Interfacial and Emulsifying Properties of Soybean Peptides with Different Degrees of Hydrolysis

Imura, Tomohiro; Nakayama, Mio; Taira, Toshiaki; Sakai, Hideki; Abe, Masahiko; Kitamoto, Daï

doi:10.5650/jos.ess14167

Cited by 15 publications

(9 citation statements)

References 22 publications

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“…Similar to our results, Imura et al 63 obtained the best emulsifying properties with soybean hydrolysates with the lowest DH and the worst properties with the most hydrolyzed proteins, even lower than those of protein isolates. An increased DH of proteins has been associated with low emulsifying capacity by many other researchers.…”

Section: Resultssupporting

confidence: 92%

“…Similar to our results, Imura et al obtained the best emulsifying properties with soybean hydrolysates with the lowest DH and the worst properties with the most hydrolyzed proteins, even lower than those of protein isolates. An increased DH of proteins has been associated with low emulsifying capacity by many other researchers. − Inversely, the stability index of emulsions was reported to be higher in hydrolysates with the greatest DH by Baharuddin et al, which is in agreement with our present data.…”

Section: Resultssupporting

confidence: 92%

“…Hydrolysates obtained by Neutrase showed the best emulsifying activity with EAI of 84.32 ± 1.43 (NH) and 88.04 ± 2.22 m 2 /g (MFNH). In contrast, Alcalase hydrolysis did not significantly improve the EAI of the protein isolates, 55.36 ± 1.77 (AH) and 61.24 ± 1.63 m 2 /g (MFAH), Similar to our results, Imura et al 63 obtained the best emulsifying properties with soybean hydrolysates with the lowest DH and the worst properties with the most hydrolyzed proteins, even lower than those of protein isolates. An increased DH of proteins has been associated with low emulsifying capacity by many other researchers.…”

Section: Scanning Electron Microscopy (Sem)supporting

confidence: 87%

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Combined Neutrase–Alcalase Protein Hydrolysates from Hazelnut Meal, a Potential Functional Food Ingredient

et al. 2022

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Consumers' interest in functional foods has significantly increased in the past few years. Hazelnut meal, the main valuable byproduct of the hazelnut oil industry, is a rich source of proteins and bioactive peptides and thus has great potential to become a valuable functional ingredient. In this study, hazelnut protein hydrolysates obtained by a single or combined hydrolysis by Alcalase and Neutrase were mainly characterized for their physicochemical properties (SDS-PAGE, particle size distribution, Fourier-transform infrared (FTIR) spectroscopy, molecular weight distribution, etc.) and potential antiobesity effect (Free fatty acid (FFA) release inhibition), antioxidant activity (DPPH and ABTS methods), and emulsifying properties. The impact of a microfluidization pretreatment was also investigated. The combination of Alcalase with Neutrase permitted the highest degree of hydrolysis (DH; 15.57 ± 0.0%) of hazelnut protein isolate, which resulted in hydrolysates with the highest amount of low-molecularweight peptides, as indicated by size exclusion chromatography (SEC) and SDS-PAGE. There was a positive correlation between the DH and the inhibition of FFA release by pancreatic lipase (PL), with a significant positive effect of microfluidization when followed by Alcalase hydrolysis. Microfluidization enhanced the emulsifying activity index (EAI) of protein isolates and hydrolysates. Low hydrolysis by Neutrase had the best effect on the EAI (84.32 ± 1.43 (NH) and 88.04 ± 2.22 m 2 /g (MFNH)), while a negative correlation between the emulsifying stability index (ESI) and the DH was observed. Again, the combined Alcalase−Neutrase hydrolysates displayed the highest radical scavenging activities (96.63 ± 1.06% DPPH and 98.31 ± 0.46% ABTS). FTIR results showed that the application of microfluidization caused the unfolding of the protein structure. The individual or combined application of the Alcalase and Neutrase enzymes caused a switch from the β-sheet organization of the proteins to α-helix structures. In conclusion, hazelnut meal may be a good source of bioactive and functional peptides. The control of its enzymatic hydrolysis, together with an appropriate pretreatment such as microfluidization, may be crucial to achieve the best suitable activity.

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Section: Resultssupporting

confidence: 92%

Section: Resultssupporting

confidence: 92%

Section: Scanning Electron Microscopy (Sem)supporting

confidence: 87%

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Combined Neutrase–Alcalase Protein Hydrolysates from Hazelnut Meal, a Potential Functional Food Ingredient

et al. 2022

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“…Amino acids fail to provide the molecular-level characteristics necessary to lower the surface or interfacial tension and stabilize emulsions. However, the covalent coupling of several amino acids in chains or peptides can provide emulsifying characteristics because a driving force resulting from the summation of all interactions, namely, hydrophobic, hydrophilic, electrostatic, aromatic (π–π stacking), hydrogen bonds, and van der Waals forces, appears to start playing a significant role [ 38 ]. The number of amino acids in a peptide ranges from 2 in dipeptides to about 50 for oligopeptides, a limit above which the amino acid chain is considered to be a protein [ 39 ].…”

Section: Molecular Characteristics Of Emulsifying Peptidesmentioning

confidence: 99%

Emerging Emulsifiers: Conceptual Basis for the Identification and Rational Design of Peptides with Surface Activity

Ricardo

Pradilla

Cruz

et al. 2021

IJMS

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Emulsifiers are gradually evolving from synthetic molecules of petrochemical origin to biomolecules mainly due to health and environmental concerns. Peptides represent a type of biomolecules whose molecular structure is composed of a sequence of amino acids that can be easily tailored to have specific properties. However, the lack of knowledge about emulsifier behavior, structure–performance relationships, and the implementation of different design routes have limited the application of these peptides. Some computational and experimental approaches have tried to close this knowledge gap, but restrictions in understanding the fundamental phenomena and the limited property data availability have made the performance prediction for emulsifier peptides an area of intensive research. This study provides the concepts necessary to understand the emulsifying behavior of peptides. Additionally, a straightforward description is given of how the molecular structure and conditions of the system directly impact the peptides’ ability to stabilize emulsion droplets. Moreover, the routes to design and discover novel peptides with interfacial and emulsifying activity are also discussed, along with the strategies to address some of their major pitfalls and challenges. Finally, this contribution reviews methodologies to build and use data sets containing standard properties of emulsifying peptides by looking at successful applications in different fields.

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“…Key words: casein peptide, micelle, surface tension, surface viscosity, high internal phase emulsion, oil gel drolysis degree on interfacial and emulsifying properties of soybean peptides have been previously reported. Soybean peptides with lower hydrolysis degree give higher surface activity and form micelle-like structures above their critical association concentration CAC 24 . Casein is a nutritional protein, and is known to form casein micelles with an average diameter of 130 nm 25 .…”

mentioning

confidence: 99%

High Internal Phase Emulsion Gels Stabilized by Natural Casein peptides

Wakita

Imura²

2018

J. Oleo Sci.

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Interfacial and Emulsifying Properties of Soybean Peptides with Different Degrees of Hydrolysis

Cited by 15 publications

References 22 publications

Combined Neutrase–Alcalase Protein Hydrolysates from Hazelnut Meal, a Potential Functional Food Ingredient

Combined Neutrase–Alcalase Protein Hydrolysates from Hazelnut Meal, a Potential Functional Food Ingredient

Emerging Emulsifiers: Conceptual Basis for the Identification and Rational Design of Peptides with Surface Activity

High Internal Phase Emulsion Gels Stabilized by Natural Casein peptides

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