Effect of extraction pH on amino acids, nutritional, in-vitro protein digestibility, intermolecular interactions, and functional properties of guar germ proteins
Copyright © 2024 Elsevier Ltd. All rights reserved..
The chemical compositions, intermolecular interactions, and functional properties of guar germ proteins (GGP) were investigated at different extraction pH (7 to 11). The protein efficiency ratio, essential amino acid index (46.53), predicted biological value (39.02), nutritional index (42.67), and protein purity (91.69 %) were found to be highest at pH 9. The in-vitro protein digestibility of GGP sample was highest at pH 11. From SDS-PAGE, the band intensity (<10 kDa) became thinner with an increase in extraction pH from 7 to 9 and then thicker. Meanwhile, smallest particle size and weaker ionic and hydrogen bonds were found at pH 11. The β-sheet content was more dominating in GGP samples. Moreover, higher denaturation temperatures of GGP samples indicated that protein molecules had a compact tertiary structure. Furthermore, the GGP extracted at pH 7 showed better functional properties. The principal component analysis suggested that pH 9 was more suitable for isolating GGP.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:444 |
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| Enthalten in: |
Food chemistry - 444(2024) vom: 30. März, Seite 138628 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Kheto, Ankan [VerfasserIn] |
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| Links: |
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| Themen: |
Amino Acids |
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| Anmerkungen: |
Date Completed 11.03.2024 Date Revised 11.03.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.foodchem.2024.138628 |
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| funding: |
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| 520 | |a Copyright © 2024 Elsevier Ltd. All rights reserved. | ||
| 520 | |a The chemical compositions, intermolecular interactions, and functional properties of guar germ proteins (GGP) were investigated at different extraction pH (7 to 11). The protein efficiency ratio, essential amino acid index (46.53), predicted biological value (39.02), nutritional index (42.67), and protein purity (91.69 %) were found to be highest at pH 9. The in-vitro protein digestibility of GGP sample was highest at pH 11. From SDS-PAGE, the band intensity (<10 kDa) became thinner with an increase in extraction pH from 7 to 9 and then thicker. Meanwhile, smallest particle size and weaker ionic and hydrogen bonds were found at pH 11. The β-sheet content was more dominating in GGP samples. Moreover, higher denaturation temperatures of GGP samples indicated that protein molecules had a compact tertiary structure. Furthermore, the GGP extracted at pH 7 showed better functional properties. The principal component analysis suggested that pH 9 was more suitable for isolating GGP | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Amino acids | |
| 650 | 4 | |a Functional properties | |
| 650 | 4 | |a Guar germ proteins | |
| 650 | 4 | |a In-vitro protein digestibility | |
| 650 | 4 | |a Intermolecular interactions | |
| 650 | 4 | |a Nutritional parameters | |
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| 650 | 7 | |a Proteins |2 NLM | |
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| 700 | 1 | |a Gul, Khalid |e verfasserin |4 aut | |
| 700 | 1 | |a Kumar, Lokesh |e verfasserin |4 aut | |
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