• Korean Journal of Fisheries and Aquatic Sciences
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• v.10 no.4
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• pp.189-197
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• 1977

In present study, the effects of various factors including the solvent concentration, extraction time and temperature, the ratio of sample vs extraction solvent, (w/v) and pH upon the extractability of the NaCl and alcohol soluble proteins of marine algae were investigated. Eight species of fresh algae, the major ones in consumption as food, namely Porphyra suborbiculata, Undarie pinnatifida, Hizikia fusiforme, Sargassum, fulvellum, Enteromorpha linza, Sargassum kjellmanianum, Codium coarctatum, and Ulva pertusa were used for the extraction of NaCl soluble protein and dried materials of four species, Perphyra suborbiculata, Undaria pinnatifida, Enteromorpha linza and Sargassum fulvellum were used for the extraction of alcohol soluble protein. The frozen and mascerated samples were prepared by the same method described in previous paper (Ryu, 1977). And the dried materials were moistened with alcohol solution before freezing. The effect of solvent concentration on the extractability of NaCl soluble protein differed from species. The extractability of Undaria Pinnatifide, Hizikia fusiforme, Perphyra suborbiculata, Enteromorpha linza, and Ulva pertusa reached maxima at 0.25M NaCl solution while the 1.0M for Sargassum fulvellum, Saygassum kjellmanianum and Codium coarctatum. In case of alcohol soluble proteins, it was shown at $20\%$ ethanol solution for Porphyra suborbiculata, Undaria pinnatifida, Enteromorpha linza, and Sargassum fulvellum. Variation of the ratio of sample vs solvent gave slight effect upon the extractability, but the ratio of 1:30(w/v) seemed most efficient for the extraction of NaCl soluble proteins and 100 ml solvent added to 1 g dried sample was effective in case of alcohol soluble proteins. Extraction time has a minimal effect upon the extraction of alcohol soluble protein, and approximately 21 to $43\%$ of algal protein was extracted within 1 hour. But in case of NaCl soluble protein extraction, the effect of time revealed differently from species to species resulting in that the extraction for 1 hour gave a maximum extractability in Ulva pertusa and Enteromorpha linza, 2 hours in Porphyra suborbiculata, Codium coarctatum and 3 hours in Undaria pinnatifica, Hizikia susiforme, Sargassum fulvellum and Sargassum kjellmanianum. When the NaCl soluble protein of Undaria pinnatifida and Enteromopha linza was extracted at various temperature, the most effective extraction temperature was $40^{\circ}C$ while the temperature was $50^{\circ}C$ for Undaria pinnatifida and $60^{\circ}C$ for Hixikia fusiforme, Sargassum fulvellum, Sargassum kjellmanianum and Codium coarctatum. Bus in case of alcohol soluble extraction, the optimum temperature was $30^{\circ}C$ for Enteromorpha linza and $40^{\circ}C$ for Undaria pinnatifida, Sargassum fulvellum and Porphyra suborbiculata. In the effect of pH on extractability, the maximum extractability of NaCl soluble proteins was obtained at pH 7to 8 and pH 8 to 9 for alcohol soluble protein.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.2
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• pp.126-132
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• 1991

Nutritional factors affecting the urinary excretion of acid-soluble peptides(ASP) in rats were studied using protein-free diet, gluten diet, casein diet, and gluten supplemented with lysine and threonine(GLT) diet. The content of urinary ASP was lowest in protein-free diet group among the four kinds of diets above. But the amino acid pattern of urinary ASP in the four dietary groups were similar each other, suggesting that urinary ASP is mainly from endogenous origin under these nutritional conditions. The efficiency of dietary protein utilization was significantly lower in gluten diet than that of casein diet or GLT diet. Those findings suggest that the rate of urinary excretion of ASP-form amino acids can be employed as an index of protein metabolism, particularly as a simple index in the assessing the status of protein nutrition.

• Applied Biological Chemistry
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• v.36 no.2
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• pp.121-126
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• 1993

To extract insoluble proteins of sesame meal residue by using microorganism, the sesame meal residue was treated with crude enzyme solution from Bacillus sp. CW-1121. It was found that the solubility reached to maximum at pH 7.5, $45^{\circ}C$. Under optimum condition, the nitrogen solubility with the enzyme solution from Bacillus sp. CW-1121 reached to 60% in 2 hours. Nitrogen solubility of protein from sesame meal showed minimum value at pH 4.5 and significantly increased above pH 6.0. When the protein from sesame meal extracted with Bacillus sp. CW-1121 was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis, water soluble protein was showed 4 bands and salt soluble protein was showed 2 bands. The amino acid composition of water soluble protein, salt soluble protein and free amino acid indicated relatively high contents of serine (17.24 mg/g), glutamic acid (10.77 mg/g) and glutamic acid (6.55 mg/g). Specially, the contents of essential amino acids were high.

