Alcalase-hydrolyzed insoluble soybean meal hydrolysate aggregates : Structure, bioactivity, function properties, and influences on the stability of oil-in-water emulsions
Copyright © 2024. Published by Elsevier B.V..
We studied the influences of hydrolysis time on the structure, functional properties, and emulsion stability of insoluble soybean meal hydrolysate aggregates (ISMHAs). We assume that the ISMHAs produced by soybean meal can be used as emulsifiers to prepare stable emulsions. The molecular weights of these ISMHAs were below 53 kDa. After hydrolysis, a decrease in α-helices and an increase in random coils indicated that the soybean meal proteins were unfolding. Moreover, the fluorescence intensity, UV absorption, and surface hydrophobicity of ISMHAs increased. These results would contribute to their antioxidant activity and functional properties. Additionally, the 90-min ISMHA sample exhibited the highest ABTS+• scavenging activity (80.02 ± 4.55 %), foaming stability (52.92 ± 8.06 %), and emulsifying properties (emulsifying activity index of 97.09 m2/g; emulsifying stability index of 371.47 min). The 90-min ISMHA emulsion exhibited the smallest particle size and excellent storage stability. Soybean meal peptide by-product emulsifier has potential for sustainable application.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2024 |
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Erschienen: |
2024 |
Enthalten in: |
Zur Gesamtaufnahme - volume:265 |
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Enthalten in: |
International journal of biological macromolecules - 265(2024), Pt 2 vom: 21. Apr., Seite 131014 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Zhang, Xiaoying [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 18.04.2024 Date Revised 18.04.2024 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.ijbiomac.2024.131014 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM370108752 |
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500 | |a Citation Status MEDLINE | ||
520 | |a Copyright © 2024. Published by Elsevier B.V. | ||
520 | |a We studied the influences of hydrolysis time on the structure, functional properties, and emulsion stability of insoluble soybean meal hydrolysate aggregates (ISMHAs). We assume that the ISMHAs produced by soybean meal can be used as emulsifiers to prepare stable emulsions. The molecular weights of these ISMHAs were below 53 kDa. After hydrolysis, a decrease in α-helices and an increase in random coils indicated that the soybean meal proteins were unfolding. Moreover, the fluorescence intensity, UV absorption, and surface hydrophobicity of ISMHAs increased. These results would contribute to their antioxidant activity and functional properties. Additionally, the 90-min ISMHA sample exhibited the highest ABTS+• scavenging activity (80.02 ± 4.55 %), foaming stability (52.92 ± 8.06 %), and emulsifying properties (emulsifying activity index of 97.09 m2/g; emulsifying stability index of 371.47 min). The 90-min ISMHA emulsion exhibited the smallest particle size and excellent storage stability. Soybean meal peptide by-product emulsifier has potential for sustainable application | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Alkaline protease | |
650 | 4 | |a Antioxidant activity | |
650 | 4 | |a Emulsion stability | |
650 | 4 | |a Functional properties | |
650 | 4 | |a Insoluble soybean meal hydrolysate aggregates | |
650 | 4 | |a Structural properties | |
650 | 7 | |a Emulsions |2 NLM | |
650 | 7 | |a Subtilisins |2 NLM | |
650 | 7 | |a EC 3.4.21.- |2 NLM | |
650 | 7 | |a Emulsifying Agents |2 NLM | |
650 | 7 | |a Soybean Proteins |2 NLM | |
650 | 7 | |a Water |2 NLM | |
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700 | 1 | |a Hao, Jiaqi |e verfasserin |4 aut | |
700 | 1 | |a Ma, Danhua |e verfasserin |4 aut | |
700 | 1 | |a Li, Ziyu |e verfasserin |4 aut | |
700 | 1 | |a Zhang, Shuang |e verfasserin |4 aut | |
700 | 1 | |a Li, Yang |e verfasserin |4 aut | |
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