• Korean Journal of Fisheries and Aquatic Sciences
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• v.11 no.2
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• pp.85-90
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• 1978

In present study, the effect of various factors including the solvent concentration, extraction time, extraction temperature and the ratio of sample vs extraction solvent(w/v) upon the extractability of the NaOH soluble proteins of marine algae were investigated. Seven species of sun-dried algae, the major ones in consumption as food, namely Porphyra suborbiculata, Undaria pinnatifida(natural and cultivated), Sargassum fulvellum, Sargassum kjellmanianum, Ulva pertusa, Enteromorpha linza and Codium coarctatum were used for the extraction of the NaOH soluble protein. The frozen and masceratd samples were prepared by the same mettled described in previous paper(Lee, 1977). In case of the TCA insoluble protein, all samples reached maxima at 0.025M NaOH solution while the 0.05M for extractable total nitrogen. Variation of the ratio of sample vs solvent gave slight effect upon the extractability, 100 ml solvent added to 1 g dried sample was effective. The effect of extraction time on the extractability differed from species. The extractabilty of Enteromorpha linza, Ulva pertusa and Codium coarctatum reached maxima within 1 hour extraction and 2 hours for the cultivated Undaria pinnatifida while 3 flours for the natural Undaria pinnatifida, Sargassum fulvellum, Sargassum kjellmanianum and Porphyra suborbiculata. The most effective extraction temperature was $60^{\circ}C$ for all samples.

• Korean Journal of Food Science and Technology
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• v.10 no.2
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• pp.162-172
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• 1978

We have studied to develop a process for the preparation of protein isolates free of isothiocyanate and oxazolidine-thione when defatted meal was extrracted with a cold alkaline solution at pH11.0. The rapeseed protein isolates were separated at $0^{\circ}C$ using 1% sodium algiante of 500 cps as a precipitation aid, also. The proteins had original colors, namely, a grey curd at pH 6.7, a light cream at pH 5.6 and a yellow cream at pH 5.0, The purity and the color was improved by washing with water and freez-drying with acetone, not at room temperature. A countercurrent procedure was a prerequisite for a continuous large scale production of protein isolates.

• Applied Biological Chemistry
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• v.21 no.2
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• pp.109-111
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• 1978

This study was undertaken in order to observe the differences of the changes in the water-holding capacity (WHC), extractability of proteins (EP) and pH value of ovine muscle during storage. WHC decreased gradually after slaughter, reached to minimum at about 2-4hr after death as well as that of pH value and then these were recovered along with the progress of the storage. The same tendency was observed in EP but the degree of the changes in pH value up to 6hr after slaughter was more rapid this that of WHC and EP. After the fourth day, the rate of recovery in WHC, EP and pH value in ovine muscle during storage showed similar pattern.

• Korean Journal of Food Science and Technology
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• v.39 no.4
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• pp.458-463
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• 2007

The ethanolic extracts of 83 kinds of agricultural products, including cereals, vegetables, and Chinese herbs, were tested for their inhibitory activities on protein cross-linking using the $[^{14}C]$-N-formyl-lysine incorporation method. Most of the extracts inhibited, but some extracts accelerated, the cross-linking of protein. Of those items with relatively high activities, we selected 20 samples to test for activity against AGE fonnation using the fluorophotometric method. The ethanol extract of buckwheat that was genninated for 1 day (GB-01) was detennined to have the highest activity with both methods. The ethanol extract of GB-01 was further fractionated by organic solvents, including chloroform, ethyl acetate, butanol, and water, in order of increasing polarity. The fraction that was extracted with ethyl acetate presented the highest protein glycation inhibitory activity (95.2% inhibition at the 100 ug/mL addition level). Polyphenol content analysis by HPLC showed that the amounts of rutin and quercetin were increased with the separation procedures. Finally, there was a significant relationship between activity and polyphenol content in the partially purified samples (p<0.05).

• Korean Journal of Food Science and Technology
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• v.22 no.7
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• pp.780-785
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• 1990

In order to establish the effective extraction and purification process of rapeseed protein, the extraction solvents were compared with one another ; and the residues of glucosinolate and phytate and the extraction yield of protein, which had been extracted by 1% sodium hexa mata-phosphate(SHMP) and purified through isoelectric precipitation, acid-washing and UF concentration, were investigated. As for the condition for extraction of rapeseed proteins, the solvent of 1% SHMP(pH 8.0) turned out the most appropriate ; so far as the purification process for the elimination of glucosinolate and phytate was concerned, the acid-washing twice or the process of the acid-washing once and UF concentration was considered the most effective. The yield and content of rapeseed protein were 37.1% and 75.3% respectively in the case of the acid-washing twice, 42.1% and 72.4% respectively in the case of the acid-washing once and UF concentraction, Consequently, with the elimination effects of glucosinolate and phytate put into consideration, the process of isoelectric precipitation, acid-washing once(pH 3.5), neutralizing(pH 7.5), UF concentration and then freeze drying proved the most effective purification process.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.6
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• pp.551-558
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• 1991

