• Food Science of Animal Resources
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• v.23 no.1
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• pp.63-69
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• 2003

This experiment was carried out to study changes in solubility and emulsifying properties of whey protein. Whey protein hydrolysates were obtained from tryptic hydrolysis of whey protein concentrate at pH 8.0 and 37$^{\circ}C$ for 6 hours. Emulsifying activity of whey protein hydrolysate was highest at 4 hours of hydroysis and at 5.50% of DH. During hydrolysis of whey protein concentrate with trypsin, ${\alpha}$-lactalbumin was not easily broken down. But ${\beta}$-lactoglobulin was hydrolysed rapidly from the early stage of hydrolysis, producing several low molecular weight peptides, which have to participate in increasing emusifying activity. The solulbility of hydyolysates tended to increase depending on hydrolysis time; however, there was a gradual decrease after 5 hours. The hydrolysate had a minimum solubility near the isoelectric point range (pH 4∼5). The more hydrolysed the whey protein concentrates, the more soluble they are near the pl. They aye also more soluble above pH 6. Emulsifying activity of hydrolysates showed similar results to solubility. Creaming stability gradually increased when hydrolysis increased, increasing rapidly above pH 8 after 4 hours of hydrolysis.

• Journal of Plant Biology
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• v.37 no.2
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• pp.151-158
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• 1994

Aleurone layers of normal and vp1 mutant maize kernels were extracted and centrifuged at 100,000g to yield a cytosol fraction. Binding of [3H]ABA cis, trans (＋)ABA to a soluble macromolecular components present in the cytosol was demonstrated by Sephadex chromatography and non-denaturing PAGE. The binding component was of high molecular weight and seems to be an aggregate of proteins. A rapid DEAE-cellulose filter method for assaying bound [3H]ABA to a soluble protein was adapted. Binding assays were performed with cytosol that had been preheated or incubated with several enzymes, indicating that heat and protease treatments disrupted the binding. This suggested that binding occurred to proteins. Some properties of the ABA binding proteins were described. The [3H]ABA binding were reduced dramatically when unlabeled ABA was added as a competitor, suggesting a specific binding of [3H]ABA. Gel filtration profiles and autoradiogram of [3H]ABA binding showed no difference in the binding components of Vp1 and vp1/vp1 mutant cytosol, indicating that Vp1 protein is not a sole ABA binding protein.

• Journal of Plant Biology
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• v.9 no.1_2
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• pp.1-6
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• 1966

Using the Chlorella cells which had been uniformly labeled with $^{32}P$, the distribution of phosphorus in various fractions of cell material was investigated. Uniformly $^{32}P$-labeled Chlorella cells were further grown in a P-free medium, and some protions of the cells were taken out at intervals during the culture, and subjected to analyze the contents of $^{32}P$ in various fractins of the cell constituents. 2. Analysis of the $^{32}P$-labeled Chlorella cells showed that the highest in P-content was the fraction of RNA followed by those of lipid, RNA-polyphosphate complex, acid-insoluble polyphosphate, acid-soluble polyphosphate, DNA and protein. 3. During the culture of $^{32}P$-labeled Chlorella cells in a P-free medium, amounts of phosphate in DNA, protein and lipid fractions increased, while the P-contents in the fraction of RNA-polyphosphate complex decreased as well as those of acid-insoluble polyphosphate and acid-soluble polyphosphate fractions. 4. It was inferred that phosphorus used in the syntheses of DNA and protein was taken from polyphosphates of the cells, and RNA-polyphosphate complex would play an important role as a phosphate pool.

