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Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes

The goal of this work is to explore if pH-shift processing could be used as a cold refinery technique to manufacture pig brain protein isolate (PI). Pig brain protein had the highest solubility at pH 2 (acid method) and pH 12 (alkaline method). As the protein solution’s zeta-potential was near 0 wit...

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Autores principales: Chanted, Jaruwan, Panpipat, Worawan, Cheong, Ling-Zhi, Chaijan, Manat
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8909572/
https://www.ncbi.nlm.nih.gov/pubmed/35267327
http://dx.doi.org/10.3390/foods11050695
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author Chanted, Jaruwan
Panpipat, Worawan
Cheong, Ling-Zhi
Chaijan, Manat
author_facet Chanted, Jaruwan
Panpipat, Worawan
Cheong, Ling-Zhi
Chaijan, Manat
author_sort Chanted, Jaruwan
collection PubMed
description The goal of this work is to explore if pH-shift processing could be used as a cold refinery technique to manufacture pig brain protein isolate (PI). Pig brain protein had the highest solubility at pH 2 (acid method) and pH 12 (alkaline method). As the protein solution’s zeta-potential was near 0 with the lowest solubility, pH 5.0 was chosen as the precipitation pH. Alkaline process produced a 32% dry matter yield with phospholipid content of 35 mg/100 g. The alkaline-made PI was better at forming soft gels and had good emulsifying and foaming capabilities. Although the acid-made PI included less residual lipid and total haem protein and was whiter in colour, it could not be gelled. Acid-made PI was more prone to lipid oxidation with a poorer ability to function as an emulsifier and foaming agent. Thus, functional proteins from pig brain may be isolated using the alkaline pH-shift technique.
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spelling pubmed-89095722022-03-11 Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes Chanted, Jaruwan Panpipat, Worawan Cheong, Ling-Zhi Chaijan, Manat Foods Article The goal of this work is to explore if pH-shift processing could be used as a cold refinery technique to manufacture pig brain protein isolate (PI). Pig brain protein had the highest solubility at pH 2 (acid method) and pH 12 (alkaline method). As the protein solution’s zeta-potential was near 0 with the lowest solubility, pH 5.0 was chosen as the precipitation pH. Alkaline process produced a 32% dry matter yield with phospholipid content of 35 mg/100 g. The alkaline-made PI was better at forming soft gels and had good emulsifying and foaming capabilities. Although the acid-made PI included less residual lipid and total haem protein and was whiter in colour, it could not be gelled. Acid-made PI was more prone to lipid oxidation with a poorer ability to function as an emulsifier and foaming agent. Thus, functional proteins from pig brain may be isolated using the alkaline pH-shift technique. MDPI 2022-02-26 /pmc/articles/PMC8909572/ /pubmed/35267327 http://dx.doi.org/10.3390/foods11050695 Text en © 2022 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
Chanted, Jaruwan
Panpipat, Worawan
Cheong, Ling-Zhi
Chaijan, Manat
Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes
title Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes
title_full Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes
title_fullStr Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes
title_full_unstemmed Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes
title_short Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes
title_sort recovery of functional proteins from pig brain using ph-shift processes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8909572/
https://www.ncbi.nlm.nih.gov/pubmed/35267327
http://dx.doi.org/10.3390/foods11050695
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