Proteolysis of Sardine ( Sardina pilchardus ) and Anchovy ( Stolephorus commersonii ) by Commercial Enzymes in
Saline Solutions

Fish sauce production is a very long process and there is a great interest in shortening it. Among the different strategies to speed up this process, the addition of external proteases could be a solution. This study focuses on the effect of two commercial enzymes (Protamex and Protex 51FP) on the p...

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Bibliographic Details
Published in:Food technology and biotechnology Vol. 53; no. 1; pp. 87 - 90
Main Authors: Le, Chau Minh, Donnay-Moreno, Claire, Bruzac, Sandrine, Baron, Régis, Nguyen, Huong Thi My, Bergé, Jean Pascal
Format: Journal Article
Language:English
Published: Croatia Sveuciliste u Zagrebu, Prehramheno-Biotehnoloski Fakultet 01-01-2015
University of Zagreb
University of Zagreb Faculty of Food Technology and Biotechnology
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Summary:Fish sauce production is a very long process and there is a great interest in shortening it. Among the different strategies to speed up this process, the addition of external proteases could be a solution. This study focuses on the effect of two commercial enzymes (Protamex and Protex 51FP) on the proteolysis of two fish species traditionally converted into fish sauce: sardine and anchovy, by comparison with classical autolysis. Hydrolysis reactions were conducted with fresh fish at a temperature of 30 °C and under different saline conditions (from 0 to 30% NaCl). Hydrolysis degree and liquefaction of the raw material were used to follow the process. As expected, the proteolysis decreased with increasing amount of salt. Regarding the fish species, higher rate of liquefaction and higher hydrolysis degree were obtained with anchovy. Between the two proteases, Protex 51FP gave better results with both fish types. This study demonstrates that the addition of commercial proteases could be helpful for the liquefaction of fish and cleavage of peptide bonds that occur during fish sauce production and thus speed up the production process.
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ISSN:1330-9862
1334-2606
DOI:10.17113/ftb.53.01.15.3893