• Korean Journal of Pharmacognosy
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• v.45 no.3
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• pp.262-267
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• 2014

Royal jelly composes of many components, especially protein. Protein is a major factor which cause allergy. We focused on water soluble royal jelly (WSRJ) that was removed allergy - inducing protein. 10-hyroxy-2-decenoic acid content of WSRJ is 2.42 g/100 g, which is double compared to that of lypophilized RJ. To further access WSRJ as a cosmetic ingredient and potential external treatment for topical use, we investigated its ability to inhibit tyrosinase activity and melanin biosynthesis on melanogenesis in B16F1 melanoma cells. We found that WSRJ increased the cell viability in B16F1 melanoma cell and WSRJ (1~10 mg/ml) inhibited melanin synthesis in with 10 nM ${\alpha}$-melanocyte-stimulating hormone (${\alpha}$-MSH) for 48 h. WSRJ inhibited direct tyrosinase activity, which decreased melanin synthesis in ${\alpha}$-MSH stimulated B16F1 melanoma cells. Thease findings suggest that WSRJ induces the down regulation of melanogenesis by inhibiting tyrosinase activation.

• Korean Journal of Food Science and Technology
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• v.20 no.1
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• pp.34-39
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• 1988

The possibility of using sodium dodecylsulfate-polyacrylamide gel electrophoresis was studied to detect specific proteins and their content in meat products such as beef, pork, fish, soybean, fish paste, ham and fish sausage. Many complicated bands were observed in the total protein fractions of the tested samples. The number of protein bands in the low salt-soluble protein fractions was considerably lesser and showed more specific bands in comparison with total protein fractions. Actone-insoluble fractions of non-meat proteins showed different patterns from meat proteins. A heating procedure seemed to be a cause for the diminished number and quantity of resolved protein bands in sausages. The results suggest that the discgel electrophoresis can be used to detect specific proteins and their content in protein foods, if a selective extraction method is emplyed.

• BMB Reports
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• v.33 no.3
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• pp.195-201
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• 2000

A human gene has been reported that may encode the enzyme acetohydroxyacid synthase. Previously this enzyme was thought to be absent from animals although it is present in plants and many microorganisms. In plants, this enzyme is the target of a number of commercial herbicides and the use of these compounds may need to be reassessed if the human enzyme exists and proves to be susceptible to inhibition. Here we report the construction of several plasmid vectors containing the cDNA sequence for this protein, and their expression in Escherichia coli. High levels of expression were observed, but most of the protein proved to be insoluble. The small amounts of soluble protein contained little or no acetohydroxyacid synthase activity. Attempts to refold the insoluble protein were successful insofar as the protein became soluble. However, the refolded protein did not gain any acetohydroxyacid synthase activity. In vivo complementation tests of an E. coli mutant produced no evidence that the protein is active. Incorrect folding, or the lack of another subunit, may explain the data but we favor the interpretation that this gene does not encode an acetohydroxyacid synthase.

• Journal of Ginseng Research
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• v.15 no.2
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• pp.124-130
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• 1991

This study was conducted to obtain basic information about the transformation of ginseng tissue, identification of opine compound and protein, and saponin production from ginseng callus transformed with Ti-plasmic of AW$.$obacterium tumefaiens C58. Ginseng crown gall callus induced by pTiC58 could be continuously cultured on the Phytohormone-free medium. The transformation was reconfirmed by the detection and identification of opine compound, from the gall callus. The transformed ginseng callus contained higher amounts of protein than normal callus and the protein pattern of transformed callus was quite different from that of normal callus. The xylose which is not detected in the normal callus and ginseng root was identified in gall callus. The saponin contents of gall callus of ginseng were three times higher than that of normal callus, and ginsenoside composition of the transformed callus was similar to that of the cultivated ginseng root, but quite different from that of normal callus.

