Physicochemical characterization of changes in pea protein as the result of cold extrusion

Helmick, Harrison; Tonner, Troy; Hauersperger, Daniel; Ettestad, Sarah; Hartanto, Christabel; Okos, Martin R.; Liceaga, Andrea M.; Bhunia, Arun K.; Kokini, Jozef L.

doi:10.1016/j.foodchem.2023.136240

Cited by 13 publications

(5 citation statements)

References 40 publications

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“…The positive control was nondenatured Scy p 9, and the negative control was bovine serum albumin (BSA). The surface hydrophobicity was performed using the 8-anilino-1-naphthalenesulfonic acid as the fluorescence probe …”

Section: Methodsmentioning

confidence: 99%

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Immunoglobulin E Epitope Mapping and Structure–Allergenicity Relationship Analysis of Crab Allergen Scy p 9

He,

Yang,

Chen

et al. 2023

J. Agric. Food Chem.

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Filamin C is an allergen of Scylla paramamosain (Scy p 9), and six IgE linear epitopes of the allergenic predominant region had previously been validated. However, the IgE epitope and structure–allergenicity relationship of Scy p 9 are unclear. In this study, a hydrophobic bond was found to be an important factor of conformation maintaining. The critical amino acids in the six predicted conformational epitopes were mutated, and the IgE-binding capacity and surface hydrophobicity of four mutants (E216A, T270A, Y699A, and V704A) were reduced compared to Scy p 9. Ten linear epitopes were verified with synthetic peptides, among which L-AA187–205 had the strongest IgE-binding capacity. In addition, IgE epitopes were mapped in the protruding surface of the tertiary structure, which were conducive to binding with IgE and exhibited high conservation among filamin genes. Overall, these data provided a basis for IgE epitope mapping and structure–allergenicity relationship of Scy p 9.

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Section: Methodsmentioning

confidence: 99%

“…Circular dichroism (CD) spectroscopy was used to measure the secondary structures of mutants using the procedures previously published by Yang et al The surface hydrophobicity was based on a previous description …”

Section: Methodsmentioning

confidence: 99%

Immunoglobulin E Epitope Mapping and Structure–Allergenicity Relationship Analysis of Crab Allergen Scy p 9

He,

Yang,

Chen

et al. 2023

J. Agric. Food Chem.

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“…37 The transition from an ordered to a disordered protein structure in DDGS under high temperature and shear stress may be responsible for the increase in the ⊎-sheet. 38,39 The FTIR results revealed a noteworthy alteration in the secondary structure of DDGS proteins during extrusion. There was a notable correlation between the spectral composition of the secondary structure and the associated physical properties.…”

Section: X-ray Diffractionmentioning

confidence: 99%

Extrusion puffing as a pretreatment method to change the surface structure, physicochemical properties and in vitro protein digestibility of distillers dried grains with solubles

Liu,

Xie,

Deng

et al. 2023

J Sci Food Agric

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BACKGROUNDDistillers dried grains with solubles (DDGS) are rich in nutrition, and they are potential protein feed raw material. However, the existence of cellulose, hemicellulose and lignin hinders animals' digestion and absorption of DDGS. Making full use of unconventional feed resources such as DDGS can alleviate the shortage of feed resources to a certain extent. This research investigated the effects of twin‐screw extrusion on the macromolecular composition, physical and chemical properties, surface structure and in vitro protein digestibility (IVPD) of DDGS.RESULTSThe findings showed that extrusion puffing significantly increased the protein solubility, bulk density, water holding capacity, and swelling capacity, while significantly decreased hemicellulose and crude protein content, particle size and zeta potential of DDGS. The structure damage of DDGS induced by the extrusion was characterized by scanning electron microscopy (SEM), Fourier‐transform infrared (FITR) spectroscopy and X‐ray diffraction (XRD) analysis. Interestingly, no random coil was observed in the analysis of the secondary structure, and extrusion promoted the transformation of α‐helix and β‐turn to β‐sheet, which led to significant increases in protein solubility and IVPD of DDGS (P < 0.05). Additionally, correlation analysis revealed that IVPD and PS had a positive relationship.CONCLUSIONExtrusion puffing was an ideal pretreatment method for DDGS modification to improve in vitro protein digestibility. © 2023 Society of Chemical Industry.

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“…Surface hydrophobicity (S o ) of Bambara proteins was determined on a Cary Eclipse fluorescence spectrophotometer (Agilent Technologies, Santa Clara, CA, USA) using a hydrophobic probe, 8-anilino-1naphthalene sulfonic acid (ANS), as described by Helmick et al (2023). Briefly, protein stock solution (10 mg mL À1 ) was prepared in 0.1 mol L À1 phosphate buffer (pH 7.0), solubilised for 1 h, and then centrifuged at 10 000 9 g for 15 min.…”

Section: Surface Hydrophobicity (S O )mentioning

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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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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Physicochemical characterization of changes in pea protein as the result of cold extrusion

Cited by 13 publications

References 40 publications

Immunoglobulin E Epitope Mapping and Structure–Allergenicity Relationship Analysis of Crab Allergen Scy p 9

Immunoglobulin E Epitope Mapping and Structure–Allergenicity Relationship Analysis of Crab Allergen Scy p 9

Extrusion puffing as a pretreatment method to change the surface structure, physicochemical properties and in vitro protein digestibility of distillers dried grains with solubles

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

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