• Applied Biological Chemistry
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• v.39 no.4
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• pp.282-286
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• 1996

To effectively utilize fish skin gelatin as a material for quality improvement in surimi gel from fish with a red muscle, conger eel skin gelatin was modified with succinic anhydride, and funtional properties such as emulsifying activity and emulsifying stability were determined. The degree of chemical modification incresed up to 0.3 g of succinic anhydride/g of gelatin, above this adding ratio a nearly constant value was reached. The maximum amount of modification was about 90%. The emulsifying activity and emulsifying stability of gelatin gradually increased up to 89.8% of succinylation extent, little changed above of succinylation extent. The other functional properties as solubility, water holding capacity, foam expansion and foam stability were improved following succinylation with 0.3 g of succinic anhydride/g of gelatin. Amino acid composition of succinylated gelatin was similar to that of unmodified gelatin. Heavy metal contents such as cadmium, lead, copper and zinc of succinylated gelatin were lower than those of unmodified gelatin.

• Journal of the East Asian Society of Dietary Life
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• v.6 no.3
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• pp.345-353
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• 1996

Addition of 0.5, 1.0 and 2.0g of succinic anhydride to 2g of sesame protein concentrates succinylated 44.9, 70.0and 83.1% of the available amino groups, respectively. Considerable amount of phytate were removed in all sesame protein concetrates and the highest reduction was obtained by addition of 2.0g of succinic anhydride. Among the minerals investigated, high amount of calcium and magnesium were presented in defatted sesame flour. In the case of calcium, magnesium and iron, the contents were decreased as the degree of succinylation was increased. Most amino acid content of sesame protein concentrates was not changed by succinylation but lysine was slightly decreased. Result of color measurement showed that the higher degree of succinylation, the higher values of L and B were founded.

• Macromolecular Research
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• v.16 no.1
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• pp.57-61
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• 2008

Chitosan is normally acylated and subsequently conjugated with drugs for biomedical applications. This study examined the relationship between the succinylation and gelation behaviors of glycol chitosan. Glycol chitosan was acylated with succinic anhydride under a wide variety of reaction conditions, such as different molar ratios of succinic anhydride to glucosamine, different methanol content in the reaction media, and different reaction temperatures. Among these reaction parameters, the methanol content in the solvent played an important role in determining the regioseletive succinylating site. N-succinylation and N-N cross-linking occurred regardless of the reaction conditions. However, O-succinylation was observed under specific conditions, i.e. a methanol content> 0.6 (v/v) and a reaction temperature> $25^{\circ}C$. O-succinylation accelerated the N-O cross-linking of glycol chitosan, and led to gelation. The N-succinylated glycol chitosans were water-soluble, whereas the N-and O-succinylated glycol chitosans fonned a gel. These physico-chemical structural differences in the succinylated glycol chitosans would definitely influence subsequent drug-conjugation reactions and consequently the drug loading and release kinetics.

• Korean journal of food and cookery science
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• v.7 no.3
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• pp.53-59
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• 1991

This study was carried out in order to investigate the change of protein functionalities such as foaming and emulsifying properties by succinylation of protein isolates. Succinylated and unsuccinylated munghean protein isolates were tested for finding out the effects of pH, heat treatment and sodium chloride concentration on the solubility, emulsion capacity, emulsion stability, foaming capacity, and foam stability. The results are summarized as follows: 1. Succinylation enhanced the solubility of MPI except at pH 4.5. When heated, succinylation greatly increased the solubility of succinylated MPI above $60^{\circ}C$. With the addition of NaCl, succinylation increased the solubility of MPI at acidic condition. 2. Emulsion capacity of succinylated MPI showed the lowest value at pH 7 and higher values at acidic and alkaine condition. when succinylated MPI was heated, emulsion capacity showed the highest at $80^{\circ}C$. With NaCl was added, emulsion capacity of succinylated MPI lincreased at pH 7, 9 or 11 decreased at pH 3 except addition of 1.0M NaCl. 3. Emulsion stability of MPI and succinylated MPI showed the highest at pH 4.5. Succinylation enhanced the emulsion stability of MPI at acidic condition. 4. The foaming capacity of MPI was increased at pH 3, 7 or 9 by succinylation. 5. When heated, foam stability of MPI and succinylated MPI showed the highest at pH 4.5 and at pH 11, respectively. When heated, both proteins showed the highest stability at $100^{\circ}C$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.12 no.3
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• pp.251-258
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• 1983

