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Volume 40, Issue 1
Displaying 1-11 of 11 articles from this issue
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Hiroshi SUZUKI, Yuji KAWARAZAKI, Noboru MURAYAMA1966 Volume 40 Issue 1 Pages 1-7
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSRice plant (Oryza sativa var. japonica) was cultured in 1/2, 000 are Wagner's pots by the early and late season growing methods. Rice plants were brought in fixed temperature glass rooms set at 17°, 21°, 25°, and 30° with or without about 50% shading after earing time, and let them mature for 30 days in the rooms. Irrespective of the growing methods, as the temperature of maturing period became lower, milled rice grains collapsed more easily in 1.7% KOH, starch became more susceptible to alkali, and blue color of starch with iodine became deeper. X-ray diffraction patterns of starches matured at 17° with or without shading and starch matured at 21° with shading showed C-type, but other starch samples showed A-type.View full abstractDownload PDF (1332K) -
Isolation of the Saponin from the Leaf of Thea sinensis L. and its PropertiesAkito HASHIZUME, Yajiro SAKATO1966 Volume 40 Issue 1 Pages 8-12
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSAn acidic saponin _??_m. p. 232_??_233° (decomp.), [α]20D-10° (c=0.800, 80% EtOH)_??_ was isolated in a pure crystalline state from the leaf of Thea sinensis L. cultivated in Miyazaki Prefecture. The IR-spectrum of this saponin has resemblance to the one isolated from the seed of Thea sinensis L. However it was found that this saponin is a different substance from the seed saponin as the differences of m. p. (decomp.), specific rotation, UV-spectrum and the intensity of colour seen in Liebermann-Bur chard reaction are shown.
As for the taste of bitterness, the saponin isolated from the leaf is much weaker than the one from the seed, but still has strong irritation to the velum and it can be said that the quantity of the saponin has much to do with the quality of the tea. The spots of these saponins showed up clearly every time on the thin-layer chromatography.View full abstractDownload PDF (1081K) -
On the Microdetermination of Substituted Anilines in Biological MaterialsToshiie NAKAMURA, Takayuki UEDA, Kyuichi TANAKA1966 Volume 40 Issue 1 Pages 13-19
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSIn order to study the enzymatic hydrolysis of mono fluoroacetanilides, the simplified microdetermination methods of substituted anilines in biological materials were examined.
(1) In case of the nuclear substituted anilines, p-iodo, p-nitro, p-nitro-o-chloro, and p-methyl anilines and p-aminobenzoates, the diazotization and coupling method using N-(1-naphthyl)-ethylenediamine dihydrochloride as coupling reagent was employed. The maximal development and the stability of the color were remarkably affected by pH of the reaction medium. The optimal pH and the stable period in each compound were determined. The analytical results in mouse liver homogenate were satisfactory with this procedure. (2) When the above method was applied to p-aminobenzoic acid and its esters, ethyl, n-butyl, and isobutyl esters, it was found that their molar absorptivities were extremely identical. The analytical procedure was able to be simplified, since the hydrolysis of the esters in biological materials was able to be ignored. (3) In case of the N-substituted anilines, N-methyl and N-ethyl anilines, the ultraviolet absorption method (each λm_??_x, 238 mμ) was employed. Although the effect on the end-absorbance of N-alkyl fluoroacetanilides as substrate was not able to be ignored in this method, a simplified determination method in the hydrolysis system was established, since the total moles of the substrate plus product are always constant. The recoveries of N-alkyl anilines in the substrate-product mixture were almost 100%. (σ=about 4)View full abstractDownload PDF (498K) -
Enzymatic Hydrolysis of Monofluoroacetanilides in Animal Tissues (II)Toshiie NAKAMURA1966 Volume 40 Issue 1 Pages 20-25
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSThe enzymatic hydrolysis of monofluoroacetanilides and their homologues in the liver homogenates of some warm-blooded animals was investigated, and the distribution of this enzyme in rat body was determined.
(1) The great activity of the enzyme which hydrolyzes monofluoroacetanilides was found in the liver homogenates of mouse, chick, cow, and rat. It is estimated that the enzyme exists commonly in the liver of warm-blooded animals. (2) Monochloroacetanilide and monoiodoacetanilide were remarkably hydrolyzed in the liver homogenates of mouse, chick, and cow as monofluoroacetanilides were. But acetanilides were scarcely hydrolyzed in the homogenates. (3) The activity of the enzyme in mouse liver homogenate was increased by addition of Mn2+, Co2+ Mg2+, and Fe2+ in the incubation medium. (4) In the homogenates of various rat tissues, the activity was greatest in liver, fairly great in kidnay, and slightly in pancreas. But no activity was found in spleen, intestinal mucosa, muscle, brain, lung, and heart.View full abstractDownload PDF (492K) -
Takashi IGUCHI, Shiro HAYAKAWA, Isao TAKEDA1966 Volume 40 Issue 1 Pages 26-34
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSLarge quantities of L-glutamic acid were produced from liquid paraffins by hydrocarbonutilizing microoganisms when penicillin was added to the growing culture. These microorganisms were distributed in wide range of gram-positive, -negative bacteria and in Nocardia. The gram-positive bacteria that accumulated a remarkable amount of L-glutamic acid was identified as the new species Corynebacterium petrophilum nov. sp.
