Channel catfish (Ictalurus punctatus) muscle protein isolate performance processed under different acid and alkali pH values.

Channel catfish (Ictalurus punctatus) muscle was subjected to 6 protein extraction and precipitation techniques using acid solubilization (pH 2.0, 2.5, and 3.0) or alkaline solubilization (pH 10.5, 11.0, 11.5) followed by precipitation at pH 5.5. The catfish protein isolate was compared with ground defatted white muscle. Alkali-processed catfish showed increased gel rigidity, gel strength, and gel flexibility compared to acid-processed catfish, which exhibited inconsistent functional performance, increasing and decreasing gel rigidity, gel strength, and gel flexibility. The gel rigidity (G') at pH 3.0 in the absence of salt had the highest G' of the acid treatments and was not significantly different from the alkaline-treated catfish muscle (P>0.05). However in the presence of added salt pH treatment it had the lowest G' and was different from alkaline treatments (P<0.05) during break force testing. These results show that pH-shift processing of channel catfish muscle provides highly functional isolates with a potentially broad range of applications. This range of applications is possible due to the modification of the textural properties of catfish muscle protein produced using different acidic or alkaline pH solubility treatments.

Carbon monoxide treatments to impart and retain muscle color in tilapia fillets.

Carbon monoxide (CO) has been used for improving the color of muscle foods. In the current study, we compared the postmortem treatment of tilapia fillets with 100% CO and euthanasia of live tilapia with CO for their ability to stabilize the color of white and red muscle of tilapia fillets. Both postmortem CO treatment and CO euthanasia were effective in increasing the redness (a* value) and lightness (L* value) of tilapia white and red muscle. Fillets obtained from CO-euthanized tilapia showed significantly higher a* and L* values during 1 mo of frozen storage at -20 degrees C and subsequent thawing and storage at 4 degrees C for 18 d. The amount of CO present in the red and white muscles decreased during the 18 d of storage at 4 degrees C. There was no significant difference in the pH, drip, or thaw loss of CO-treated tilapia fillets compared to the untreated fillets.

Effect of high pressure treatment on the quality of rainbow trout (Oncorhynchus mykiss) and mahi mahi (Coryphaena hippurus).

High pressure processing (HPP) is becoming a promising seafood preservation method. The objective was to investigate the effect of HPP on quality of rainbow trout and mahi mahi during cold storage. Skinless fillets treated with different pressures (150, 300, 450, and 600 MPa for 15 min) and stored at 4 degrees C were analyzed at 1, 3, and 6 d storage. Red muscle was analyzed for lipid oxidation products by measuring thiobarbituric reactive substances (TBARS) and whole muscle was analyzed for total aerobic count, texture profile analysis, and color. A pressure of 300 MPa effectively inactivated the initial microbial population in rainbow trout (6-log reduction). However, inactivation of the initial population on mahi mahi was only about 4-log reduction at the same pressure. Microbial growth was significantly retarded after HPP. Color results showed that redness (a* value) of rainbow trout at 300 MPa and above was significantly (P < 0.05) lower compared to mahi mahi. TBARS values for rainbow trout increased with increased pressure, whereas the same trend was not seen for mahi mahi where maximum oxidation was found at 300 MPa and then declined. This study demonstrates the usefulness of HPP in seafood processing and the influence of species variation on processing parameters. The optimum HPP conditions for influencing lipid oxidation, microbial load, and color changes were found to be 300 MPa for rainbow trout and 450 MPa for mahi mahi.

Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases.

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).

Fish protein hydrolysates: production, biochemical, and functional properties.

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.