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Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing–Thawing Cycles
This study aims to investigate the influence of the mixture (CGO/EWP) of carrageenan oligosaccharide (CGO) and egg white protein (EWP) (CGO/EWP, CGO: EWP = 1:1, m/m) on the functional, structural, and gelling properties of Culter alburnus myofibrillar protein (MP) during repeated freezing–thawing cy...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8772764/ https://www.ncbi.nlm.nih.gov/pubmed/35052537 http://dx.doi.org/10.3390/antiox11010032 |
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author | Zhang, Zhongli Xiong, Zhouyi Walayat, Noman Lorenzo, Jose M. Liu, Jianhua Nawaz, Asad Xiong, Hanguo |
author_facet | Zhang, Zhongli Xiong, Zhouyi Walayat, Noman Lorenzo, Jose M. Liu, Jianhua Nawaz, Asad Xiong, Hanguo |
author_sort | Zhang, Zhongli |
collection | PubMed |
description | This study aims to investigate the influence of the mixture (CGO/EWP) of carrageenan oligosaccharide (CGO) and egg white protein (EWP) (CGO/EWP, CGO: EWP = 1:1, m/m) on the functional, structural, and gelling properties of Culter alburnus myofibrillar protein (MP) during repeated freezing–thawing cycles by treating MP samples separately with EWP, CGO, or CGO/EWP based on the wet weight (1%, m/m), using samples without any cryoprotectant as the blank group. After the second repeated freezing–thawing cycle, the sulfhydryl group content was found to be significantly (p < 0.05) higher in the CGO/EWP (30.57 nmol/mg) and CGO (36.14 nmol/mg) groups than in the EWP group (23.80 nmol/mg), indicating that CGO/EWP and CGO can more effectively delay the oxidative deterioration of functional groups. Additionally, the surface hydrophobicity was shown to be significantly lower in the CGO (25.74) and CGO/EWP (27.46) groups than in the EWP (34.66) and blank (39.32) groups. Moreover, the α-helix content was higher in the CGO (35.2%) and CGO/EWP (32.3%) groups than in the EWP (29.2%) and blank (25.0%) groups. These data indicated that CGO and CGO/EWP could more effectively increase the structural stability, thereby inhibiting the exposure of hydrophobic groups and curbing the decline of α-helix content. During the heat-induced gel-forming process, EWP and CGO/EWP could enhance the gel viscoelasticity and strength. After the second freezing–thawing cycle, when compared with the blank group, the CGO/EWP group showed significantly (p < 0.05) higher water-holding capacity (66.30% versus 53.93%) and shorter T(22) relaxation time (413.56 versus 474.99 ms). The integrated results indicated that CGO/EWP could more effectively delay the decrease of protein–water molecular interaction forces in the MP gel. This study shed light on the mechanism of CGO/EWP as a cryoprotective mixture in improving the deterioration of MP gelation properties during repeated freezing–thawing cycles. |
format | Online Article Text |
id | pubmed-8772764 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87727642022-01-21 Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing–Thawing Cycles Zhang, Zhongli Xiong, Zhouyi Walayat, Noman Lorenzo, Jose M. Liu, Jianhua Nawaz, Asad Xiong, Hanguo Antioxidants (Basel) Article This study aims to investigate the influence of the mixture (CGO/EWP) of carrageenan oligosaccharide (CGO) and egg white protein (EWP) (CGO/EWP, CGO: EWP = 1:1, m/m) on the functional, structural, and gelling properties of Culter alburnus myofibrillar protein (MP) during repeated freezing–thawing cycles by treating MP samples separately with EWP, CGO, or CGO/EWP based on the wet weight (1%, m/m), using samples without any cryoprotectant as the blank group. After the second repeated freezing–thawing cycle, the sulfhydryl group content was found to be significantly (p < 0.05) higher in the CGO/EWP (30.57 nmol/mg) and CGO (36.14 nmol/mg) groups than in the EWP group (23.80 nmol/mg), indicating that CGO/EWP and CGO can more effectively delay the oxidative deterioration of functional groups. Additionally, the surface hydrophobicity was shown to be significantly lower in the CGO (25.74) and CGO/EWP (27.46) groups than in the EWP (34.66) and blank (39.32) groups. Moreover, the α-helix content was higher in the CGO (35.2%) and CGO/EWP (32.3%) groups than in the EWP (29.2%) and blank (25.0%) groups. These data indicated that CGO and CGO/EWP could more effectively increase the structural stability, thereby inhibiting the exposure of hydrophobic groups and curbing the decline of α-helix content. During the heat-induced gel-forming process, EWP and CGO/EWP could enhance the gel viscoelasticity and strength. After the second freezing–thawing cycle, when compared with the blank group, the CGO/EWP group showed significantly (p < 0.05) higher water-holding capacity (66.30% versus 53.93%) and shorter T(22) relaxation time (413.56 versus 474.99 ms). The integrated results indicated that CGO/EWP could more effectively delay the decrease of protein–water molecular interaction forces in the MP gel. This study shed light on the mechanism of CGO/EWP as a cryoprotective mixture in improving the deterioration of MP gelation properties during repeated freezing–thawing cycles. MDPI 2021-12-24 /pmc/articles/PMC8772764/ /pubmed/35052537 http://dx.doi.org/10.3390/antiox11010032 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zhang, Zhongli Xiong, Zhouyi Walayat, Noman Lorenzo, Jose M. Liu, Jianhua Nawaz, Asad Xiong, Hanguo Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing–Thawing Cycles |
title | Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing–Thawing Cycles |
title_full | Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing–Thawing Cycles |
title_fullStr | Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing–Thawing Cycles |
title_full_unstemmed | Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing–Thawing Cycles |
title_short | Influence of the Mixture of Carrageenan Oligosaccharides and Egg White Protein on the Gelation Properties of Culter alburnus Myofibrillar Protein under Repeated Freezing–Thawing Cycles |
title_sort | influence of the mixture of carrageenan oligosaccharides and egg white protein on the gelation properties of culter alburnus myofibrillar protein under repeated freezing–thawing cycles |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8772764/ https://www.ncbi.nlm.nih.gov/pubmed/35052537 http://dx.doi.org/10.3390/antiox11010032 |
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