• Macromolecular Research
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• v.15 no.7
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• pp.671-675
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• 2007

Soybean proteins appear to harbor a great deal of potential as functional ingredients due to the fact that they are composed of highly bioavailable peptides and amino acids. To develop drink- or gel-type foods formulated with soybean protein, the physicochemical properties of intact and chemically modified soy glycinin were assessed. Maleylation to soy glycinin altered the surface charges of glycinin via the modification of lysine residues, and subsequently generated the dissociation of glycinin subunits owing to the increase in charge repulsion. This modification thus improved the solubility of glycinin, particularly under acidic pH conditions. It is worthy of note that maleylation increased the susceptibility of the basic subunits of mTGase and the formation of a substantial quantity of molecules at a low protein solution concentration. The results of dynamic rheological studies indicated that the 5% intact glycinin progressively formed the gel with mTGase treatment in a concentration-dependent manner, but maleylated-glycinin did not.

• Korean Journal of Poultry Science
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• v.17 no.3
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• pp.217-223
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• 1990

This study was undertaken to find out the changes of chemically modified egg albumen grl after heat treatment at $95^{\circ}C$ for 30 minutes or at $120^{\circ}C$ for 30 minutes. Acetylation and succinylation increased the hardness of egg albumen gel, it was rather higher at high heat treatment($120^{\circ}C$, 30min.) than at low heat treatment($95^{\circ}C$, 30min). The cohesiveness of egg albumen gel was improved remarkably by succinylation and maleylation at both low and high heat treatment. The lightness and yellowness of egg albumen gel were decreased by chemical modification. Initial heat denaturation temperature of egg albumen was increased by 11$^{\circ}C$ by acetylation, by $12.5^{\circ}C$ by maleylation and by ,$14.5^{\circ}C$ by succinylation.

• Preventive Nutrition and Food Science
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• v.2 no.1
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• pp.17-22
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• 1997

Casein was chemically modified with acetic, succinic, and maleic anhydride and changes in functional pro-perties were evaluated as affected by the degree of modification. Chemical modification resulted in casein with unique functional properties depending upon the type of anhydrid used and the degree of modification. It was possible to control heat coagulation, calcium precipitability, forming and emulsion capacity and stability. At pH 4.5 heat coagulation was 0% in the case 74.1% acetylated casein; on the contrary, succinylation and maleyation resulted in highly heat sensitive protein. Foaming properties were improved markedly by suc-cinylation and maleylation at pH 4.5. However, emulsifying properties were enhanced only by maleylation.

• Journal of Environmental Health Sciences
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• v.30 no.4
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• pp.314-319
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• 2004

Glycinin of more than $97\%$ purity was modified using maleic anhydride. Glycinin samples of $0\%,\;65\%,\;and\;95\%$ lysine residue modifications were used to determine the changes in turbidimetric characteristics of the protein due to maleylation. The solubility behavior of the protein as a function of pH was changed with maleylation. The isoelectric point of $65\%\;and\;95\%$ modified glycinin shifted to pH 4.0 and pH 3.5-4.0, respectively, as compared to pH 4.6 for native glycinin. Maleylated glycinins exhibited increased solubility at pH above 4.6. Turbidity of native glycinin decreased substantially by the addition of NaCl, but the stabilizing effect of NaCl decreased when the protein was chemically modified. The effect of NaCl on $65\%$ modified glycinin was intermediate between native glycinin and $95\%$ modified sample. Thermal aggregation of native glycinin was completed within 5 min of heating at $80^{\circ}C$. Maleylation contributed significantly to the thermostability of the protein at pH of 7.0 and 9.0, exhibiting little turbidity. Addition of NaCl suppressed thermal aggregation of native glycinin, but turbidity actually increased for the samples of $65\%\;and\;95\%$ modification.

• Clean Technology
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• v.10 no.4
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• pp.195-201
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• 2004

Cellulase was modified with copolymer with polyethylene(PE)/polypropylene(PP) oxide and maleic anhydride(MA) by maleylation reaction, and modified cellulase was applied to the reprocessing of old newsprint (ONP). Cellulase of modified cellulase enhanced the detachment of ink particles by fibrillation of fiber. The copolymer, which acted as the surfactant formed bubbles and removed the ink particles in the floatation process. Modified cellulase showed the same deinking ability without excess dosage compared with the conventional method. And, it improved the physical properties including tensile strength, brightness, and whiteness compared with the conventional deinking process. The bond between the ink and fiber got stronger as the storage time increased, and it became very difficult to remove the ink particle. But, modified cellulase increased the deinking ability by 41% compared with the conventional process at the experiment of the ONP for 1 year storage time. It removed the yellowing and increased the whiteness and brightness as well as tensile strength and internal bond strength.

• Applied Biological Chemistry
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• v.33 no.1
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• pp.52-61
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• 1990

Fish protein was acylated with acetic anhydride(AA), succinic anhydride(SA) and maleic anhydride(MA) in order to improve the functional properties of the protein. The surface hydrophobicity and functional properties of protein were measured to study the relationship between them. It was found that the extented acylation of nucleophilic groups such as amino and sulfhydryl groups of the amino acid residues of fish protein was higher than other groups when acylated with AA, and the degree of acylation was 89.5 % for amino groups and 72.2 % for sulfhydryl groups. The surface hydrophobicity of fish protein was decreased by succinylation and maleylation, whereas acetylation caused tittle change. The acylated fish protein concentrate(FPC) showed higher surface hydrophobicity than the acylated fish myofibrilla protein(FMP). Acylation with AA, SA and MA of fish protein resulted in a significant increase in protein solubility, emulsifier properties, foaming properties, water adsorption capacity and oil adsorption capacity. These properties of acylated FMP were more improved than those of acylated FPC. Decrease in protein hydrophobicity was highly correlated with increase in protein solubility, and emulsifier properties and foaming properties were largely dependent on the solubility as well as surface hydrophobicity. The water adsorption capacity of the protein was significantly affected by solubility. Surface hydrophobicity had greater influence on oil adsorption capacity, whereas it had tittle effect on water adsorption capacity.