• Journal of Life Science
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• v.25 no.2
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• pp.130-135
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• 2015

When the alginate lyase gene (aly) from Pseudoalteromonas elyakovii IAM 14594 was expressed in E. coli, most of the gene product expressed was produced as aggregated insoluble particles known as inclusion bodies. In order to produce with an elevated level of a soluble and active form of alginate lyase in E. coli, the hyperthermophilic chaperonins (ApCpnA and ApCpnB) from archaeon Aeropyrum pernix K1 were employed as the coexpression partners. At $25^{\circ}C$ culture temperature, the level of alginate lyase activity was increased from 10.1 unit/g-soluble protein in aly single expression to 83.1 unit/g-soluble protein by coexpressing with ApCpnA and to 100.3 unit/g-soluble protein by coexpressing with ApCpnB. This results indicate that the coexpression of aly with ApCpnA and ApCpnB revealed a marked enhancement, about 8~10 fold, in the production of alginate lyase as a soluble and active form. Based on the results of various examinations on the expression variables, the optimal conditions for the maximal production of alginate lyase were determined as 1.0 mM IPTG for the inducer concentration, $25^{\circ}C$ for the culture temperature after IPTG induction, and ApCpnB for the coexpression partner. The coexpression set in the present report may be useful in the industrial production of functionally or medically important recombinant proteins in E. coli.

• Korean Journal of Food Science and Technology
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• v.20 no.6
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• pp.883-889
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• 1988

The salted small shrimps(Acetes japonicus) were fermented for 3 months at room temperature. During the period of fermentation, the changes of shrimp protein properties were determined. The extractability of soluble protein was slightly decreased in 1 month fermentation, but thereafter increased. The contents of 10% TCA soluble fraction were gradually increased during 3 month fermentation, and the rate of 10% TCA soluble fraction/total soluble protein was also greatly increased during the period of fermentation. Sephadex G-100 gel filtration pattern was changed after 1 month fermentation, showing the disappearance of low molecular weight protein peaks, the decomposition and the delay of elution time of main shrimp protein peaks. Polyacrylamide gel disc electrophoresis patterns showed the degradation of main protein bands into lots of smaller bands after 1 month fermentation. The contents of total free amino acids were slightly decreased in 1 month fermentation and then gradually increased during the Period of fermentation. The rate of free amino acids/soluble protein was steadily increased during the period of fermentation, but the rate of free amino acids/10% TCA soluble fraction was decreased continually during the period of fermentation. The contents of most free amino acids were increased during the period of fermentation, but those of histidine and arginine were greatly decreased in 1 month fermentation. Ammonia was increased after 1 month fermentation. The pH value of salted shrimp was slowly changed during 3 months of fermentation, showing increase from 7.8 to 8.2.

• Journal of Plant Biology
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• v.38 no.3
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• pp.251-258
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• 1995

The soluble acid invertase ($\beta$-D-fructofuranoside fructohydrolase, EC 3.2.1.26) was isolated and characterized from the hypocotyls of mung bean (Phaseolus radiatus L.). The enzyme was purified to apparent homogeneity by consecutive step using diethylaminoethyl (DEAE)-cellulose anion exchange, Concanavalin (Con) A affinity and Sephacryl S-300 chromatography. The overall purification was about 148-fold with a yield of about 15%. The finally purified enzyme exhibited a specific activity of about 139 $\mu$mol of glucose produced mg-1 protein min-1 at pH 5.0 and appeared to be a single protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and nondenaturing PAGE. The enzyme had the native molecular weight of 70 kD and subunit molecular weight of 70 kD as estimated by Sephadex G-200 chromatography and SDS-PAGE, respectively, suggesting that the enzyme was composed of a monomeric protein. On the other hand, the enzyme appeared to be a glycoprotein containing N-linked high mannose oligosaccharide chain on the basis of its ability to bind to the immobilized C on A. The enzyme had a Km for sucrose of 1.8 mM at pH 5.0 and maximum activity around pH 5.0. The enzyme showed highest enzyme activity with sucrose as substrate, but the activity was slightly measured with raffinose and cellobise. No activity was measured with maltose and lactose. These results indicate the soluble acid invertase is a $\beta$-fructofuranosidase.

