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Application of a crude digestive proteases preparation to improve the ripening of marinated fillets from low-technological value Baltic herring (Clupea harengus membras L.). | LitMetric

Background: As a result of climate change (reduced the oxygen content and food available in the waters) and overfishing, ever larger batches of the herring catch are classified as low-value fish and used for feedstuff or canned food production. Fast and complete ripening of marinated fillets, especially from low-value Baltic herring, poses a problem because of the low muscle protease activity and changes in muscle tissue proteins.

Results: For the first time, a crude digestive proteases preparation (CDPP) was obtained from herring viscera using a two-stage method consisting of ethanol extraction and then salt precipitation. CDPP had a reduced hemoglobin content, with optimum activity at pH 7.5-8.8 or 60-120 g kg NaCl. At pH 4-5, it still exhibited 24-68% of proteolytic activity. CDPP was used for 4-24 h of brining of fresh and frozen-thawed fillets or injection of fresh fillets before marinating. CDPP-brining increased especially cathepsin D and carboxypeptidase A activities, whereas it decreased cathepsin B and L activities in the marinades. CDPP-brining mitigated the negative effect of freezing-thawing on mass-yield, protease activity, protein hydrolysis, texture profile, colour and sensory quality of the marinated fillets. CDPP-injection was found to be the best method because it increased mass-yield and ripeness of the marinated fillets to a greater extent than CDPP-brining did. The marinades from the CDPP-treated fillets had no bitter taste as a result of the presence of hemoglobin or chymotrypsin, and there were no results indicating lipid oxidation.

Conclusion: The application of CDPP in marinating technology is a viable approach to enable the use of low-value herring in food production, shorten the marinating time, and improve the ripeness and sensory quality of meat. © 2024 Society of Chemical Industry.

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http://dx.doi.org/10.1002/jsfa.13358DOI Listing

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