Characterization of protein hydrolysates and lipids obtained from black scabbardfish (Aphanopus carbo) by-products and antioxidative activity of the hydrolysates produced
Introduction
The fishery of black scabbard fish (Apanopus carbo) in the Portuguese continental waters started in the 1980s. In last years the landings of this species in the continental fishing harbours has been around 3000 metric tons. Black scabbardfish is a deep sea fish caught by long lines at depths around 1000 m. It is mostly sold eviscerated with head on but it is also processed into fillets and sold as fresh fillets. The by-products generated in the filleting process are mainly constituted by heads, some viscera, skin, backbone and trimmings. This material is usually reduced into fish meal. However, these proteinaceous by-products may be also upgraded by converting them in fish protein hydrolysates (FPH), which has been recognized as an alternative to upgrading these raw materials in many works [1], [2], [3], [4], [5]. The production of FPH also enables the recovery of bones and skins present in the by-products, which can be used for the extraction of high added value products. FPH present a wide range of potential applications, which include the use in animal feeds [6], [7], [8], [9], [10], foods [11], [12], [13] or microbial growth media [14], [15], [16], [17], [18], [19], [20]. FPH also exhibits antioxidant properties such as reported by several authors [4], [21], [22], [23], [24], [25], [26], [27], [28] and constitute a source of health beneficial molecules such as secretagogues, calciotropic hormones and growth factors [29], [30], [31], [32]. In addition hypotensive activity [33], [34], [35], immuno-stimulant activity [36], [37], and antiproliferative activity [38] has been found as well. The production of protein hydrolysates has been also used as a tool for the lipid recovery from by-products [39], [40], [41]. The mild temperature conditions used in this method makes it suitable to hamper autoxidative changes occurring in the highly unsaturated fatty acids present in marine lipids. The beneficial health effects of these lipids are well documented and have increasing applications in foods and feeds for aquaculture, healthcare and pharmaceutical products.
The aim of this study was to produce a protein hydrolysate from BSB with different DH using Protamex, to characterize the lipid fraction and to evaluate the antioxidative activities of the hydrolysates obtained.
Section snippets
Raw material
Fresh black scabbardfish (Aphanopus carbo) by-products (heads, viscera, frames, skin, trimmings) from the filleting industry were ground and immediately frozen in 100 g plastic bags and stored at −20 °C until use.
Enzymes
The food-grade enzyme Protamex™ (EC. 3.4.21.14/3.4.24.28) a protease complex from Bacillus subtilis with optimal working conditions at 35–60 °C and at pH 5.5–7.5 was provided by Novo Nordisk (Bagsvaerd, Denmark).
Proximate chemical composition
Moisture was determined by drying the samples in an oven at 105 ± 2 °C for 24 h.
Results and discussion
The proximate chemical composition of BSB was 70.39% water, 14.92% protein, 10.13% fat, and 3.53% ash. The fat content is higher than the usual range reported [53] for the edible part of black scabbardfish because some liver remained in the BSB used. The ash content is also above the range 0.9–1.2% indicated for the edible part of this species, which may result from the presence of high proportion of bones in the raw material. The dried BSB hydrolysates prepared with 1% Protamex had 3.16%
Conclusion
This study allow to concluding that Protamex is suitable for the preparation of protein hydrolysates from black scabbardfish by-products. About 80% of nitrogen solubilization and 60% of DH were achieved with 1% of Protamex after 2 h of hydrolysis. The hydrolysis with this enzyme also permitted the separation of oil, which attained almost 40% of the initial oil content of the raw material. The BSB hydrolysates present some antioxidant activity, which increased with increasing DH. The high
Acknowledgement
This work was done in the frame of the projects BE-FAIR (LIFE 05 ENV/E000267-BE FAIR).
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