Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes
Proteins and peptides when forming complexes with zinc can increase zinc bioavailability. Such complexation was investigated on hemp protein hydrolysates (HPHs) in the present study using Pepsin, Alcalase, Flavourzyme, Papain, Protamex, and Trypsin. Two solubility fractions of Zn2+–HPH complexes, i....
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Elsevier
2018-10-01
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| Series: | Journal of Functional Foods |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S1756464618304419 |
| _version_ | 1830187372449366016 |
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| author | Qingling Wang Youling L. Xiong |
| author_facet | Qingling Wang Youling L. Xiong |
| author_sort | Qingling Wang |
| collection | DOAJ |
| description | Proteins and peptides when forming complexes with zinc can increase zinc bioavailability. Such complexation was investigated on hemp protein hydrolysates (HPHs) in the present study using Pepsin, Alcalase, Flavourzyme, Papain, Protamex, and Trypsin. Two solubility fractions of Zn2+–HPH complexes, i.e., P1 (water-insoluble large peptides) and P2 (water-soluble small peptides, precipitable by ethanol), were collected. The FTIR analysis on Pepsin-HPH suggested that P1 and P2 peptides had different Zn2+-binding sites where NH and CO were the primary sites in P1 and P2, respectively. Although the Zn2+-binding capacity (P1 and P2 combined) of HPHs was lower than that of nonhydrolyzed hemp protein, the P2-bound Zn2+ was more abundant in HPHs (up to 63.4%) than in nonhydrlyzed protein (29.6%). Isothermal titration calorimetry corroborated with Zn2+-binding capacity for different HPH samples. Peptides produced with Flavourzyme had the highest Zn2+-binding activity (88.8%) while those with Pepsin exhibited the maximum solubility. |
| first_indexed | 2024-12-17T22:27:28Z |
| format | Article |
| id | doaj.art-5a59ebe382ed441985672bea8fedbbfa |
| institution | Directory Open Access Journal |
| issn | 1756-4646 |
| language | English |
| last_indexed | 2024-12-17T22:27:28Z |
| publishDate | 2018-10-01 |
| publisher | Elsevier |
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| series | Journal of Functional Foods |
| spelling | doaj.art-5a59ebe382ed441985672bea8fedbbfa2022-12-21T21:30:19ZengElsevierJournal of Functional Foods1756-46462018-10-0149105112Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexesQingling Wang0Youling L. Xiong1State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, ChinaState Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, United States; Corresponding author.Proteins and peptides when forming complexes with zinc can increase zinc bioavailability. Such complexation was investigated on hemp protein hydrolysates (HPHs) in the present study using Pepsin, Alcalase, Flavourzyme, Papain, Protamex, and Trypsin. Two solubility fractions of Zn2+–HPH complexes, i.e., P1 (water-insoluble large peptides) and P2 (water-soluble small peptides, precipitable by ethanol), were collected. The FTIR analysis on Pepsin-HPH suggested that P1 and P2 peptides had different Zn2+-binding sites where NH and CO were the primary sites in P1 and P2, respectively. Although the Zn2+-binding capacity (P1 and P2 combined) of HPHs was lower than that of nonhydrolyzed hemp protein, the P2-bound Zn2+ was more abundant in HPHs (up to 63.4%) than in nonhydrlyzed protein (29.6%). Isothermal titration calorimetry corroborated with Zn2+-binding capacity for different HPH samples. Peptides produced with Flavourzyme had the highest Zn2+-binding activity (88.8%) while those with Pepsin exhibited the maximum solubility.http://www.sciencedirect.com/science/article/pii/S1756464618304419Hemp protein hydrolysatePeptidesZn2+-bindingBioavailabilityIsothermal titration |
| spellingShingle | Qingling Wang Youling L. Xiong Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes Journal of Functional Foods Hemp protein hydrolysate Peptides Zn2+-binding Bioavailability Isothermal titration |
| title | Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes |
| title_full | Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes |
| title_fullStr | Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes |
| title_full_unstemmed | Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes |
| title_short | Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes |
| title_sort | zinc binding behavior of hemp protein hydrolysates soluble versus insoluble zinc peptide complexes |
| topic | Hemp protein hydrolysate Peptides Zn2+-binding Bioavailability Isothermal titration |
| url | http://www.sciencedirect.com/science/article/pii/S1756464618304419 |
| work_keys_str_mv | AT qinglingwang zincbindingbehaviorofhempproteinhydrolysatessolubleversusinsolublezincpeptidecomplexes AT youlinglxiong zincbindingbehaviorofhempproteinhydrolysatessolubleversusinsolublezincpeptidecomplexes |