Heat-induced changes in microstructure of spray-dried plant protein isolates and its implications on in vitro gastric digestion

Rio, Andrea Rivera del; Opazo-Navarrete, Mauricio; Cepero-Betancourt, Yamira; Tabilo‐Munizaga, Gipsy; Boom, R.M.; Janssen, A.E.M.

doi:10.1016/j.lwt.2019.108795

Cited by 24 publications

(24 citation statements)

References 18 publications

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“…These results may have been due to the fact that the high‐temperature conditions had induced the unfolding of the protein molecules to a certain extent, which caused the initial hydrophobic groups inside the molecules to be exposed to the polar surrounding environment, thereby exposing more hydrophobic groups (Jiang et al ., 2014). Some of the previous study results have shown that many hydrophobic groups will be exposed after the thermal processing of proteins (Rivera del Rio et al ., 2020; Sun et al ., 2020).…”

Section: Resultsmentioning

confidence: 99%

“…The immunological method of indirect competitive ELISA was utilised in this study to detect the antigenicity of the soy globulin after processing (Segura-Gil et al, 2018;Segura-Gil et al, 2020). The soy glycinin was diluted to 2.5 µg mL −1 with CBS, 100 µL per well were used to coat 96-well microtiter plates.…”

Section: Antigenicity Determination (Elisa)mentioning

confidence: 99%

“…They are also rich in unsaturated fatty acids, vitamins, minerals and other nutrients. Therefore, due to the high nutritional value, high-protein content and good functional properties of soybean, it is widely used in the food industry (Segura-Gil et al, 2020). However, soybean is also classified as one of the fourteen major food allergens recognised by the FAO (Zhang et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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The effects of ultra‐high‐pressure treatments combined with heat treatments on the antigenicity and structure of soy glycinin

2021

Int J of Food Sci Tech

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Glycinin is one of the important allergens found in soybeans, which can potentially cause severe allergic reactions. Therefore, reducing the antigenicity of glycinin is of major significance to the research of soybean allergies. In order to detect the relationships between the antigenicity and structure of glycinin, samples were extracted from defatted soybean and then processed by ultra-high-pressure combined heat treatments. The processed proteins were determined using SDS-PAGE, enzyme-linked immunosorbent assay (ELISA), immunoblotting, exogenous fluorescence, free sulfhydryl groups and Fourier transform methods. The results revealed that the antigenicity of the processed soy glycinin had decreased. In addition, the content levels of the hydrophobic groups, free sulfhydryl groups, α-helix, β-turn and random coils had increased, and the content of β-sheets had decreased. The results indicated that the reduction in the antigenicity of the glycinin was due to the processing treatments, which effectively destroyed the spatial structure of the glycinin.

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Section: Resultsmentioning

confidence: 99%

Section: Antigenicity Determination (Elisa)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The effects of ultra‐high‐pressure treatments combined with heat treatments on the antigenicity and structure of soy glycinin

2021

Int J of Food Sci Tech

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“…Commercial soybean and pea PI dispersions heated at 90 and 120 °C for 30 min did not show different DH during in vitro gastric digestion compared to their unheated counterparts. Upon close inspection of the soluble and sedimented tailings, we found that heating improved the solubility of the commercial PI, and that the proteins separated into this fraction could be more extensively hydrolysed than those in the sedimented fractions [ 70 ].…”

Section: Post-fractionation Processingmentioning

confidence: 99%

“…The following supporting information can be downloaded at: , Table S1: Summary of digestion assays, sample treatment and measurement from studies investigating the effect of processing on protein digestion. References [ 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 ,…”

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confidence: 99%

Effect of Fractionation and Processing Conditions on the Digestibility of Plant Proteins as Food Ingredients

Rio

Boom

Janssen

2022

Foods

Self Cite

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Plant protein concentrates and isolates are used to produce alternatives to meat, dairy and eggs. Fractionation of ingredients and subsequent processing into food products modify the techno-functional and nutritional properties of proteins. The differences in composition and structure of plant proteins, in addition to the wide range of processing steps and conditions, can have ambivalent effects on protein digestibility. The objective of this review is to assess the current knowledge on the effect of processing of plant protein-rich ingredients on their digestibility. We obtained data on various fractionation conditions and processing after fractionation, including enzymatic hydrolysis, alkaline treatment, heating, high pressure, fermentation, complexation, extrusion, gelation, as well as oxidation and interactions with starch or fibre. We provide an overview of the effect of some processing steps for protein-rich ingredients from different crops, such as soybean, yellow pea, and lentil, among others. Some studies explored the effect of processing on the presence of antinutritional factors. A certain degree, and type, of processing can improve protein digestibility, while more extensive processing can be detrimental. We argue that processing, protein bioavailability and the digestibility of plant-based foods must be addressed in combination to truly improve the sustainability of the current food system.

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Novel Drying Technologies for Future Animal- and Plant-Derived Protein Foods: Research Progress, Challenges, and Potential Applications

Niu,

Zhang,

Mujumdar

et al. 2024

Food Bioprocess Technol

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Heat-induced changes in microstructure of spray-dried plant protein isolates and its implications on in vitro gastric digestion

Cited by 24 publications

References 18 publications

The effects of ultra‐high‐pressure treatments combined with heat treatments on the antigenicity and structure of soy glycinin

The effects of ultra‐high‐pressure treatments combined with heat treatments on the antigenicity and structure of soy glycinin

Effect of Fractionation and Processing Conditions on the Digestibility of Plant Proteins as Food Ingredients

Novel Drying Technologies for Future Animal- and Plant-Derived Protein Foods: Research Progress, Challenges, and Potential Applications

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