• Korean Journal of Medicinal Crop Science
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• v.17 no.4
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• pp.293-300
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• 2009

This study was carried out to investigate the effect of Cinnamomum camphora on melanogenesis. The MeOH extract of Cinnamomum camphora inhibited mushroom tyrosinase activity in dose-dependent manner. Moreover, it significantly suppressed the melanin production in melan-a cells at the concentration of $100{\mu}/m{\ell}$. The MeOH extract was partitioned with ethyl acetate, n-butanol and water. Among them, the BuOH soluble fraction exhibited significant inhibitory effect on mushroom tyrosinase. In addition, the BuOH soluble fraction reduced the melanin production in melan-a cells. But, the BuOH soluble fraction had less inhibition effects on melan-a cell originated tyrosinase. So, it was performed western blotting for melanogenic proteins (tyrosinase, tyrosinase-related protein (TRP-2)) using melan-a cells. The BuOH soluble fraction inhibited the protein expression of tyrosinase at the concentration of $100{\mu}/m{\ell}$. The results suggested that the BuOH soluble fraction of C. camphora might be a potent inhibitor of melanin biosynthesis in melan-a cells.

• Asian-Australasian Journal of Animal Sciences
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• v.23 no.10
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• pp.1386-1398
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• 2010

Soybean contains a high concentration of carbohydrates that consist mainly of non-starch polysaccharides (NSP) and oligosaccharides. The NSP can be divided into insoluble NSP (mainly cellulose) and soluble NSP (composed mainly of pectic polymers, which are partially soluble in water). Monogastric animals do not have the enzymes to hydrolyze these carbohydrates, and thus their digestion occurs by means of bacterial fermentation. The fermentation of soybean carbohydrates produces short chain fatty acids that can be used as an energy source by animals. The utilization efficiency of the carbohydrates is related to the chemical structure, the level of inclusion in the diet, species and age of the animal. In poultry, soluble NSP can increase digesta viscosity, reduce the digestibility of nutrients and depress growth performance. In growing pigs, these effects, in particular the effect on gut viscosity, are often not so obvious. However, in weaning piglets, it is reported that soy oligosaccharides and soluble NSP can cause detrimental effects on intestinal health. In monogastrics, consideration must be given to the anti-nutritive effect of the NSP on nutrient digestion and absorption on one hand, as well as the potential benefits or detriments of intestinal fermentation products to the host. This mirrors the needs for i) increasing efficiency of utilization of fibrous materials in monogastrics, and ii) the maintenance and improvement of animal health in antibiotic-free production systems, on the other hand. For example, ethanol/water extraction removes the low molecular weight carbohydrate fractions, such as the oligosaccharides and part of the soluble pectins, leaving behind the insoluble fraction of the NSP, which is devoid of anti-nutritive activities. The resultant product is a high quality soy protein concentrate. This paper presents the composition and chemical structures of carbohydrates present in soybeans and discusses their nutritive and anti-nutritive effects on digestion and absorption of nutrients in pigs and poultry.

• Korean Journal of Agricultural Science
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• v.8 no.2
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• pp.231-237
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• 1981

In order to obtain the basical data for utilization of protein in hazel nut, protein was extracted from defatted hazel nut meal with salt solutions and alkaline solutions, and precipitated by adjusting pH of extract to 5.5 or addition of organic solvents. Amino acid composition of the isolated protein and defatted hazel nut meal were analyzed, protein isolates were identified by polyacrylamide gel electrophoresis. The results summarized were as follows. 1. Defatted hazel nut showed highly nutritional value as the content of 'protein was 53.6%. 2. Extractabilities of salt-soluble protein treated with 2.5M $MgCl_2$, and 1M NaCl(pH 11.0) were 53.0%, 31.5%, respectively 3. Protein in hazel nut were contained 53% of salt-soluble globulin, 14% of water-soluble albumin, 29.5% of glutelin based on solubility. 4. At pH 5.5, 85% of the extracted protein was precipitated, and about 90% of the extracted protein was separated by addition of organic solvents such as acetone and ethanol at 60-70% concentration. 5. Proteins extracted from defatted hazel nut with water and 0.027N NaOH showed 3 and 6 hands by polyacrylamide gel electrophoresis, respectively. 6. Amino acids of defatted hazel nut and protein isolate were chiefly composed of glutamic acid, arginine and aspartic acid.