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Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones
The focus on natural foods and “clean” labeled products is increasing and encourages development of new biobased ingredients. Fish solubles derived from downstream processing of side stream materials in the fish filleting industries have potential as emulsifiers based on their surface-active and emu...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7824041/ https://www.ncbi.nlm.nih.gov/pubmed/33375534 http://dx.doi.org/10.3390/foods10010038 |
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author | Steinsholm, Silje Oterhals, Åge Underhaug, Jarl Aspevik, Tone |
author_facet | Steinsholm, Silje Oterhals, Åge Underhaug, Jarl Aspevik, Tone |
author_sort | Steinsholm, Silje |
collection | PubMed |
description | The focus on natural foods and “clean” labeled products is increasing and encourages development of new biobased ingredients. Fish solubles derived from downstream processing of side stream materials in the fish filleting industries have potential as emulsifiers based on their surface-active and emulsion stabilizing properties. The aim of this study was to evaluate and compare emulsion properties and critical micelle concentration (CMC) of direct protein extracts and protein hydrolysates based on fish backbones, and to identify associations between molecular weight distribution and process yield with the studied physicochemical properties. Protein extracts and enzymatic protein hydrolysates were produced based on two raw materials (cod and salmon backbones), two enzymes with different proteolytic specificity, and varying hydrolysis time. Emulsion activity index (EAI), emulsion stability index (ESI) and CMC were measured and compared with casein as a reference to protein-based emulsifiers. Protein hydrolysis was found to have negative impact on EAI and CMC, likely due to generation of small peptides disrupting the amphiphilic balance. The direct protein extracts had comparable EAI with casein, but the latter had superior ESI values. Protein hydrolysates with acceptable EAI could only be obtained at the expense of product yield. The study emphasizes the complexity of physicochemical properties of protein hydrolysates and discusses the challenges of achieving both good surface-active properties and high product yield. |
format | Online Article Text |
id | pubmed-7824041 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-78240412021-01-24 Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones Steinsholm, Silje Oterhals, Åge Underhaug, Jarl Aspevik, Tone Foods Article The focus on natural foods and “clean” labeled products is increasing and encourages development of new biobased ingredients. Fish solubles derived from downstream processing of side stream materials in the fish filleting industries have potential as emulsifiers based on their surface-active and emulsion stabilizing properties. The aim of this study was to evaluate and compare emulsion properties and critical micelle concentration (CMC) of direct protein extracts and protein hydrolysates based on fish backbones, and to identify associations between molecular weight distribution and process yield with the studied physicochemical properties. Protein extracts and enzymatic protein hydrolysates were produced based on two raw materials (cod and salmon backbones), two enzymes with different proteolytic specificity, and varying hydrolysis time. Emulsion activity index (EAI), emulsion stability index (ESI) and CMC were measured and compared with casein as a reference to protein-based emulsifiers. Protein hydrolysis was found to have negative impact on EAI and CMC, likely due to generation of small peptides disrupting the amphiphilic balance. The direct protein extracts had comparable EAI with casein, but the latter had superior ESI values. Protein hydrolysates with acceptable EAI could only be obtained at the expense of product yield. The study emphasizes the complexity of physicochemical properties of protein hydrolysates and discusses the challenges of achieving both good surface-active properties and high product yield. MDPI 2020-12-25 /pmc/articles/PMC7824041/ /pubmed/33375534 http://dx.doi.org/10.3390/foods10010038 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Steinsholm, Silje Oterhals, Åge Underhaug, Jarl Aspevik, Tone Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones |
title | Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones |
title_full | Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones |
title_fullStr | Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones |
title_full_unstemmed | Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones |
title_short | Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones |
title_sort | emulsion and surface-active properties of fish solubles based on direct extraction and after hydrolysis of atlantic cod and atlantic salmon backbones |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7824041/ https://www.ncbi.nlm.nih.gov/pubmed/33375534 http://dx.doi.org/10.3390/foods10010038 |
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