• Journal of Microbiology and Biotechnology
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• v.1 no.1
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• pp.54-62
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• 1991

Cyclodextrin glucanotransferase(CGTase) derived from Bacillus macerans was immobilized by (1) covalent linkage on chitosan and chitin with glutaraldehyde, (2) adsorption on DEAE-cellulose and Amberite IRA 900 after succinylation, and (3) entrapment on alginate and polyacrylamide by cross linking. Adsorption on Amberite IRA 900 and covalent linking on chitosan were identified to be the most suitable immobilization methods considering the yield of activity and stability of immobilized CGTase. The enzymatic properties of immobilized CGTase were investigated and compared with those of the soluble CGTase. Thermal stability of CGTase immobilized on chitosan was increased from 50 to $55^{\circ}C$, and the optimum temperature of CGTase immobilized on Amberite IRA 900 was shifted from 55 to $50^{\circ}C$. The effect of molecular size of soluble starch (substrate) on immobilized CGTase investigated using partially liquefied substrates with different dextrose equivalent(DE). Cyclodextrin(CD) conversion yield augmented according to the increase of DE level for immobilized CGTase on Amberite IRA 900. CD conversion yield of partially cyclized starch with soluble CGTase was higher compared with liquefied one with ${\alpha}-amylase$.

• Asian-Australasian Journal of Animal Sciences
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• v.13 no.12
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• pp.1770-1774
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• 2000

Extended use of porcine blood in food ingredients depends on the decolorization of red blood cell concentrates and the modification of its functional properties. The purpose of this study is to compare the relative effect of cation ion exchanger for decolorization of porcine red blood globin. The globin extract is freeze-dried for determination of various functional properties, such as solubility, emulsion capability and foaming ability. Since the isoelectric point of blood globin is located at pH 6.8, which is the neutral pH ranges (6-8), so its functionalities are inferior around these pHs. This weakness has been the main reason, which limit the extended use of blood globin in food industry. Acetylation and succinylation of blood globin can be an alternative way to improve its functionalities. These results may provide new information to understand the decolorization mode by cation ion exchanger for the blood globin. With chemical, the functionalities of blood globin could be obviously improved. The above findings could enable food industry to extend the use of blood globin as a food ingredient.

• The Korean Journal of Food And Nutrition
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• v.2 no.1
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• pp.18-26
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• 1989

The objective of this study was to improved the limited functional characteristics of mungbean whole globulin. The mungbean whole globulin was acylated with succinic and acetic anhydride, and the functional properties of acylated protein were investigated, The results obtained ware as follows. 1. The UV-absorption spectra of acylated whole globulins with that of the succinylated 74% whole globulin as large blue shift of the absorption maximum and minimum wavelength from 275 nm to 269 nm, respectively. 2. The mobility of acylated whole globulin were increased on PAGE pattern, and degree of mobility was particularly remarkable in case of succinylation, 3. The water absorption capacity of whole globulin was increased by acylation. The most increased rate of whole globulin was 174,02% from succinylated 74%. The oil absorption capacity of whole globulin was increased by acylation The most increased rate of whole globulin was 165.41% from acetylated 81.77%. 4. The bulk density of whole globulin was decreased by acylation. and the greater the extent of acylation, the smaller the bulk density. 5. The foaming capacity and stability of whole globulin was increased by acylation, and remarkably high in 74% succinylated whole globulin. In contrast, however, the foaming capacity and stability of native and acylated whole globulin were decreased by heat treatment.

• Korean Journal of Environmental Agriculture
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• v.13 no.3
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• pp.262-270
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• 1994

The established methods in the residue analysis of endosulfan require an extensive sample clean-up prior to quantification by relatively complex equipment. A radioimmunoassay(RIA) provides a simple procedure with theoretically higher sensitivity and specificity necessitating only a minimum of sample clean-up. Endosulfan-specific antibodies were developed in rabbits by using a bovine serum albumin(BSA) conjugate wherein the alcohol form of endosulfan was multiply bound to the protein via succinylation. Produced antibodies showed the high titers to endosulfan-BSA(1 : 32,000). An RIA method was developed in water and carp by using $^{14}C-labeled$ endosulfan as a tracer. The lowest detection amount of endosulfan was 1 ng in the liver, kidneys, gut and water samples, and 3 ng in the whole body sample of carp without any clean-up, corresponding to 0.1 ppb of endosulfan.

