The effect of in vitro gastrointestinal conditions on the structure and conformation of oat β-glucan

Korompokis, Konstantinos; Nilsson, Lars; Zielke, Claudia

doi:10.1016/j.foodhyd.2017.11.007

Cited by 22 publications

(11 citation statements)

References 52 publications

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“…However, it is unlikely that the β-glucan can significantly contribute to the viscosity of digesta at the concentrations used in the simulated digestion. Existing evidence shows that the digestive enzymes do not directly affect the β-glucan structure. , Therefore, the differential effect on the proteins could be attributed to difference in the protein profile, which determines protein behavior and interaction with the other biomolecules. Pea protein isolates obtained under the experimental conditions mainly consist of globulins (55–80%) and albumins (18–25%) with negligible amounts of glutelins and prolamins. , Conversely, lentil protein isolates are composed of 11% glutelins and 3% prolamins.…”

Section: Resultsmentioning

confidence: 99%

β-Glucan Interaction with Lentil (Lens culinaris) and Yellow Pea (Pisum sativum) Proteins Suppresses Their In Vitro Digestibility

Boachie

Commandeur

Abioye

et al. 2021

J. Agric. Food Chem.

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In this study, β-glucan interaction with lentil and yellow pea proteins and the effect on in vitro protein digestibility were investigated. Proteins were mixed with β-glucan at mass ratios of 1:0.5, 1:1, and 1:2. The interaction between β-glucan and the proteins was demonstrated by the decrease in transmittance and surface charge and the increase in particle size of the complexes. Bright-field microscopy showed the formation of aggregates between the biopolymers, although increased molecular size was not observed by discontinuous native polyacrylamide gel electrophoresis. Fluorescence microscopy indicated that β-glucan formed aggregates with lentil proteins, while the interaction with yellow pea proteins appeared as distinct phases of protein within the βglucan network. The in vitro protein digestibility of lentil and pea protein decreased by 27.3 and 34.5%, respectively, in the presence of a β-glucan mass ratio of 1:2. The findings confirm the possibility to modulate protein digestibility by changing the physical characteristics of a food matrix.

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Section: Resultsmentioning

confidence: 99%

β-Glucan Interaction with Lentil (Lens culinaris) and Yellow Pea (Pisum sativum) Proteins Suppresses Their In Vitro Digestibility

Boachie

Commandeur

Abioye

et al. 2021

J. Agric. Food Chem.

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“…Purified β-glucan can only be obtained by isolation from the plant matrix using different extraction techniques [14]. Wet extraction procedures can involve different extraction stage pHs like acidic [15,16], neutral [17,18,19] and alkaline [20,21,22,23] or the utilization of different enzymes for consecutive digestion of botanical fractions [24,25]. Despite the different characteristics of the process, alkaline water procedures deliver the highest yield of extracted β-glucan [22,23].…”

Section: Introductionmentioning

confidence: 99%

Proteinaceous Residue Removal from Oat β-Glucan Extracts Obtained by Alkaline Water Extraction

et al. 2019

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Background: Wet methods of 1-3, 1-4 -β-D-glucan isolation from cereals differ mainly in the type of grain fraction used as raw material, the solid-liquid ratio of β-glucan in raw material vs. solvent used, and the type of aqueous solvent modification (alkali, neutral or acidic). All these factors impact the characterization of the residues finally found in extracts. Oat bran is a rich source of globulin fraction which can be transferred into the extracts, especially when a high pH is employed. Methods: A multi-stage (enzymatic and acidic) purification procedure was performed to remove the residues, especially starch and protein, from β-glucan isolates from oat of different molar mass. Pancreatin, thermostable α-amylase, amyloglucosidase, and papain were used for consecutive residue removal. Three levels of low pH = 4.5, 3.5 and 3.0 were also tested for effective protein precipitation. Results: The starch hydrolysis and liquefaction significantly facilitate the proteinaceous matter removal although papain usage showed an intensive unfavorable impact on β-glucan molar mass. Soluble protein content was significantly decreased after pancreatin and α-amylase treatment, while the significant reduction of amine nitrogen was noted after complete starch hydrolysis and a second acidification step. Conclusions: A complex procedure employing different enzymes is needed to successfully reduce the possibly bioactive residues in isolated oat β-glucan fractions.

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“…β-glucan is a linear polysaccharide located in the endosperm and aleurone layer of cereal grains [8,9]. Oat β-glucan is a linear polysaccharide formed by β-(1→3) and β-(1→4) glycosidic linkages connected to glucopyranose units [10,11], with more than 85% of β-glucan chains There is a β-(1→3) glycosidic bond between 2 to 3 β-(1→ 4) glycosidic bonds in the segment, and about 15% of the segments are composed of β-(1→4) glycosidic bonds, and β-(1→3) glycosidic bonds are alternately connected.…”

Section: β-Glucanmentioning

confidence: 99%

Preparation of Grain β-glucan Gel and Characteristics of Its Slow-release

Xu¹,

Wu²,

Zhao³

2020

JFNR

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The β-glucan freeze-thaw gel has been used as a carrier to release curcumin. The freeze-dried gel has the ideal sustained release following 5% β-glucan solution by adding 1% β-glucan quality curcumin, repeated freezing and thawing 8 times. The Peppas equation can significantly describe the release mechanism of curcumin in the β-glucan gel. This study further shows that the release of curcumin in the oat β-glucan gel is the Fick diffusion mechanism and coated barley β-glucan is a non-Fick release. Trying to use β-glucan as a completely natural drug delivery carrier opens up new ideas for the use of β-glucan.

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The effect of in vitro gastrointestinal conditions on the structure and conformation of oat β-glucan

Cited by 22 publications

References 52 publications

β-Glucan Interaction with Lentil (Lens culinaris) and Yellow Pea (Pisum sativum) Proteins Suppresses Their In Vitro Digestibility

β-Glucan Interaction with Lentil (Lens culinaris) and Yellow Pea (Pisum sativum) Proteins Suppresses Their In Vitro Digestibility

Proteinaceous Residue Removal from Oat β-Glucan Extracts Obtained by Alkaline Water Extraction

Preparation of Grain β-glucan Gel and Characteristics of Its Slow-release

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