Extraction optimization of gel-forming proteins and collagen hydrolysate from whole lanternfish (Benthosema pterotum) with a biorefinery approach

Document Type : scientific research article

Authors

1 gorgan university

2 fisheries, Gorgan University of Agricultural Sciences and natural Resources

3 Chalmers University

4 Gorgan uni

Abstract

Here the advantages of employing a biorefinery approach in conjunction with optimization techniques were utilized to attain high overall process efficiency. Initially, an alkaline pH-shift process assisted by ultrasonic and its subsequent optimization were employed to maximize the extraction yield and whiteness index of muscle proteins isolated from lanternfish (B. pterotum). The optimal strategy was determined as follows: 6 mL g-1, pH1 (solubilization) 11.5, 310 W, and pH2 (precipitation) 5.8 with desirability of 0.84. Collagen hydrolysate was obtained from the connective tissue-containing sediment residue emerging during pH-shift process. The optimal isolated protein (OIP) was utilized to produce heat-set gels in combination with collagen hydrolysate. Breaking force and deformation of the OIP gel were measured at 123 (g) and 10.12 (mm) respectively. Collagen hydrolysate made breaking force (up to 2% w/w) and deformation (up to 10% w/w) improved and had positive effects on color characteristics (especially whiteness index) as well as water holding capacity. Hence, it can be concluded that the integration of a novel extraction technique such as ultrasonic with pH-shift process followed by optimization, as well as concurrent utilization of muscle and connective tissue proteins through a biorefinery approach; provides a significant advancement towards scaling up the extraction process.

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