Considerable amounts of fish processing byproducts are discarded each year. By developing enzyme technologies for protein recovery and modification, production of a broad spectrum of food ingredients and industrial products may be possible. Hydrolyzed vegetable and milk proteins are widely used food ingredients. There are few hydrolyzed fish protein foods with the exception of East Asian condiments and sauces. This review describes various manufacturing techniques for fish protein hydrolysates using acid, base, endogenous enzymes, and added bacterial or digestive proteases. The chemical and biochemical characteristics of hydrolyzed fish proteins are discussed. In addition, functional properties of fish protein hydrolysates are described, including solubility, water-holding capacity, emulsification, and foam-forming ability. Possible applications of fish protein hydrolysates in food systems are provided, and comparison with other food protein hydrolysates where pertinent.

Protein hydrolysates (5, 10, and 15% degrees of hydrolysis) were made from minced salmon muscle treated with one of four alkaline proteases (Alcalase 2.4L, Flavourzyme 1000L, Corolase PN-L, and Corolase 7089) or endogenous digestive proteases. Reaction conditions were controlled at pH 7.5, 40 degrees C, and 7.5% protein content, and enzymes were added on the basis of standardized activity units (Azocoll units). Proteases were heat inactivated, insoluble and unhydrolyzed material was centrifuged out, and soluble protein fractions were recovered and lyophilized. Substrate specificities for the proteases was clearly different. Protein content for the hydrolysates ranged from 71.7 to 88.4%, and lipid content was very low. Nitrogen recovery ranged from 40.6 to 79.9%. The nitrogen solubility index was comparable to that of egg albumin and ranged from 92.4 to 99.7%. Solubility was high over a wide range of pH. The water-holding capacity of fish protein hydrolysates added at 1.5% in a model food system of frozen minced salmon patties was tested. Drip loss was on average lower for the fish protein hydrolysates than for egg albumin and soy protein concentrate, especially for Alcalase hydrolysates. Emulsification capacity for fish protein hydrolysates ranged quite a bit (75-299 mL of oil emulsified per 200 mg of protein), and some were better than soy protein concentrate (180 mL of oil emulsified per 200 mg of protein), but egg albumin had the highest emulsifying capacity (417 mL of oil emulsified per 200 mg of protein). Emulsification stability for fish protein hydrolysates (50-70%) was similar to or lower than those of egg albumin (73%) or soy protein concentrate (68%). Fat absorption was greater for 5 and 10% degrees of hydrolysis fish protein hydrolysates (3.22-5.90 mL of oil/g of protein) than for 15% hydrolysates, and all had greater fat absorption than egg albumin (2. 36 mL of oil/g of protein) or soy protein concentrate (2.90 mL of oil/g of protein).

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A process for the effective extraction and fractionation of phlorotannins from Fucus vesiculosus with high antioxidant potentials was investigated. The antioxidant activity of F. vesiculosus extract/fractions was assessed by 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging, reducing power, and ferrous ion-chelating assays. Among the crude extract and different polarity fractions, the phlorotannin-enriched ethyl acetate fraction possessed the highest DPPH scavenging activity and reducing power. This fraction was further fractionated by Sephadex LH-20 column chromatography or ultrafiltration. The antioxidant properties were evaluated by both the above chemical antioxidant tests and a mononuclear cell-based bioassay. Sephadex subfractions LH-2 and LH-3 with high total phlorotannin content exhibited strong DPPH quenching activity, comparable to those of ascorbic acid and butylated hydroxytoluene and significantly higher than that of α-tocopherol. Polyphenols in F. vesiculosus were found to consist mainly of high molecular weight phlorotannin polymers. There were no clear relationships between the degree of polymerization, molecular size, and antioxidant activity. All the subfractions separated by Sephadex LH-20 column chromatography and ultrafiltration showed a high ability to scavenge reactive oxygen species generated by mononuclear cells. Further characterization of the phlorotannin compounds was performed on six Sephadex subfractions. Several phlorotannin oligomers were tentatively identified on the basis of HPLC-ESI-MS(n) analyses.

Conformational and structural changes of cod myosin at pH 2.5 and 11 and after subsequent pH readjustment to pH 7.5 were studied. Results suggest that on acid unfolding, the myosin rod may fully dissociate due to electrostatic repulsion within the coiled coil, while it does not dissociate at alkaline pH. Both pHs led to significant conformational changes in the globular head fraction of the myosin heavy chains, suggesting that it takes on a molten globular configuration. A large part of the myosin light chains are lost on both pH treatments. On pH readjustment to neutrality, the heavy chains take on a structural form similar to the native state with the coiled-coil rod reassociating from acid pH while leaving the globular head less packed, more hydrophobic and structurally less stable. The irreversible change brought about in the globular head region leads to the failure of light chains to reassemble onto it, a drastic loss in ATPase activity, and more exposure of reactive thiol groups. The acid and alkali processes therefore lead to substantial changes in the globular part of the myosin molecule and perhaps more importantly to different molecular changes in myosin, depending on which pH treatment is employed.