Cargando…

Study on the mechanism of soy protein isolate to improve quality of reduced-salt Hypophthalmichthys molitrix surimi gel: Focus on gel quality, protein structure, and in vitro digestibility

Excessive intake of sodium chloride may bring a series of diseases; as a result, reduced-salt surimi gels have gained growing popularity for sodium reduction. This paper studied soy protein isolate (SPI, 2.0%, 4.0%, and 6.0%, w/w) as a gel enhancer for reduced-salt silver carp surimi. Compared with...

Descripción completa

Detalles Bibliográficos
Autores principales: Zhang, Xuehua, Pan, Hao, Jiang, Xin, Shi, Wenzheng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10518566/
https://www.ncbi.nlm.nih.gov/pubmed/37753325
http://dx.doi.org/10.1016/j.fochx.2023.100878
_version_ 1785109542773719040
author Zhang, Xuehua
Pan, Hao
Jiang, Xin
Shi, Wenzheng
author_facet Zhang, Xuehua
Pan, Hao
Jiang, Xin
Shi, Wenzheng
author_sort Zhang, Xuehua
collection PubMed
description Excessive intake of sodium chloride may bring a series of diseases; as a result, reduced-salt surimi gels have gained growing popularity for sodium reduction. This paper studied soy protein isolate (SPI, 2.0%, 4.0%, and 6.0%, w/w) as a gel enhancer for reduced-salt silver carp surimi. Compared with the control (2.0% NaCl), the addition of SPI significantly increased (P < 0.05) the total SH content, hydrophobic interaction force, disulfide bond, hardness, gel strength, and water-holding capacity of the gels. During the thermal denaturation process, SPI and myofibrillar protein jointly participated in the formation of the gel network, resulting in a G′ value increase at 90 °C, forming a denser/more stable gel network structure. In vitro pepsin digestion results showed the digestibility of the reduced-salt gel with SPI was higher than that of the control. Therefore, appropriate SPI addition can improve the gel performance of reduced-salt surimi gel without affecting digestion and absorption.
format Online
Article
Text
id pubmed-10518566
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Elsevier
record_format MEDLINE/PubMed
spelling pubmed-105185662023-09-26 Study on the mechanism of soy protein isolate to improve quality of reduced-salt Hypophthalmichthys molitrix surimi gel: Focus on gel quality, protein structure, and in vitro digestibility Zhang, Xuehua Pan, Hao Jiang, Xin Shi, Wenzheng Food Chem X Article Excessive intake of sodium chloride may bring a series of diseases; as a result, reduced-salt surimi gels have gained growing popularity for sodium reduction. This paper studied soy protein isolate (SPI, 2.0%, 4.0%, and 6.0%, w/w) as a gel enhancer for reduced-salt silver carp surimi. Compared with the control (2.0% NaCl), the addition of SPI significantly increased (P < 0.05) the total SH content, hydrophobic interaction force, disulfide bond, hardness, gel strength, and water-holding capacity of the gels. During the thermal denaturation process, SPI and myofibrillar protein jointly participated in the formation of the gel network, resulting in a G′ value increase at 90 °C, forming a denser/more stable gel network structure. In vitro pepsin digestion results showed the digestibility of the reduced-salt gel with SPI was higher than that of the control. Therefore, appropriate SPI addition can improve the gel performance of reduced-salt surimi gel without affecting digestion and absorption. Elsevier 2023-09-12 /pmc/articles/PMC10518566/ /pubmed/37753325 http://dx.doi.org/10.1016/j.fochx.2023.100878 Text en © 2023 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Zhang, Xuehua
Pan, Hao
Jiang, Xin
Shi, Wenzheng
Study on the mechanism of soy protein isolate to improve quality of reduced-salt Hypophthalmichthys molitrix surimi gel: Focus on gel quality, protein structure, and in vitro digestibility
title Study on the mechanism of soy protein isolate to improve quality of reduced-salt Hypophthalmichthys molitrix surimi gel: Focus on gel quality, protein structure, and in vitro digestibility
title_full Study on the mechanism of soy protein isolate to improve quality of reduced-salt Hypophthalmichthys molitrix surimi gel: Focus on gel quality, protein structure, and in vitro digestibility
title_fullStr Study on the mechanism of soy protein isolate to improve quality of reduced-salt Hypophthalmichthys molitrix surimi gel: Focus on gel quality, protein structure, and in vitro digestibility
title_full_unstemmed Study on the mechanism of soy protein isolate to improve quality of reduced-salt Hypophthalmichthys molitrix surimi gel: Focus on gel quality, protein structure, and in vitro digestibility
title_short Study on the mechanism of soy protein isolate to improve quality of reduced-salt Hypophthalmichthys molitrix surimi gel: Focus on gel quality, protein structure, and in vitro digestibility
title_sort study on the mechanism of soy protein isolate to improve quality of reduced-salt hypophthalmichthys molitrix surimi gel: focus on gel quality, protein structure, and in vitro digestibility
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10518566/
https://www.ncbi.nlm.nih.gov/pubmed/37753325
http://dx.doi.org/10.1016/j.fochx.2023.100878
work_keys_str_mv AT zhangxuehua studyonthemechanismofsoyproteinisolatetoimprovequalityofreducedsalthypophthalmichthysmolitrixsurimigelfocusongelqualityproteinstructureandinvitrodigestibility
AT panhao studyonthemechanismofsoyproteinisolatetoimprovequalityofreducedsalthypophthalmichthysmolitrixsurimigelfocusongelqualityproteinstructureandinvitrodigestibility
AT jiangxin studyonthemechanismofsoyproteinisolatetoimprovequalityofreducedsalthypophthalmichthysmolitrixsurimigelfocusongelqualityproteinstructureandinvitrodigestibility
AT shiwenzheng studyonthemechanismofsoyproteinisolatetoimprovequalityofreducedsalthypophthalmichthysmolitrixsurimigelfocusongelqualityproteinstructureandinvitrodigestibility