• Archives of Pharmacal Research
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• v.19 no.4
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• pp.326-334
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• 1996

We investigated the optimum conditions for conversion of water-insoluble components of basidiocarps of Ganoderma lucidum to water-soluble components by hydrolyzing with chitinase. We also tried it with Ganoderma luciclum residue remaining after extracting hot water-soluble components of Ganoderma lucidum. After hydrolyzing under optimum conditions (20 ppm chitinase, 2% Ganoderma lucidum or 6% Ganoderma lucidum residue, at pH 3 and at $ 35^{\circ}C$), the contents of total water-soluble components (polysaccharide or protein) were measured, and it was found that the contents of water-soluble components increased to 1.5-2.7 fold. Michaelis constant, $K_m$ and maximum rate, $V_max$ calculated by Lineweaver-Burk plot for hydrolysis of Ganoderma lucidum were 1.75% and 0.02%/min respectively and those for hydrolysis of Ganoderma lucidum residue were 53.15% and 0.53%/min respectively The protein-bound polysaccharide was isolated after hydrolysis and molecular weights were measured by Sepharose CL-4B gel filtration and compared with the molecular weights of polysaccharide before hydrolysis.

• KSBB Journal
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• v.17 no.6
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• pp.515-519
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• 2002

The changes in the levels of total soluble protein and some free amino acids were investigated in germinating brown rice. Nongerminated (N) brown rice was germinated for 72 hrs by applying following solutions: 1) distilled water (W), 2) 50 ppm chitosan in 5 mM lactic acid (CL), and 4) 50 ppm chitosan in 5 mM glutamic acid (CG). The level of total soluble protein was higher in the N extract than those of W, CL and CG. Alanine levels were enhanced and aspartic acid levels were decreased significantly in the germinated brown rice, highest increases of alanine were found in the CG germinated brown rice. The levels of serine, decreased during germination in solutions W and CL, were increased significantly by germination in CG solution. The levels of essential amino acids, such as Iysine, isoleucine and methionine were also increased significantly by germination in CG solution. Our results show that the germination of brown rice with CG solution can significantly increase the levels of alanine and some other essential amino acids and can restore the serine level.

• Korean Journal of Microbiology
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• v.6 no.1
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• pp.22-28
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• 1968

Chlorella ellipsoidea cells were cultured in an iron, copper, zinc, manganese, molybdenum or boron-free medium. Biosynthetic activities of nucleic acids, protein and phospholipid in chlorella cells, which were growing in a microelement deficient medium were compared with those of the normal cells by measuring the contents of phosphate, amino acids or UV-absorbing substances in the various cell fractions. When the algae were grown in a molybdenum-free medium, the amounts of phosphate in the acid-soluble fraction of the cells increased, whereas the amounts of alkali-stable protein and RNA decreased compared with the normal cells showing that the synthesis of protein and RNA from the early products of photosynthesis was inhibited. When the algae were grown in a boron-free medium, amounts of alkali-labile protein and phospholipid of the cells decreased, while the amount of phosphate in acid-soluble fraction increased compared with the normal cells showing that the biosynthesis of protein and phospholipid from the early products of photosynthesis was retarded. In general, amounts of protein and RNA in the microelement deficient cells significantly decreased compared with those of the normal cells. Phosphate content in the acid-soluble fraction of the algal cell grown in an zinc, copper, molybdenum, or boron-free medium increased considerably, whereas that of the algal cell grown in an iron or manganese-free medium decreased remarkably compared with that of the control. It is considered, therefore, that molybdenum, zinc, copper and boron etc. play an important role in the biosyntbesis of macromolecule from acid-soluble phosphate compounds, in contrast to the principal action of iron and manganese on the photosynthetic process itself.

• Journal of Plant Biology
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• v.26 no.4
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• pp.173-180
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• 1983

L-canavanine was added to GAs treated barley seeds, and induced amylase activity, soluble protein content, and arginine content were mesured. Canavanine, added at the beginning of the incubation period, inhibited amylase activity and protein accumulation. Amylase activity decreased markedly by addition of canavanine at 6 hr after incubation, where soluble protein content was not affected. The addition of canavanine after 12 hr incubation did not show serioud inhibited effect on the amylase activity and protein accumulation. GAs incubation caused decrement in arginine content per mg protein, but it was somewhat recovered by canavanine treatment. The longer the time between GAs and canavanine addition was, the less the recovery ration was. Arginine content in the $\alpha$-amylase fraction (ammonium sulfate 20~50% saturation) was lower than in 0~20% fraction, but higher than in 50~80% fraction. These results and control expreiments, using cordycepin and cycloheximide, support the idea that canavanine might incorporate into protein.