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Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds

Zinc is a crucial micronutrient for maintaining body immune system and metabolism function. However, insufficient intake from diet may lead to zinc deficiency and impair normal body function. In addition, conventional zinc salts supplementation has the disadvantage of low bioavailability since the z...

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Autores principales: Lu, Dan, Peng, Mengyao, Yu, Min, Jiang, Bo, Wu, Hong, Chen, Jingjing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8044297/
https://www.ncbi.nlm.nih.gov/pubmed/33869265
http://dx.doi.org/10.3389/fnut.2021.647782
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author Lu, Dan
Peng, Mengyao
Yu, Min
Jiang, Bo
Wu, Hong
Chen, Jingjing
author_facet Lu, Dan
Peng, Mengyao
Yu, Min
Jiang, Bo
Wu, Hong
Chen, Jingjing
author_sort Lu, Dan
collection PubMed
description Zinc is a crucial micronutrient for maintaining body immune system and metabolism function. However, insufficient intake from diet may lead to zinc deficiency and impair normal body function. In addition, conventional zinc salts supplementation has the disadvantage of low bioavailability since the zinc ions may be easily chelated by dietary fiber or phytate commonly found in diets rich in plants, and form precipitates that cannot be absorbed. Therefore, the objective of the present study is to prepare pumpkin seed derived peptides and to evaluate the effect of structure and surface properties on the zinc binding behavior of the pumpkin seed protein hydrolysate (PSPH), as well as their gastrointestinal stability. Briefly, different PSPHs were prepared using enzymatic hydrolysis method with bromelain, papain, flavourzyme, alcalase, and pepsin. The particle size, zeta potential, surface hydrophobicity, degree of hydrolysis, ATR-FTIR spectra, and zinc binding capacity were determined. The representative samples were chosen to characterize the binding energy and surface morphology of PSPH-Zn. At last, the in vitro gastrointestinal stability of PSPH and PSPH-Zn were evaluated. Our results showed that peptides hydrolyzed by papain had the largest average molecular weight, smallest particle size, highest hydrophobicity, and the greatest zinc binding capacity. Zinc showed better gastrointestinal stability in PSPHs chelates than in its salt. Meanwhile, PSPH-Zn with higher zinc binding capacity showed better stability. The result of this study indicated pumpkin seed hydrolyzed by papain may be used as a potential source for zinc fortification. The findings in this study may provide important implications for developing plant-based zinc chelating peptides.
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spelling pubmed-80442972021-04-15 Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds Lu, Dan Peng, Mengyao Yu, Min Jiang, Bo Wu, Hong Chen, Jingjing Front Nutr Nutrition Zinc is a crucial micronutrient for maintaining body immune system and metabolism function. However, insufficient intake from diet may lead to zinc deficiency and impair normal body function. In addition, conventional zinc salts supplementation has the disadvantage of low bioavailability since the zinc ions may be easily chelated by dietary fiber or phytate commonly found in diets rich in plants, and form precipitates that cannot be absorbed. Therefore, the objective of the present study is to prepare pumpkin seed derived peptides and to evaluate the effect of structure and surface properties on the zinc binding behavior of the pumpkin seed protein hydrolysate (PSPH), as well as their gastrointestinal stability. Briefly, different PSPHs were prepared using enzymatic hydrolysis method with bromelain, papain, flavourzyme, alcalase, and pepsin. The particle size, zeta potential, surface hydrophobicity, degree of hydrolysis, ATR-FTIR spectra, and zinc binding capacity were determined. The representative samples were chosen to characterize the binding energy and surface morphology of PSPH-Zn. At last, the in vitro gastrointestinal stability of PSPH and PSPH-Zn were evaluated. Our results showed that peptides hydrolyzed by papain had the largest average molecular weight, smallest particle size, highest hydrophobicity, and the greatest zinc binding capacity. Zinc showed better gastrointestinal stability in PSPHs chelates than in its salt. Meanwhile, PSPH-Zn with higher zinc binding capacity showed better stability. The result of this study indicated pumpkin seed hydrolyzed by papain may be used as a potential source for zinc fortification. The findings in this study may provide important implications for developing plant-based zinc chelating peptides. Frontiers Media S.A. 2021-03-31 /pmc/articles/PMC8044297/ /pubmed/33869265 http://dx.doi.org/10.3389/fnut.2021.647782 Text en Copyright © 2021 Lu, Peng, Yu, Jiang, Wu and Chen. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Nutrition
Lu, Dan
Peng, Mengyao
Yu, Min
Jiang, Bo
Wu, Hong
Chen, Jingjing
Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds
title Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds
title_full Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds
title_fullStr Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds
title_full_unstemmed Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds
title_short Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds
title_sort effect of enzymatic hydrolysis on the zinc binding capacity and in vitro gastrointestinal stability of peptides derived from pumpkin (cucurbita pepo l.) seeds
topic Nutrition
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8044297/
https://www.ncbi.nlm.nih.gov/pubmed/33869265
http://dx.doi.org/10.3389/fnut.2021.647782
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