Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes

Qingling Wang; Youling L. Xiong

doi:10.1016/j.jff.2018.08.019

Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes

Qingling Wang
, Youling L. Xiong

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

46 Scopus citations

Abstract

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 N–H and C[dbnd]O 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.

Original language	English
Pages (from-to)	105-112
Number of pages	8
Journal	Journal of Functional Foods
Volume	49
DOIs	https://doi.org/10.1016/j.jff.2018.08.019
State	Published - Oct 2018

Bibliographical note

Publisher Copyright:
© 2018 Elsevier Ltd

Funding

This study was supported by the USDA National Institute of Food and Agriculture (Hatch project 2351267000) and an Oversea Study Fellowship from the China Scholarship Council (to Q. W.). We thank Dr. Akinbode Adedeji from the Department of Biosystems and Agricultural Engineering at the University of Kentucky for providing the FTIR support. Approved for publication as journal article number 18-07-035 by the Director of the Kentucky Agricultural Experiment Station.

Funders	Funder number
US Department of Agriculture National Institute of Food and Agriculture, Agriculture and Food Research Initiative	2351267000
China Scholarship Council

Keywords

Acrylamide (PubChem CID: 6579)
Bioavailability
Ethanol (PubChem CID: 702)
Hemp protein hydrolysate
Isothermal titration
Peptides
Silver nitrate (PubChem CID: 24470)
Sodium dodecyl sulfate (PubChem CID: 3423265)
Zinc sulfate (PubChem CID: 24424)
Zn-binding

ASJC Scopus subject areas

Food Science
Medicine (miscellaneous)
Nutrition and Dietetics

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10.1016/j.jff.2018.08.019

Cite this

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title = "Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes",

abstract = "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 N–H and C[dbnd]O 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.",

keywords = "Acrylamide (PubChem CID: 6579), Bioavailability, Ethanol (PubChem CID: 702), Hemp protein hydrolysate, Isothermal titration, Peptides, Silver nitrate (PubChem CID: 24470), Sodium dodecyl sulfate (PubChem CID: 3423265), Zinc sulfate (PubChem CID: 24424), Zn-binding",

author = "Qingling Wang and Xiong, \{Youling L.\}",

note = "Publisher Copyright: {\textcopyright} 2018 Elsevier Ltd",

year = "2018",

month = oct,

doi = "10.1016/j.jff.2018.08.019",

language = "English",

volume = "49",

pages = "105--112",

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T1 - Zinc-binding behavior of hemp protein hydrolysates

T2 - Soluble versus insoluble zinc-peptide complexes

AU - Wang, Qingling

AU - Xiong, Youling L.

PY - 2018/10

Y1 - 2018/10

N2 - 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 N–H and C[dbnd]O 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.

AB - 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 N–H and C[dbnd]O 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.

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KW - Ethanol (PubChem CID: 702)

KW - Hemp protein hydrolysate

KW - Isothermal titration

KW - Peptides

KW - Silver nitrate (PubChem CID: 24470)

KW - Sodium dodecyl sulfate (PubChem CID: 3423265)

KW - Zinc sulfate (PubChem CID: 24424)

KW - Zn-binding

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DO - 10.1016/j.jff.2018.08.019

M3 - Article

AN - SCOPUS:85051682024

SN - 1756-4646

VL - 49

SP - 105

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JO - Journal of Functional Foods

JF - Journal of Functional Foods

ER -

Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

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