Functionalisation of pea protein by tryptic hydrolysis – Characterisation of interfacial and functional properties

Klost, Martina; Drusch, Stephan

doi:10.1016/j.foodhyd.2018.03.013

Cited by 81 publications

(41 citation statements)

References 30 publications

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“…However, on day 3, a decrease in ζ-potential of 2 and 8 mV was observed for A and E, respectively. Similar values were founded by Klost & Drusch [48] for O/W emulsions at pH 3. They detected a ζ-potential of 30 mV for pea extracted with an alkaline method.…”

Section: ζ-Potential and Hydrodynamic Diametersupporting

confidence: 89%

Physical Stability and Interfacial Properties of Oil in Water Emulsion Stabilized with Pea Protein and Fish Skin Gelatin

et al. 2020

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This study aimed to investigate the physical stability and interfacial properties of oil-in-water (O/W) emulsions stabilized with fish skin gelatin (FG) and pea protein (PP) at pH 3. Physico-chemical properties, elemental composition and SDS-PAGE of the proteins were determined in the first part of this work. Emulsions were prepared at different ratio FG: PP (100: 0-75: 25-50: 50-25: 75-0: 100) by mechanical stirring followed by ultrasound treatment. Higher physical stability was observed in the presence of FG (ratio 100: 0), where the O/W were stable~50 h. An average hydrodynamic diameter < 1 μm was found for all the emulsions except for the ratio 75: 25, where it was 2.8 μm. The presence of the protein on the O/W interface was explored by confocal laser scanning microscopy whereas the thermal properties of the protein ratios were analyzed by differential scanning calorimetry. The lower denaturation temperature was observed for ratio 50: 50, which was founded at~89°C, whereas the denaturation temperatures for the others O/W emulsions were in the range of 99 and 108°C. A predominant viscous behavior was observed for all the ratios while a slight decrease of the surface tension was observed in the presence of PP. The equal mixing of FG with PP showed an increase in the emulsifying properties of PP forming a more stable emulsion with lower particle size.

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Section: ζ-Potential and Hydrodynamic Diametersupporting

confidence: 89%

Physical Stability and Interfacial Properties of Oil in Water Emulsion Stabilized with Pea Protein and Fish Skin Gelatin

et al. 2020

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“…Pea protein was produced on lab scale as previously described in more detail (Klost & Drusch, 2019). Briefly, dry peas were ground and the flour was dispersed in 0.0375 M NaOH leading to an initial pH value of approximately 8.7 which dropped to just above pH 8 during the extraction time.…”

Section: Methodsmentioning

confidence: 99%

“…When rapeseed oil was added to the samples, the oil was emulsified by the protein during the homogenisation step before fermentation. From a previous study (Klost & Drusch, 2019) we know that a protein content of 1% is sufficient to stabilise 5% rapeseed oil. Samples in the current study contained 10% protein and 4% oil, leading to sufficient bulk protein for network formation.…”

Section: Samplementioning

confidence: 99%

Structure formation and rheological properties of pea protein-based gels

2019

Self Cite

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Nutritional recommendations for the elderly, but also the general public, include incorporation of plant proteins in the diet, an increase in the intake of Ω-3 fatty acids and an increase in intake of dietary fibre. Protein structure and structuring behaviour of plant proteins differ from that of milk proteins. Therefore, the aim of the presented study was to characterise the structuring process and resulting structure of yoghurt-style gels containing 10% pea protein with and without addition of nutritionally recommended ingredients like rapeseed-oil and/or commercial oat fibre. Rheological measurements were combined with microscopy for sample characterisation. Generally, all studied formulations were able to form acid induced gels via fermentation. The acidification led to a two-phase gelation process resulting in thick gels that showed mainly weak rheological behaviour. Supplementation with oil and/or fibre resulted in an increase of the relative concentration of pea protein in the aqueous phase and led to a strong increase in the complex shear modulus |G*| as well as the maximum structuring velocity d|G*|/dt. These effects need to be considered when tailoring yoghurt-style gels with high consumer acceptance.

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“…Figure 1B demonstrates that the 23, 33 and 34 kDa proteins are the main components of Po SMP, followed by 38 and 49 kDa proteins. The 34 kDa band with the highest protein content was conveniently hydrolysed by alcalase and pepsin, which suggested that the band may have a large number of amino acids at the two enzyme cleavage sites or related to the hydrolysis condition [30]. In contrast, proteins at 23 and 38 kDa showed strong resistance to most of the selected enzymes, and only pepsin could hydrolyse under acidic conditions, which may be related to the spatial structure and special functions of the proteins [31].…”

Section: Resultsmentioning

confidence: 99%

In Vitro and In Silico Antioxidant Activity of Novel Peptides Prepared from Paeonia Ostii ‘Feng Dan’ Hydrolysate

Wang

et al. 2019

Antioxidants

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Antioxidant peptides derived from natural products have superior performance and broader application prospects. In this study, five novel antioxidant peptides were prepared from Paeonia ostii (P. ostii) seed meal, moreover the bioactive and the relationship between structure and properties of antioxidant peptides were elucidated by quantum chemical calculations. The free radical-scavenging activities were used as indexes to purify and concentrate the antioxidant peptides through five proteases and separation techniques. FSAP (Phe-Ser-Ala-Pro), PVETVR (Pro-Val-Glu-Thr-Val-Arg), QEPLLR (Gln-Glu-Pro-Leu-Leu-Arg), EAAY (Glu-Ala-Ala-Tyr) and VLRPPLS (Val-Leu-Arg-Pro-Pro-Leu-Ser) were identified by nano liquid chromatography–tandem mass spectrometry (LC-MS/MS). In vitro antioxidant activity test, EAAY exhibited the highest 2, 2’-azino-bis (ABTS) and hydroxyl radical-scavenging activity of 98.5% ± 1.1% and 61.9% ± 1.3%, respectively (p < 0.01), at 0.5 mg/mL. In silico calculations were carried out using the density functional theory (DFT) with the B3LYP/6-31G* basis set. According to natural bond orbital (NBO) analysis, the bioactivity of free-radical scavenging of the peptides was presumed. Moreover, the antioxidant peptides demonstrated no obvious cytotoxicity to L929 fibroblast cells. Therefore, the peptides from P. ostii seed by-products might potentially have excellent uses in functional foods, nutraceuticals and pharmacological products.

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Functionalisation of pea protein by tryptic hydrolysis – Characterisation of interfacial and functional properties

Cited by 81 publications

References 30 publications

Physical Stability and Interfacial Properties of Oil in Water Emulsion Stabilized with Pea Protein and Fish Skin Gelatin

Physical Stability and Interfacial Properties of Oil in Water Emulsion Stabilized with Pea Protein and Fish Skin Gelatin

Structure formation and rheological properties of pea protein-based gels

In Vitro and In Silico Antioxidant Activity of Novel Peptides Prepared from Paeonia Ostii ‘Feng Dan’ Hydrolysate

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