We investigated the physicochemical and functinal properties of rapeseed(Brassica napus var. Youngsan) protein prepared by combining various soluvent and purification procedures, such as ultrafiltration (UF) concentration and acid-washin. The lightness value(YCIE) of each protein was greadully improved and its hydrophobicity increased by the degree of purification. The analysis of each protein by sodium dodecyl sulfate-plyacrylamide gel electrophoresis (SDS-PAGE) had nine bands revealed without difference, the considerable portion of which were of $1.96~1.59{\times}10^4$ dalton molecular weight. The content of amino acid increased a little more in the other processed proteins than in the control, and decreased considerably in the proteins extracted by the mixed solvent of 1% sodium hexametaphosphate(SHMP) and 0.25M ethlene diamine tetraacetic acid (EDTA). The better proteins were purified, the lower the kinematic viscosities were in their values. The water absorption and foaming properties were scarcely different according to the processes. The oil absorption and the emulsion activity index normally increased according to the degree of purification. The properties of heat coagulation revealed high values only in the proteins processed by EDTA while they showed considerably low values the other proteins.

• Journal of Sericultural and Entomological Science
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• v.43 no.2
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• pp.109-115
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• 2001

Silk sericin protein was extracted by treatment with enzyme or NaOH solution from raw silk and culled-cocoon shell. The extracted sericin was characterized and examined the functional properties as well as subjective properties for its use as a soap and a body cleaner. The optimum extraction conditions on specimen are NaOH (0.02 wt.%) or enzyme, Flavourzyme 3% under N2 gas. Molecular weights of sericin was decreased by treatment with enzyme, Actinase, from 10,000-30,000 to 2,700-4,200. Sericin showed important bioactive properties, for instance, lowering effect on blood glucose and alcohol. Subjective test of sericin soap and body cleaner showed superior in washability, foamability, and skin hydration, etc., to commercial soap and body cleaner. Therefore, it is thought that silk sericin can be expected as the source of bioactive and skin-compatible materials.

• Journal of Life Science
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• v.29 no.8
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• pp.854-860
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• 2019

This study investigated the optimum pH conditions for efficient extraction of protein from defatted Tenebrio molitor (TM) larvae. We examined the anti-inflammatory effect of protein derived from defatted TM larvae obtained by an alkaline extraction method. Six extraction pH values (7, 8, 9, 10, 11, and 12) and three precipitation pH values (2, 4, and 6) were used. The protein content, browning degree, and recovery yield of the protein obtained under each pH condition were determined. For efficient extraction of protein from defatted TM larvae, a combination of an extraction pH of 9 and precipitation pH of 4 resulted in a 32.4% recovery yield based on the extraction value and degree of browning. To determine whether the protein ameliorated inflammation by inhibition of macrophage activation by lipopolysaccharides (LPS), we measured nitric oxide (NO), cyclooxygenase-2 (COX-2), and inducible nitric oxide synthase (iNOS) expression in LPS-stimulated raw 264.7 macrophage cells. The protein markedly inhibited the production of NO without cytotoxicity and reduced the expression level of COX-2 and iNOS protein through the regulation of mitogen-activated protein kinases (MAPKs) and nuclear factor kappa B ($NF-{\kappa}B$) signaling. These results suggested that protein derived from TM larvae could have potential applications in anti-inflammatory therapeutic agents and protein supplements.

• Proceedings of the Korean Nutrition Society Conference
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• 2001.05a
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• pp.231.2-231
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• 2001

• Food Science of Animal Resources
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• v.24 no.1
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• pp.80-85
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• 2004

This study was carried out to separate immunoglobulin G(IgG) from colostrum using reverse micellar extraction of cationic surfactant and to suggest suitable extraction conditions. The reconstituted colostrum powder was solubilized into a reverse micellar phase containing CDAB(cetyldimethylethyl ammonium bromide) by mixing equal volume of the aqueous and organic phase with constant stirring. The solubilization of proteins from the aqueous to the organic phase was manipulated by pH and ionic strength of the aqueous phase and concentration of surfactant in the organic phase. Based on the SDS-PAGE and densitometry, about more than 90% of initial IgG was remained in the aqueous phase after reverse micellar extraction. Although the aqueous phase contained lactoferrin and bovine serum albumin as minor components, about 93% of the total protein was IgG. The efficient extraction was achieved by the reaction of sodium phosphate buffer(pH 8) containing 50 mM KCl and organic phase containing 100 mM CDAB. The separation of IgG using reverse micellar extraction was simple, highly efficient and easy to be scaled up.