The influence of lipid content and pretreatment methods on protein conformation in fish (capelin, Mallotus villosus) during smoking and drying

The paper examines effects of blanching, drying, and smoking on capelin proteins as influenced by lipid content and pretreatment method. Changes in protein structure were due to denaturation and aggregation. Lipids had a protective effect on fish proteins from heat. Blanching and drying had the greatest influence on protein changes.

Abstract

The influence of lipid content and pretreatment methods (blanching and brining) on proteins conformation in fish (Capelin, Mallotus villosus) during drying and smoking were assessed. Soluble protein fractions were examined through changes in salt‐soluble proteins, sulfhydryl groups, and disulfide bonds contents. The salt level and moisture content were also evaluated. Conformational changes in muscle protein were significant (p < 0.05) after blanching and during initial drying when moisture content and dryness rates were high. Salt‐soluble proteins and total sulfhydryl groups contents reduced, whereas available sulfhydryl group and disulfide bonds contents intensified. The conformational changes were explained by muscle protein denaturation and aggregation ascribed to high temperature and dehydration during processing. The study reports fish protein denaturation to have reduced protein solubility as well as the nutritional value (loss of thermolabile compounds) and yield after smoking. More so, protein aggregation that was significantly (p < 0.05) higher in dried blanched fish could have reduced the dried fish sensory quality. Blanching pretreatment is thus not suitable for commercial capelin drying. Lipids were found to have protective effect against fish protein conformation.

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