Effects of lysine on the physiochemical properties of plant-protein high-moisture extrudates

Dai, Hui-Hui; An, Hong‐Zhou; Ma, Yuxiang; Guo, Yuexin; Du, Youwei; Zhu, Xue-Qing; Luo, Qiong

doi:10.1016/j.lwt.2022.114410

Cited by 10 publications

(4 citation statements)

References 47 publications

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“…As expected, Bambara globulin and fractions were good sources of lysine (9.2%) but low in methionine. Lysine has been reported to affect the aggregation of proteins by aiding the formation of hydrogen bonds and hydrophobic interactions, which might enhance the gel‐forming property of proteins (Dai et al ., 2023).…”

Section: Resultsmentioning

confidence: 99%

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Gel‐forming properties of Bambara groundnut globulin and protein subfractions: structural and rheological characterisation

Alabi,

Amonsou

2024

Int J of Food Sci Tech

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SummaryThe gel‐forming ability of the pulse proteins influences the formation of food products with desirable texture, structure, and stability. In this study, Bambara globulin was fractionated into legumin and vicilin for structural and physicochemical analyses, and heat‐induced gel rheological characterisation. Bambara globulin showed major vicilin (7S, Mw: 120 kDa) and minor legumin (11S, Mw: 410 kDa) components by size exclusion chromatography and gel electrophoresis analyses. Legumin had the lowest amount of all the charged amino acids. One basic subunit (22 kDa) was identified in the legumin fraction with predominant helical structures. The sol–gel transition temperatures increased in the order of globulin (40 °C) < legumin (50 °C) < vicilin (80 °C). The G′ and G″ of globulin showed relatively low dependency on heating time beyond the gel point compared to legumin and vicilin subfractions, suggesting a more rapid establishment of its gel network during gelation. Vicilin gel consisted of a microporous structure with a small lath sheet‐like structure compared to others. Bambara vicilin could be a prospective ingredient in the development of new products with defined textural characteristics.

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Section: Resultsmentioning

confidence: 99%

“…The highest G′ indicated more rigidity or firmness of the vicilin gel compared to globulin and legumin. Lysine had been reported to impact the aggregation of proteins by aiding the formation of hydrogen bonds and hydrophobic interactions, which thus enhance the gel‐forming ability of protein and its elasticity (Dai et al ., 2023).…”

Section: Resultsmentioning

confidence: 99%

Gel‐forming properties of Bambara groundnut globulin and protein subfractions: structural and rheological characterisation

Alabi,

Amonsou

2024

Int J of Food Sci Tech

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“…Moreover, Lys could help to form fibrous structure in the during the high moisture extrusion protein process. Hence, the high Lys content of LSP indicated that LSP was also an option for processing high moisture extruded protein products 34 . In addition, a high arginine/lysine (Arg/Lys) ratio had a positive effect on the prevention of cardiovascular disease 35 .…”

Section: Resultsmentioning

confidence: 99%

“…Hence, the high Lys content of LSP indicated that LSP was also an option for processing high moisture extruded protein products. 34 In addition, a high arginine/lysine (Arg/Lys) ratio had a positive effect on the prevention of cardiovascular disease. 35 Mung bean protein contributed to lowering blood lipids and promoting cardiovascular health as a result of the high Arg/Lys ratio (1.02).…”

Section: Colormentioning

confidence: 99%

Structure, functional and physicochemical properties of lotus seed protein under different pH environments

Zhong,

Li,

Sun

et al. 2024

J Sci Food Agric

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BACKGROUDThis study investigated the structure, functional and physicochemical properties of lotus seed protein (LSP) under different pH environments. The structures of LSP were characterized by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE), fourier transform infrared spectroscopy (FTIR), zeta potential, particle size distributions, free sulfhydryl and rheological property. The functional and physicochemical properties of LSP were characterized by color, foaming property, emulsification property, solubility, oil holding capacity (OHC), water holding capacity (WHC), differential scanning calorimetry analysis (DSC) and surface hydrophobicity.ResultsLSP was mainly composed of 8 subunits (18 kDa, 25 kDa, 31 kDa, 47 kDa, 51 kDa, 56 kDa, 65 kDa and 151 kDa), in which the richest band was 25 kDa. FTIR results showed that LSP had high total contents of α‐helix and β‐sheet (44.81%–46.85%) in acidic environments. Meanwhile, there were more β‐structure and random structure in neutral and alkaline environments (pH 7.0 and 9.0). At pH 5.0, LSP had large particle size (1576.98 nm), high emulsion stability index (91.43 min), foaming stability (75.69%), water holding capacity (2.21 g g−1), but low solubility (35.98%), free sulfhydryl content (1.95 μmol g−1) and surface hydrophobicity (780). DSC analysis showed the denaturation temperatures (82.23°C) of LSP at pH 5.0 was higher than those (80.10°C, 80.52°C, 71.82°C) at pH 3.0, 7.0, 9.0. The analysis of rheological properties showed that LSP gel had high stability and great strength in alkaline environment.ConclusionThe findings were anticipated to serve as a valuable reference for the implementation of LSP in the food industry.This article is protected by copyright. All rights reserved.

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Advancing molecular understanding in high moisture extrusion for plant-based meat analogs: Challenges and perspectives

Zhang,

Shen,

Zhang

et al. 2024

Food Chemistry

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Effects of lysine on the physiochemical properties of plant-protein high-moisture extrudates

Cited by 10 publications

References 47 publications

Gel‐forming properties of Bambara groundnut globulin and protein subfractions: structural and rheological characterisation

Gel‐forming properties of Bambara groundnut globulin and protein subfractions: structural and rheological characterisation

Structure, functional and physicochemical properties of lotus seed protein under different pH environments

Advancing molecular understanding in high moisture extrusion for plant-based meat analogs: Challenges and perspectives

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