Cargando…

A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation

Currently, the application of protein mixture derived from plants and animals is of great interest to the food industry. However, the synergistic effects of isolated protein blends (BL) are not well established. Herein, the development of a more effective method (co-precipitation) for the production...

Descripción completa

Detalles Bibliográficos
Autores principales: Zhou, Xiaohu, Zhang, Chaohua, Cao, Wenhong, Zhou, Chunxia, Zheng, Huina, Zhao, Liangzhong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8701264/
https://www.ncbi.nlm.nih.gov/pubmed/34945588
http://dx.doi.org/10.3390/foods10123037
_version_ 1784620958116478976
author Zhou, Xiaohu
Zhang, Chaohua
Cao, Wenhong
Zhou, Chunxia
Zheng, Huina
Zhao, Liangzhong
author_facet Zhou, Xiaohu
Zhang, Chaohua
Cao, Wenhong
Zhou, Chunxia
Zheng, Huina
Zhao, Liangzhong
author_sort Zhou, Xiaohu
collection PubMed
description Currently, the application of protein mixture derived from plants and animals is of great interest to the food industry. However, the synergistic effects of isolated protein blends (BL) are not well established. Herein, the development of a more effective method (co-precipitation) for the production of protein mixtures from pea and grass carp is reported. Pea protein isolate (PPI), grass carp protein isolate (CPI), and pea–carp protein co-precipitates (Co) were prepared via isoelectric solubilization/precipitation using peas and grass carp as raw materials. Meanwhile, the BL was obtained by blending PPI with CPI. In addition, the subunit composition and functional properties of Co and BL were investigated. The results show that the ratios of vicilin to legumin α + β and the soluble aggregates of Co were 2.82- and 1.69-fold higher than that of BL. The surface hydrophobicity of Co was less than that of BL, PPI, and CPI (p < 0.05). The solubility of Co was greater than that of BL, PPI, and CPI (p < 0.05), and the foaming activity was higher than that of BL and CPI (p < 0.05) but slightly lower than that of PPI. In addition, based on the emulsifying activity index, particle size, microstructure, and viscosity, Co had better emulsifying properties than BL, PPI, and CPI. The study not only confirmed that co-precipitation was more effective than blending for the preparation of mixed protein using PPI and CPI but also provided a standard of reference for obtaining a mixture of plant and animal proteins.
format Online
Article
Text
id pubmed-8701264
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-87012642021-12-24 A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation Zhou, Xiaohu Zhang, Chaohua Cao, Wenhong Zhou, Chunxia Zheng, Huina Zhao, Liangzhong Foods Article Currently, the application of protein mixture derived from plants and animals is of great interest to the food industry. However, the synergistic effects of isolated protein blends (BL) are not well established. Herein, the development of a more effective method (co-precipitation) for the production of protein mixtures from pea and grass carp is reported. Pea protein isolate (PPI), grass carp protein isolate (CPI), and pea–carp protein co-precipitates (Co) were prepared via isoelectric solubilization/precipitation using peas and grass carp as raw materials. Meanwhile, the BL was obtained by blending PPI with CPI. In addition, the subunit composition and functional properties of Co and BL were investigated. The results show that the ratios of vicilin to legumin α + β and the soluble aggregates of Co were 2.82- and 1.69-fold higher than that of BL. The surface hydrophobicity of Co was less than that of BL, PPI, and CPI (p < 0.05). The solubility of Co was greater than that of BL, PPI, and CPI (p < 0.05), and the foaming activity was higher than that of BL and CPI (p < 0.05) but slightly lower than that of PPI. In addition, based on the emulsifying activity index, particle size, microstructure, and viscosity, Co had better emulsifying properties than BL, PPI, and CPI. The study not only confirmed that co-precipitation was more effective than blending for the preparation of mixed protein using PPI and CPI but also provided a standard of reference for obtaining a mixture of plant and animal proteins. MDPI 2021-12-07 /pmc/articles/PMC8701264/ /pubmed/34945588 http://dx.doi.org/10.3390/foods10123037 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
Zhou, Xiaohu
Zhang, Chaohua
Cao, Wenhong
Zhou, Chunxia
Zheng, Huina
Zhao, Liangzhong
A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation
title A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation
title_full A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation
title_fullStr A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation
title_full_unstemmed A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation
title_short A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation
title_sort comparative functional analysis of pea protein and grass carp protein mixture via blending and co-precipitation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8701264/
https://www.ncbi.nlm.nih.gov/pubmed/34945588
http://dx.doi.org/10.3390/foods10123037
work_keys_str_mv AT zhouxiaohu acomparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhangchaohua acomparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT caowenhong acomparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhouchunxia acomparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhenghuina acomparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhaoliangzhong acomparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhouxiaohu comparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhangchaohua comparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT caowenhong comparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhouchunxia comparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhenghuina comparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation
AT zhaoliangzhong comparativefunctionalanalysisofpeaproteinandgrasscarpproteinmixtureviablendingandcoprecipitation