequi almonds were extracted, toasted and untoasted. Evaluation digestibility was structurally characterized by SDS-PAGE 15%, which can be used to analyze simulated gastric fluid (SFG) and digestion in intestinal fluid (SFI) in the presence of pepsin and trypsin/chymotrypsin. The extract from Pequi almonds showed inhibitory activity and was not detected hemagglutination. The intensity of the bands according to 2S albumins, after heat treatment, did not decrease in comparison to the condition native, significantly. In the crisp crude extract, which was incubated under SGF and SIF, the intensity of the corresponding bands at 8 and 3 kDa was resistant to SGF and indigestible after 4 hours under SIF. The characterization of Pequi almonds demonstrated that the product of the crude extract has anti-nutritional factors, which were confirmed by evaluating digestibility.Keywords: Caryocar brasiliense; almonds; in vitro digestibility; 2S albumin; peptidase inhibitor; lectins.Practical Application: The study of anti-nutritional factors identification is very important because of its inactivation on food industry and it can also be used to avoid allergy due to them.

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Section: Electrophoresis Of Isolated Fractions Of Pequi Seedsmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Anti-nutritional factors and digestibility of protein in Cayocar brasiliense seeds

et al. 2017

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“…Penekanan pada non-imun, dimaksudkan untuk membedakan lektin dari antibodi-karbohidrat tertentu, seperti kinase, glicosidase, transferase ataupun transporter (Goldstein et al, 1980). Kemampuan lektin untuk mengikat karbohidrat secara spesifik pada permukaan sel (glikokonjugat), memungkinkan protein ini dapat dikembangkan untuk berbagai tujuan, termasuk untuk deteksi dan identifikasi kelompok darah dan mikroorganisme, determinasi karbohidrat dalam suatu larutan, juga untuk pemurnian glikoprotein (Van Damme, 2014). Karena kemampuannya untuk mengikat karbohidrat di permukaan sel secara spesifik tersebut, lektin juga mempunyai banyak peran penting dalam interaksi antara host-patogen, komunikasi sel-sel, mengenali dan mengikat karbohidrat yang kemudian menghasilkan efek fungsional untuk menginduksi apoptosis, berperan sebagai antibiotik, antiinflammatory, anti-HIV serta anti agregasi platelet (Liao et al, 2003;Dinh et al, 2011;Sato et al, 2011;Hamid et al, 2013;Takebe et al, 2013).…”

Section: Pendahuluanunclassified

Penapisan Senyawa Hemagglutinin dari Makroalga Asal Pantai Binuangeun, Banten, Indonesia

Fajarningsih

Yamin

Yunita

et al. 2015

JPBKP

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ABSTRAKSebagai bagian dari penelitian penapisan lektin dari makroalga Indonesia, 17 esktrak protein makroalga yang dikoleksi dari Pantai Binuangeun, Banten telah diuji aktivitas hemagglutinasinya terhadap eritrosit kelinci dan eritrosit manusia golongan A, B, O, masing-masing dengan perlakuan enzim dan native. Ekstraksi dilakukan dengan menggunakan 2 jenis buffer, yaitu Phosphate Buffer Saline (PBS) dan Tris Buffer Saline (TBS) pH 7. Hasil penelitian menunjukkan bahwa pada beberapa sampel, ekstrak yang dihasilkan kedua buffer, menunjukkan aktivitas hemagglutinasi yang berbeda walaupun kadar total protein ekstrak makroalga yang diekstraksi dengan PBS dan TBS tidak berbeda. Sebagian besar ekstrak makroalga yang diuji mampu mengagglutinasi setidaknya satu jenis sel eritrosit yang digunakan. Secara umum, kelompok makroalga hijau memperlihatkan aktivitas hemagglutinasi yang lebih rendah dibandingkan kelompok makroalga merah dan coklat. Meskipun ekstrak Padina australis (makroalga coklat) memberikan hasil hemagglutinasi eritrosit kelinci negatif, namun ekstrak tersebut positif menghemagglutinasi eritrosit golongan darah B dan O. Di antara 8 makroalga hijau yang diuji, hanya dua sampel yang menunjukkan aktivitas hemagglutinasi, yaitu Chaetomorpha crassa dan Halimeda macroloba. Keempat ekstrak makroalga merah yang diuji menunjukkan aktivitas hemagglutinasi yang kuat terhadap eritrosit kelinci. Ekstrak makroalga merah Gracilaria lichenoides dan Gelidiella acerosa aktif terhadap semua jenis eritrosit uji. Sementara itu, hanya ekstrak Laurencia tronoi yang menunjukkan aktivitas hemagglutinasi terhadap eritrosit golongan darah A. KATA KUNCI:makroalga, lektin, hemagglutinasi ABSTRACT As part of lectins screening project from Indonesia's macroalgae, protein extracts from 17 macroalgae species collected from Binuangen Coast, Banten were examined for their hemagglutinating activity using native and enzyme-treated rabbit and human erythrocytes (A,B,O). Extraction of the macroalgae hemagglutinins was conducted using 2 buffers, e.g Phosphat buffer saline (PBS) and Tris buffer saline (TBS) pH

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“…To summarize the advantage of the FAC-FD method over others [36,40,41]: (1) the principle is clear (based on a Langmuir's adsorption law); (2) Even weak interactions such as those between lectins and glycans can be determined; (3) Only a small quantity (<5 pmol) of fluorescently labeled glycans is required; (4) Combined with an HPLC system, high-throughput analysis is easily achievable (a series of Kd's can be obtained once Bt is determined by concentration-dependence analysis); (5) The analysis is highly reproducible due to simple isocratic elution as well as independence from [A]0 according to Equation (2). To our knowledge therefore, FAC-FD is the only method that enables both the quantitative and high-throughput determination of lectin-glycan interactions in terms of Kd.…”

Section: Fac: Basic Principle and Proceduresmentioning

confidence: 99%

“…Thus, both the classification and designation have long been complicated issues in lectin research, both for plant and animal lectins [2,17].…”

mentioning

confidence: 99%

The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography

et al. 2015

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Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms-from humans to microorganisms, including viruses-and while their functions are yet to be fully elucidated, their main underlying actions are thought to mediate cell-cell and cell-glycoconjugate interactions, which play important roles in an extensive range of biological processes. The basic feature of each lectin's function resides in its specific sugar-binding properties. In this regard, it is beneficial for researchers to have access to fundamental information about the detailed oligosaccharide specificities of diverse lectins. In this review, the authors describe a publicly available lectin database named "Lectin frontier DataBase (LfDB)", which undertakes the continuous publication and updating of comprehensive data for lectin-standard oligosaccharide interactions in terms of dissociation constants (Kd's). For Kd determination, an advanced system of frontal affinity chromatography (FAC) is used, with which quantitative datasets of interactions between immobilized lectins and >100 fluorescently labeled standard glycans have been generated. OPEN ACCESS

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History of Plant Lectin Research

Cited by 57 publications

References 19 publications

Anti-nutritional factors and digestibility of protein in Cayocar brasiliense seeds

Anti-nutritional factors and digestibility of protein in Cayocar brasiliense seeds

Penapisan Senyawa Hemagglutinin dari Makroalga Asal Pantai Binuangeun, Banten, Indonesia

The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography

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