Functional Properties of Enzyme‐modified Acylated Fish Protein Derivatives

Miller, Ruth; Groninger, Herman S.

doi:10.1111/j.1365-2621.1976.tb00598.x

Cited by 78 publications

(37 citation statements)

References 15 publications

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“…Foaming capacity (FC) and foaming stability (FS) were determined by the method applied by Miller and Groniger (1976). An amount of powder was added to distilled water to make a solution with 10% protein.…”

Section: Methodsmentioning

confidence: 99%

Characteristics of freeze-dried fish protein isolated from saithe (Pollachius virens)

et al. 2011

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Fish proteins isolated from by-products or low commercial/underutilized species using pH-shift process is a new source of proteins that may be used as wet or dried ingredients to develop value-added convenience foods. This paper reports the effects of freeze-drying on characteristics of fish protein isolates (FPI) from saithe (Pollachius virens) with or without lyoprotectants. Freeze-dried saithe mince from the same lot and without additives was used as a control. The resulting fish protein powders contained 71-93% protein, 1.5-3% moisture, 0-21% carbohydrate and 0.5-2% fat. Lipid oxidation (assessed by TBARS) of FPI powder groups was higher than that of fish mince powder. The results revealed that oxidation started during the pHshift process and was increased by freeze-drying. Functional properties and sensory attributes were influenced by the advanced oxidation. However, the mince powder was less oxidized and had higher functional properties such as water binding capacity, gel forming ability, emulsification, foaming properties and colour and lower sensory scores for rancid odour and flavour than the FPI powders. Further studies on how to prevent oxidation of fish flesh during pHshift and drying processes are recommended.

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Section: Methodsmentioning

confidence: 99%

Characteristics of freeze-dried fish protein isolated from saithe (Pollachius virens)

et al. 2011

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“…Besides the underutilized trash fish, the waste generated from fish processing operations contains 27-49% protein on a dry weight basis and constitutes another valuable resource (3). Since the 1940s, a variety of chemical modifications have been employed to modify the functional properties (water absorption, emulsifying activity, emulsifying capacity, gelation and aeration capacity) of fish protein (FP) concentrate (4)(5)(6). However, these chemically modified protein products have never been introduced in the market owing to safety concerns.…”

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confidence: 99%

Synthesis and properties of fish protein‐based hydrogel

Hwang

Damodaran

1997

J Americ Oil Chem Soc

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The novel use of fish protein (FP) in the manufacture of a superabsorbent hydrogel was investigated. Following the introduction of a large number of hydrophilic groups into fish protein by modification with ethylenediaminetetraacetic dianhydride (EDTAD), proteins were cross-linked by sulfhydryl-disulfide interchange reaction between the endogenous sulfhydryl groups and disulfide bonds to produce an insoluble gel structure. The water uptake of 76% EDTAD-modified FP hydrogel was 540 g water/g dry gel at 214 × g, and it depended on pH and ionic strength of the solution. The structural changes in proteins consequent to modification were also investigated. EDTAD-FP hydrogels had increased rigidity after glutaraldehyde treatment but displayed diminished water uptake characteristics.The total world fishery catch was about one million metric tons in 1993 (1), of which approximately 30% can be considered underutilized and unexploited by-catch (2). Typically, most of these low-cost fish resources are used in the manufacture of fish meal. Besides the underutilized trash fish, the waste generated from fish processing operations contains 27-49% protein on a dry weight basis and constitutes another valuable resource (3). Since the 1940s, a variety of chemical modifications have been employed to modify the functional properties (water absorption, emulsifying activity, emulsifying capacity, gelation and aeration capacity) of fish protein (FP) concentrate (4-6). However, these chemically modified protein products have never been introduced in the market owing to safety concerns. In the present study, a new application for FP as a superabsorbent hydrogel for nonfood uses has been investigated. The process to synthesize FP hydrogel and the swelling properties of the gel are described. EXPERIMENTAL PROCEDURESMaterials. Ethylenediaminetetraacetic dianhydride (EDTAD) and N-acetylhomocysteine thiolactone (NAHCTL) were obtained from Aldrich Chemical Co. (Milwaukee, WI). Picrylsulfonic acid (TNBS), 25% glutaraldehyde solution, and 5,5′-dithio-bis(2-nitrobenzoic acid) were from Sigma Chemical Co. (St. Louis, MO). All other chemicals were of analytical grade. Heat-sealable, water-wettable paper was purchased from Bolmet Inc. (Dayville, CT).Preparation of crude FP. The fish used in this study was walleye pike (Stizostedion vitreum), obtained from a Wisconsin fish farm. The fish were filleted immediately upon arrival, and whole muscle was chopped and blended in chilled deionized water at a meat-to-water ratio of 1:10. The pH of the fish suspension was adjusted to 12 by the addition of 2.5 N NaOH solution, and the suspension was mixed for 30 min to totally solubilize the fish protein (FP) from muscle cells. The suspension was filtered through a 0.5-mm sieve to remove insoluble material. The filtrate was dialyzed against water (the molecular weight cut-off of the membrane was 6,000-8,000 Daltons) and lyophilized.Protein determination. The protein content of the lyophilized sample was determined by subtracting the lipid and moisture content of ...