• Korean journal of food and cookery science
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• v.3 no.2
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• pp.1-8
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• 1987

Eighty eight percent of succinylation at $\varepsilon$-amino group of lysine was obtained from silkworm larvae protein concentrate and it resulted in increased bulk density and fat absorption, improved flavor and color, increased solubility over fivefold. Both emulsifying activity and emulsion stability of the succinylated protein were improved by 30% and emulsifying capacity was enhanced by 4%. Foaming capacity of the succinylated Protein concentrate was improved by 30% and foaming stability improved fivefold. The viscosity of succinylated silkworm larvae protein concentrate was increased at all concentrations and reached the highest at 4~5% of concentations. Acetylation of silkworm larvae protein concentrate caused negligible change in the functional properties studied. Therefore, high emulsification properties of silkworm larvae protein concentrate would be a good protein source for the emulsified foods.

• Macromolecular Research
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• v.14 no.5
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• pp.573-578
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• 2006

Three different, polymer-platinum conjugates (hydrogels, microparticles, and nanoparticles) were synthesized by complexation of cis-dichlorodiammineplatinum(II) (cisplatin) with partially succinylated glycol chitbsan (PSGC). Succinic anhydride was used as a linker to introduce cisplatin to glycol chitosan (GC). Succinylation of GC was investigated systematically as a function of the molar ratio of succinic anhydride to glucosamine, the methanol content in the reaction media, and the reaction temperature. By controlling the reaction conditions, water-soluble, partially water-soluble, and hydrogel-forming PSGCs were synthesized, and then conjugated with cisplatin. The complexation of cisplatin with water-soluble PSGC via a ligand exchange reaction of platinum from chloride to the carboxylates induced the formation of nano-sized aggregates in aqueous media. The hydrodynamic diameters of PSGC/cisplatin complex nano-aggregates, as determined by light scattering, were 180-300 nm and the critical aggregation concentrations (CACs), as determined by a fluorescence technique using pyrene as a probe, were $20-30{\mu}g/mL$. The conjugation of cisplatin with partially water-soluble PSGC, i.e., borderline between water-soluble and water-insoluble PSGC, produced micro-sized particles $<500{\mu}m$. Cisplatin-complexed PSGC hydrogels were prepared from water-insoluble PSGCs. All of the cisplatin-incorporated, polymer matrices released platinum in a sustained manner without any significant initial burst, suggesting that they may all be useful as slow release systems for cisplatin. The release rate of platinum increased with the morphology changes from hydrogel through microparticle to nanoparticle systems.

• 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.

• Korean journal of food and cookery science
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• v.3 no.2
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• pp.9-16
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• 1987

This study was designed to determine the amino acid composition and to investigate microstructure by scanning electron micrographs of silkworm larvae protein and modified silkworm larvae protein concentrate. The results were as follows: 1, The protein contents of soybean and silkworm larvae protein concentrate were 70.3% and 84.1%, respectively. 2. In general, the essential amino acid content of silkworm larvae protein concentrate were higher than soybean protein concentrate as well as FAO provisional scoring pattern. Silkworm larvae protein concentrate was especially high in lysine and methionine indicating that it could be a good supplemental source for cereals and beans. Succinylation and acetylation resulted in no difference in most amino acid content. 3. The scanning electron microscopic observations revealed that silkworm larvae protein concentrate had smooth surface topography while defatted silkworm larvae flour showed different shapes and sizes with relatively rough surfaces. Acylated silkworm larvae protein concentrate exhibited less cellularity and denser than protein concentrate. However, succinylated silkworm larvae protein concentrate showed especially good texture indicating that it could increase the functional properties of silkworm larvae protein concentrate.

• Applied Biological Chemistry
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• v.39 no.5
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• pp.361-367
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• 1996

As a part of investigation for quality improvement of surimi gel from fish with a red muscle by addition of emulsion curd, we investigated the processing conditions of emulsion curd contained succinylated gelatin from conger eel skin as an emulsifier and emulsion curd-added surimi gel. Activity and stability of emulsion curd on standing at room temperature, chilled temperature and vibration were remarkably improved by the addition of 15 tunes of soybean oil and 5 times of water to succinylated gelatin from conger eel skin. The proximate composition of the emulsion curd was moisture 18%, protein 5%, lipid 76% and ash 0.5% and its appearance was white. Peroxide value and fatty acid composition of emulsion curd contained succinylated gelatin as an emulsifier were similar to these of soybean oil. By the addition of 6% of emulsion curd to mackerel surimi, gel strength, appearance and texture of the resulting surimi gel were improved, while its peroxide value and brown pigment revealed minor change. From the results of volatile basic nitrogen, viable cell counts and histamine content, the emulsion curd-added mackerel surimi gel can be safe In the sense of food sanitation.