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1.
J Agric Food Chem ; 52(3): 597-601, 2004 Feb 11.
Artigo em Inglês | MEDLINE | ID: mdl-14759155

RESUMO

Surimi containing omega-3 fatty acids from algal oil was prepared by the addition of oil-in-water emulsions or bulk oil. Emulsion and bulk oil were added separately to surimi to provide approximately 500 mg of omega-3 fatty acids per serving of surimi (85 g). Addition of the emulsion had no effect on surimi gel strength, whereas bulk oil decreased gel strength an average of 31%. All surimi treatments containing algal oil increased in Hunter b values due to the presence of carotenoids in the oil. Among cryoprotectants, sodium tripolyphosphate was the major surimi additive responsible for retarding the formation of lipid hydroperoxides and thiobarbituric acid reactive substances (TBARS). Lipid hydroperoxide and TBARS formation was lower in surimi containing bulk oil compared to surimi with emulsified oil. Both EDTA and lipid soluble antioxidants were able to decrease lipid oxidation in surimi fortified with omega-3 fatty acids. This suggests that surimi containing nutritionally beneficial omega-3 fatty acids could be developed with good oxidative stability and gel strength.


Assuntos
Ácidos Graxos Ômega-3/análise , Produtos Pesqueiros/análise , Alimentos Fortificados , Animais , Antioxidantes/farmacologia , Crioprotetores , Ácido Edético/farmacologia , Emulsões , Peroxidação de Lipídeos , Músculo Esquelético , Substâncias Reativas com Ácido Tiobarbitúrico/análise
2.
J Agric Food Chem ; 51(14): 3992-8, 2003 Jul 02.
Artigo em Inglês | MEDLINE | ID: mdl-12822935

RESUMO

Fish muscle proteins can be isolated from a variety of low-value raw materials by solubilization in either acid or base. If the consistency of the resulting solution is sufficiently low, it is possible to recover most of the solubilized proteins and remove most of the lipids by centrifugation. Lipid removal should greatly stabilize the isolated proteins. In a previous investigation into the use of herring for production of these protein isolates, it was observed that this species had particularly high consistency values when the proteins were solubilized. This study was undertaken to determine the consistencies obtained with herring light muscle tissue over the pH range covered by the two processes, from about pH 2.7 to 10.8. Protein solubility was compared to consistency of the resultant solutions. Maximum consistencies of the homogenates, approximately 220 and approximately 175 mPa.s, were obtained at pH values of approximately 3.5 and 10.5, respectively. Consistency began to increase approximately when solubilization began. Storage of homogenates at pH 2.7 decreased the consistency over a 10 min time period. The magnitude of the consistency peaks at both acid and alkaline pH values increased when using ice-stored as well as frozen-stored herring, especially in the acid range. Protein solubility at pH <4 and pH >/=10.8 slightly decreased after post-mortem storage of the herring muscle. It is suggested that the observed changes in consistency result from the expansion and solvation of protein aggregates which eventually dissociate into smaller units, perhaps even monomers.


Assuntos
Peixes/metabolismo , Proteínas Musculares/química , Proteínas Musculares/isolamento & purificação , Animais , Concentração de Íons de Hidrogênio , Músculos/química , Solubilidade
3.
J Agric Food Chem ; 50(25): 7371-9, 2002 Dec 04.
Artigo em Inglês | MEDLINE | ID: mdl-12452661

RESUMO

Proteins from herring (Clupea harengus) light muscle were extracted using acidic or alkaline solubilization; 92 and 89% of the initial muscle proteins were solubilized at pH 2.7 and 10.8, respectively, of which 96 and 94% were recovered during precipitation at pH 5.5. Consistency of the pH-adjusted muscle homogenates increased with increased raw material age and homogenization intensity; it declined following holding on ice. Some hydrolytic myofibrillar protein degradation occurred during cold storage of the acidified (pH 2.7) homogenates. With alkalized homogenates, hydrolysis was negligible. The total lipid content changed from 0.13 g/g of protein in the muscle to 0.04 g/g of protein in both the acid- and alkali-produced protein isolates. Corresponding values for the phospholipid content were from 0.037 to 0.02 g/g of proteins. Acid- and alkali-produced proteins made gels with equal strain and color. Stress values were equal or lower in acid- versus alkali-produced protein gels. When ice-stored raw material was used, strain and stress values of gels were reduced.


Assuntos
Peixes , Proteínas Musculares/isolamento & purificação , Músculo Esquelético/química , Animais , Centrifugação , Precipitação Química , Géis , Concentração de Íons de Hidrogênio , Hidrólise , Miofibrilas/química , Solubilidade
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