Foaming characteristics of oat protein and modification by partial hydrolysis

Brückner-Gühmann, Monika; Heiden-Hecht, Theresia; Sözer, Nesli; Drusch, Stephan

doi:10.1007/s00217-018-3118-0

Cited by 55 publications

(23 citation statements)

References 63 publications

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“…However, Autio et al [62] using trypsin observed that viscosity of β-glucan samples was lowered, which could confirm existing interactions between protein and polysaccharides like β-glucan. The more pronounced action from the papain also may be allocated both to the residual β-glucanasic activity or strong cleavage action towards protein-β-glucan linkages.…”

Section: Discussionmentioning

confidence: 99%

“…Oat globulins showed a limited solubility under acidic conditions. Researchers [62,64] observed the protein particles with hexameric structures at pH 7 whereas at pH 4 the protein structures were smaller than 20 kDa. In other works, the solubility of oat proteins has increased in highly acidic conditions (pH 1–4) [38,40,48,50] but, the present study did not consider pH beneath 3.…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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

et al. 2019

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“…A commercial mixture of peptides, ranging from 10 to 170 kDa, was used as marker (cat# 26616, Thermo Scientific). SEC was carried out on HPLC ÄKTAbasic TM 10 (Amersham Biosciences, Sweden), according to Brückner-Gühmann et al (2018). The analysis was performed using phosphate buffer at pH 7.…”

Section: Chickpea Protein Extraction and Characterizationmentioning

confidence: 99%

Functional properties of chickpea protein-pectin interfacial complex in buriti oil emulsions and spray dried microcapsules

et al. 2020

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The aim of the present study was to investigate the impact of chickpea protein (CP) alone or in the form of sequentially adsorbed chickpea protein and high methoxylated pectin (CP-HMP) on the microencapsulation of buriti oil by spray drying. CP was extracted and characterized by its molecular weight distribution, zeta potential and solubility. The adsorption of CP and CP-HMP complexes to the oil/water (O/W) interface was investigated by measurement of the interfacial tension. The intractions between the molecules at the O/W interface were analyzed by interfacial shear rheology. Emulsions containing CP or CP-HMP were prepared at pH 3.5, homogenized and spray dried at 180/70 ºC and 210/90 ºC (inlet/outlet) temperature. The oil droplet size distribution (ODS) of emulsions before and after spray drying, the encapsulation efficiency (EE) of microcapsules and their oxidative stability were evaluated. The interfacial tension of CP at the O/W interface was not affected by pectin addition. However, interfacial shear rheology revealed strong interactions between CP-HMP complexes, maintaining the physical integrity of emulsion oil droplets during spray drying. On the other hand, interactions in the CP film were weaker and the droplets were affected by spray drying, suffering from an increase in size. The EE of CP-HMP microcapsules was higher than for CP microcapsules, which suggests a synergistic effect. The spray drying temperature had no effect on the EE. During six months of storage, a slight increase of the conjugated dienes content was observed for all microcapsules. However, the type of microcapsule and the temperature of spray drying had no effect on the development of lipid oxidation.

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“…Furthermore, Brückner‐Gühmann et al. (2018) evaluated the foamability of OPI hydrolyzed with trypsin, and showed that stable and fast forming foams can be prepared from hydrolyzed OPI at pH 4 and 7. Brückner‐Gühmann et al.…”

Section: Techno‐functional Properties Of Oat Proteins and Their Application In Food Industrymentioning

confidence: 99%

Oat protein as a novel protein ingredient: Structure, functionality, and factors impacting utilization

Mel

Malalgoda

2021

Cereal Chem

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Background and Objectives This review outlines the current state of oat usage and potential use as a protein ingredient, oat protein extraction techniques, oat protein structure and functionality, and the effect of genotype and environment (G × E) factors on oat protein quality. Findings Oat protein shows structural similarities to soy glycinin and has the potential to be used as a novel functional ingredient in food processing. Additionally, the globulin protein, which accounts for about 70%–80% of oat protein content, exhibits high heat stability than most plant proteins. The protein content of oat is strongly dependent on G × E, as well as agricultural practices, such as fertilizer use, thus, the importance of investigating these factors for increasing oat protein utilization in the food industry. Conclusions The versatility of oat protein as a food ingredient is yet to be discovered, and current research addresses some of aspects of oat protein utilization, although more research is needed to determine G × E impacts on oat protein structure and functionality. Significance and Novelty This review provides novel insights into how oat protein can be used as a functional protein ingredient in food applications and how structural properties and functionality could be influenced by G × E factors.

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Foaming characteristics of oat protein and modification by partial hydrolysis

Cited by 55 publications

References 63 publications

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

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

Functional properties of chickpea protein-pectin interfacial complex in buriti oil emulsions and spray dried microcapsules

Oat protein as a novel protein ingredient: Structure, functionality, and factors impacting utilization

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