Emulsion and Surface-Active Properties of Fish Solubles Based on Direct Extraction and after Hydrolysis of Atlantic Cod and Atlantic Salmon Backbones

• Published in: Foods
• Main Authors: Silje Steinsholm, Åge Oterhals, Jarl Underhaug, Tone Aspevik
• Format: Article in Journal/Newspaper
• Language: English
• Published: MDPI AG 2020
• Subjects: enzymatic protein hydrolysates; emulsion activity; critical micelle concentration; fish by-products; emulsion stability; Chemical technology; TP1-1185; atlantic cod; Atlantic salmon
• Online Access: https://doi.org/10.3390/foods10010038; https://doaj.org/article/9d1f90f0deae4b619e73a3e39cbfb412

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.