Valorization of Aquaculture By-Products of Salmonids to Produce Enzymatic Hydrolysates: Process Optimization, Chemical Characterization and Evaluation of Bioactives.

Mar Drugs

Grupo de Biotecnología y Bioprocesos Marinos, Instituto de Investigaciones Marinas (IIM-CSIC), C/Eduardo Cabello, 6, CP 36208 Vigo, Galicia, Spain.

Published: November 2019

In the present manuscript, various by-products (heads, trimmings, and frames) generated from salmonids (rainbow trout and salmon) processing were evaluated as substrates for the production of fish protein hydrolysates (FPHs), potentially adequate as protein ingredients of aquaculture feeds. Initially, enzymatic conditions of hydrolysis were optimized using second order rotatable designs and multivariable statistical analysis. The optimal conditions for the Alcalase hydrolysis of heads were 0.1% (v/w) of enzyme concentration, pH 8.27, 56.2°C, ratio (Solid:Liquid = 1:1), 3 h of hydrolysis, and agitation of 200 rpm for rainbow trout and 0.2% (v/w) of enzyme, pH 8.98, 64.2 °C, 200 rpm, 3 h of hydrolysis, and S:L = 1:1 for salmon. These conditions obtained at 100 mL-reactor scale were then validated at 5L-reactor scale. The hydrolytic capacity of Alcalase and the protein quality of FPHs were excellent in terms of digestion of wastes (V > 84%), high degrees of hydrolysis ( > 30%), high concentration of soluble protein (Prs > 48 g/L), good balance of amino acids, and almost full digestibility (Dig > 93%). Fish oils were recovered from wastes jointly with FPHs and bioactive properties of hydrolysates (antioxidant and antihypertensive) were also determined. The salmon FPHs from trimmings + frames (TF) showed the higher protein content in comparison to the rest of FPHs from salmonids. Average molecular weights of salmonid-FPHs ranged from 1.4 to 2.0 kDa and the peptide sizes distribution indicated that hydrolysates of rainbow trout heads and salmon TF led to the highest percentages of small peptides (0-500 Da).

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6950744PMC
http://dx.doi.org/10.3390/md17120676DOI Listing

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