This experiment was carried out to investigate the capability of production of artificial milk for leaf protein concentrate (LPC). Chloroplastic protein and cytoplasmic protein were extracted from leaves of Dystaenia takeshimana Nakai and LPC was extracted from leaves of Italian ryegrass to increase the functional properties of LPC as a level of milk casein. One gram of chloroplastic protein and cytoplasmic protein and 1g of LPC were succinylated by addition of succinic anhydride 0.1, 0.25, and 1g respectively. Their functional properties were investigated in this experiment. The results obtained were summarized as follows: 1. The non-succinylated LPC showed a higher value in bulk density than the chloroplastic protein, the cytoplasmic protein and LPC succinylated by addition of succinic anhydride 0.1, 0.25, and 1g respectively. Nevertheless, succinylation had an enhancing effect as indicated by the rises as the degrees of succinylation was increased. 2. Although solubility of non-succinylated LPC was lower than that of milk casein, succinylation caused an effective increase in the solubility of the protein and LPC. 3. Water absorption and fat absorption of succinylated LPC were twice to eight times higher than those of milk casein. Fat absorption was not influenced to the extent by succinylation as the water absorption. Excessive succinylation resulted in the decrease of both water absorption and fat absorption. 4. Emulsifying activity and emulsion stability were increased in proportion to the succinylated degree of LPC. More than 10% increase in the amount of succinic anhydride resulted in an apparent increase in emulsifying activity and emulsion stability. Besides, the succinylated LPC showed more excellent functional properties in emulsifying activity and emulsion stability than milk.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.5
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• pp.573-579
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• 1992

The influence of succinylation on several functional properties of fungal protein (Aspergillus fumigatus) was investigated. Fungal protein was succinylated to 20.7 and 85.3% by addition of 2.5 and 10% succinic anhydride, respectively. Succinylated fungal protein decreased the absorbance at 260nm, nucleic acid and carbohydrate, but increased the proteinous nitrogen and protein extraction in fungal protein. Succinylation had an enhancing effect on the functional properties as much as the degree of it was increased. Oil retention of succinylated fungal protein was higher about from two to five times than those of milk casein. Nitrogen solubility of succinylated fungal protein was increased to 32 and 51% than that of milk casein and soy flour. Emulsifying activity and stability were increased in proportion to the succinylated degree of fungal protein. As the result of succinylation increase more than 80%, emulsifying activity increased about 8.4 times. In conclusion, succinylated fungal protein improved functional properties, compared with nonsuccinylated fungal protein, milk casein and soy flour.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.4 no.4
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• pp.407-410
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• 1991

The relationship between the possible structural change due to chemical modifications and functionality changes was studied in pigskin collagen. Amino groups in collagen were modified by succinylation and reductive alkylation. Carboxyl groups were modified using carbodiimide. Thermal denaturation temperature of collagen increased remarkably by carboxyl groups modification whereas decreased by succinylation and reductive alkylation. Emulsifying capacity was improved by reductive alkylation and carboxyl groups modification while emulsion stability was improved by succinylation. Chemical modifications increased solubility whereas decreased the foaming capacity of collagen. Viscosity of collagen at various pH varied with methods of modification.

• Journal of Applied Biological Chemistry
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• v.42 no.4
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• pp.180-185
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• 1999

Protein concentrate was produced and succinylated from rice bran to assess and improve its functional properties for the purpose of expanding the uses of rice bran proteins. The most effective solvent for the extraction of rice bran proteins was 20% aqueous ethanol at pH 9. The protein content of rice bran protein concentrate produced was 70.0% and the total protein yield was 64.3%. The extent of succinylation of free amino groups in the modified products was 72.8%. Though the modified protein products showed good functional properties including solubility, emulsion properties, and oil absorption capacity, it did not form gel. Succinylation improved solubility and emulsion and gelling properties. These improvements in functionality will enhance the value of rice bran proteins, thus enabling them to be more competitive with other food proteins.

• Korean Journal of Food Science and Technology
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• v.16 no.3
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• pp.353-357
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• 1984

The myofibril prepared from PSE (pale, soft, exudative) porcine meat was modified by reacting with succinic anhydride and the chemical and functional properties of modified myofibrils were investigated. $No\;Ca^{2+}-and\;Mg^{2+}-ATPase$ activity were observed irrespective of the degree of succinylation. Isoelectric point of the succinylated myofibril changed to around pH 3 from the pH 5 of unmodified myofibril. Salt soluble property was not affected by changing the salt concentration. The modified myofibril in aqueous solution did not coagulate during heating at $98^{\circ}C$ for 10 min. Water absorption ability was not improved but emulsion capacity was improved a little by succinylation.