Quantification of lectin in soybeans and soy products by liquid chromatography-tandem mass spectrometry

Yang, Wen; Liu, Anguo; Meng, Chengzhen; Zhen, Li; He, Pingli

doi:10.1016/j.jchromb.2021.122987

Cited by 14 publications

(5 citation statements)

References 26 publications

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“…P34 is known as Gly m Bd 30K and is a major allergenic protein [ 32 ]. Lectin and trypsin inhibitors are known as anti-nutritional factors [ 33 ]. Thus, their extensive degradation in the FSPI curd digestates can substantially improve the nutritional value of soy proteins.…”

Section: Resultsmentioning

confidence: 99%

Assessment of In Vitro Digestive Behavior of Lactic-Acid-Bacteria Fermented Soy Proteins: A Study Comparing Colloidal Solutions and Curds

Wang

Azarpazhooh

et al. 2022

Molecules

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This study investigated the effect of lactic-acid-bacteria fermentation on the microstructure and gastrointestinal digestibility of soy proteins using a digestomics approach. Fermented soy protein isolates (FSPIs) under varied fermentation-terminal pH demonstrated a colloidal solution (FSPI-7.0/6.0) or yogurt-like curd (FSPI-5.0/4.0) state. Cryo-electron microscopy figures demonstrated the loosely stacked layer of FSPI-7.0/6.0 samples, whereas a denser gel network was observed for FSPI-5.0/4.0 samples. Molecular interactions shifted from dominant ionic bonds to hydrophobic forces and disulfide bonds. The gastric/intestinal digestion demonstrated that the curd samples afforded a significantly low particle size and high-soluble protein and peptide contents in the medium and late digestive phases. A peptidomics study showed that the FSPI-6.0 digestate at early intestinal digestion had a high peptidome abundance, whereas FSPI curd digestates (FSPI-5.0/4.0) elicited a postponed but more extensive promotion during medium and late digestion. Glycinin G2/G4 and β-conglycinin α/α’ subunits were the major subunits promoted by FSPI-curds. The spatial structures of glycinin G2 and β-conglycinin α subunits demonstrated variations located in seven regions. Glycinin G2 region 6 (A349–K356) and β-conglycinin α subunit region 7 (E556–E575), which were located at the interior of the 3D structure, were the key regions contributing to discrepancies at the late stage.

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Section: Resultsmentioning

confidence: 99%

Assessment of In Vitro Digestive Behavior of Lactic-Acid-Bacteria Fermented Soy Proteins: A Study Comparing Colloidal Solutions and Curds

Wang

Azarpazhooh

et al. 2022

Molecules

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“…The origin of nitrogen can come from the storage proteins, which are characterized by the two following main components: glycinin and β-conglycinin, which account for over 65% of the total soy protein content [42]. In addition, lectins, a type of carbohydrate-binding protein, contribute about 10% of the total soy protein and serve as an additional source of nitrogen [43]. During the formation of carbon dots, nitrogen from these proteins undergoes degradation, resulting in the creation of nitrogen-containing functional groups through deamination and condensation reactions [44].…”

Section: Structural Analysismentioning

confidence: 99%

Tailoring the Optoelectronic Properties of Soybean-Derived Nitrogen Self-Doped Carbon Dots through Composite Formation with KCl and Zeolite, Synthesized Using Autogenic Atmosphere Pyrolysis

Lagunay,

Akhetova,

O’Reilly

et al. 2024

Crystals

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This article investigates the environmentally friendly synthesis and characterization of carbon dots (CDs) derived from soybean biomass, in conjunction with their composites containing potassium chloride (KCl) or zeolite. By using an environmentally sustainable synthetic approach, this study sought to unlock the potential of these materials for various applications. The physicochemical properties of the CDs and composites were comprehensively analyzed using various techniques including scanning electron microscopy, transmission electron microscopy, X-ray photoelectron spectroscopy, and X-ray diffraction analysis. In addition, various optical properties such as UV–Vis absorption, band gap, and excitation–emission behavior were investigated. A key finding to arise from this study was that the inclusion of a doping agent such as KCl or zeolite significantly reduced the size of the resulting CDs. In this light, whereas the undoped species are associated with average sizes of 8.86 ± 0.10 nm, those doped with either zeolite or KCl were associated with average sizes of 3.09 ± 0.05 and 2.07 ± 0.05 nm, respectively. In addition, it was shown that doping with either zeolite or KCl resulted in an alteration of the elemental composition of the CDs and influenced their optical properties, especially their excitation-dependent emission. These promising results point to potential applications in environmental sensing and energy-related fields.

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“…The classical approach is the erythrocyte agglutination test, which is mainly used for qualitative or semiquantitative detection and has the drawbacks of a complicated operation and poor repeatability. Quantitative methods have also been developed for SBA detection, including liquid chromatography–mass spectrometry [ 13 ], electrochemical biosensors [ 14 , 15 , 16 , 17 ], and ELISAs [ 18 , 19 , 20 , 21 ]. Among these, ELISAs are simple, specific, and low cost, making them a useful tool for detecting soybean proteins in foods [ 22 , 23 ].…”

Section: Introductionmentioning

confidence: 99%

Development of a Phage-Displayed Nanobody-Based Competitive Immunoassay for the Sensitive Detection of Soybean Agglutinin

Zhang,

Qiu,

You

et al. 2024

Foods

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Soybean agglutinin (SBA) is a primary antinutritional factor in soybeans that can inhibit the growth of humans and mammals, disrupt the intestinal environment, and cause pathological changes. Therefore, detecting and monitoring SBA in foods is essential for safeguarding human health. In this paper, M13 phage-displayed nanobodies against SBA were isolated from a naive nanobody library. An M13 phage-displayed nanobody-based competitive enzyme-linked immunosorbent assay (P-cELISA) was then established for SBA analysis using biotinylated anti-M13 phage antibody (biotin-anti-M13) and streptavidin poly-HRP conjugate (SA-poly-HRP). The biotin-anti-M13@SA-poly-HRP probe can easily amplify the detection signal without the chemical modifications of phage-displayed nanobodies. The established P-cELISA presented a linear detection range of 0.56–250.23 ng/mL and a limit of detection (LOD) of 0.20 ng/mL, which was 12.6-fold more sensitive than the traditional phage-ELISA. Moreover, the developed method showed good specificity for SBA and acceptable recoveries (78.21–121.11%) in spiked wheat flour, albumen powder, and whole milk powder. This study proposes that P-cELISA based on biotin-anti-M13@SA-poly-HRP may provide a convenient and effective strategy for the sensitive detection of SBA.

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Quantification of lectin in soybeans and soy products by liquid chromatography-tandem mass spectrometry

Cited by 14 publications

References 26 publications

Assessment of In Vitro Digestive Behavior of Lactic-Acid-Bacteria Fermented Soy Proteins: A Study Comparing Colloidal Solutions and Curds

Assessment of In Vitro Digestive Behavior of Lactic-Acid-Bacteria Fermented Soy Proteins: A Study Comparing Colloidal Solutions and Curds

Tailoring the Optoelectronic Properties of Soybean-Derived Nitrogen Self-Doped Carbon Dots through Composite Formation with KCl and Zeolite, Synthesized Using Autogenic Atmosphere Pyrolysis

Development of a Phage-Displayed Nanobody-Based Competitive Immunoassay for the Sensitive Detection of Soybean Agglutinin

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