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“…So liegen Ergebnisse verschiedener Laboratorien iiber die funktionellen Eigenschaften acetylierter und succinylierter Proteine tierischer (Fischproteine [2][3][4][5], Eiproteine [6--81 Effect of succinylation on some physico-chemical and functional properties of casein Succinylation of amino groups of the casein complex results in a spontaneous dissociation of the protein into low-molecular 1.84 components. Succinylated samples of casein are characterized by a higher electrophoretic mobility of the components in alkaline mediums and by a lower mobility in acidic buffer systems.…”

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confidence: 99%

Chemische Modifizierung von Proteinen 7. Mitt. Beeinflussung physikochemischer und funktioneller Eigenschaften von Casein durch Succinylierung

Schwenke

Rauschal

Linow³

et al. 1981

Nahrung

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Succinylation of amino groups of the casein complex results in a spontaneous dissociation of the protein into low-molecular 1.8-S components. Succinylated samples of casein are characterized by a higher electrophoretic mobility of the components in alkaline mediums and by a lower mobility in acidic buffer systems. The anodic migration in alkaline buffer systems increases depending on the degree of modification. This effect is more pronounced for the beta-casein than for the alpha s-casein fraction. In the potentiometric acid-base titration of the modified casein a hysteresis occurs during the back-titration. Increasing with the degree of modification, this effect points to a more or less strong break-up of the structure (entropy production). The solubility minimum of casein is shifted to lower pH values by succinylation. Samples succinylated to 90 or more per cent of the amino groups are insoluble at pH less than 3.5. Succinylated casein shows at a moderate degree of substitution (approximately equal to 40%) a highly increased water adsorption capacity. The oil adsorption capacity of the protein decreases after succinylation. Amongst the modified casein samples those ones with the highest water adsorption show the highest oil adsorption, too. The emulsifying capacity of low (approximately equal to 20%) succinylated casein samples decreases below the value determined for the unmodified protein. At higher modified samples the emulsifying capacity increases as the degree of succinylation increases. The emulsifying activity and emulsion stability of modified samples are lower than that measured for the parent protein. The foaming capacity of the casein is not improved by succinylation.

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Functional Properties of Enzyme‐modified Acylated Fish Protein Derivatives

Cited by 78 publications

References 15 publications

Characteristics of freeze-dried fish protein isolated from saithe (Pollachius virens)

Characteristics of freeze-dried fish protein isolated from saithe (Pollachius virens)

Synthesis and properties of fish protein‐based hydrogel

Chemische Modifizierung von Proteinen 7. Mitt. Beeinflussung physikochemischer und funktioneller Eigenschaften von Casein durch Succinylierung

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