On the production of L-glutamic acid, the effects on the additional concentration and phase of penicillin, on the organic nutrients such as corn steep liquor, and on the inorganic nitrogen sources were studied by Cory. petrophilum nov. sp. Various kinds of hydrocarbons were also tested. Synthetic penicillin, bacitracin, cycloserine, glycine and 5-bromouracil were effective for the accumulation of L-glutamic acid from liquid paraffin.
The action of these compounds to the L-glutamic acid production seems to be explained from the cellular permeability of L-glutamic acid.View full abstractDownload PDF (675K) -
Isomerization with Various Kinds of Alkali ReagentsKeiji KAINUMA, Katsuko TADOKORO, Shigeo SUZUKI1966 Volume 40 Issue 1 Pages 35-40
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSIn the previous paper, the fundamental conditions of alkali-catalyzed isomerization using sodium hydroxide were described mainly from the point of the formation of ketose, organic acid and colored substances.
In this paper, 12 kinds of alkali, alkali salts, buffer solutions and anion exchange resin were examined as the catalysts. Some of them were effective for preventing color formation or decrease of ketose during prolonged reaction time. The former is sodium sulfite and the latter sodium tetraborate.
Decreasing of pH during isomerization were already reported in the previous paper. To keep the pH of the reaction mixture in the alkali side for long period, 0.2M carbonate buffer solution was examined as the catalyst with several concentrations of dextrose. In the case, when the mol ratio of ‘salt in buffer solution/dextrose’ is 1/1, the reaction pH was kept rather well after 60min. at 97°C, but destruction of sugar was extremely high. After 30min. and 60min., 37% and 45% of sugar were destructed respectively and decrease of PKF (percent of ketose formed) were started after 10min. Among the catalysts examined, none was more effective than sodium hydroxide from the point of view of ketose formation.
It is proved again in this paper that the initial pH value of the reaction mixture was the most important factor for ketose formation.View full abstractDownload PDF (488K) -
Effect of Heating on Amino Acid Liberation with Enzymes in Defatted Soybean FlourHarue TAIRA, Hirokadzu TAIRA, Yosito SAKURAI1966 Volume 40 Issue 1 Pages 41-47
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSThe influence of heat treatment on amino acid liberation in defatted soybean flour was studied by the enzymic treatment with two proteases, one obtained from Aspergillus oryzae and the other from Streptomyces griseus. The samples were autoclaved at 0kg/cm2 (100°C) and 0.35kg/cm2 (108°C) for 1, 2 and 4 hours and at 0.7kg/cm2 (115°C) and 1.4kg/cm2 (126°C) for 0.5, 1, 2 and 4 hours with an equal weight of water. After heat treatment, the samples were incubated at 37°C with both the enzymes and the eighteen amino acids were determined by microbiological assay.
On the degree of amino acid liberation with Aspergillus-protease, heat treatment caused the increase of glutamic acid, lysine, arginine, tyrosine, proline and methionine, and the decrease of alanine, aspartic acid, histidine and cystine. In the case of Streptomyces-protease, all the amino acids, except proline, were increased and especially glutamic acid, arginine, lysine, phenylalanine, methionine and cystine were increased.
The samples autoclaved at 0.7 and 1.4kg/cm2 for 4 hours showed the low liberation value on both the enzymic digestions, and, especially at 1.4kg/cm2, aspartic acid, lysine, histidine, tyrosine and cystine were the lowest value on Aspergillus-protease digestion and glycine, glutamic acid, lysine, tryptophan, methionine and cystine on Streptomyces-protease digestion.
The pattern of the liberated amino acids with Aspergillus-protease was different from that with Streptomyces-protease and was similar to the free amino acid pattern of “Mamemiso” processing in a previous paper.View full abstractDownload PDF (581K) -
Shigeo AKAIKE1966 Volume 40 Issue 1 Pages 48-51
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSThe Eη values of tissue fluid of water-cultured tobacco plants (var. Bright Yellow) were determined. The values were found to be positive and to vary within the range of +100 to +380 mV in leaves, and about +500 mV in roots. The relation between pH and Eη, of tissue fluids differed slightly with leaf positions, but showed systematic variance. The effect of leaf position on the Eη value varies with the leaf age generally, and the value showed to be high in upper than in lower leaves. After topping the potential increased gradually and reached maximum by fifteenth day in upper leaves and tenth day in lower, and then decreased rapidly in both leaves. These variations in topped plants were special phenomenon in contrast with non-topped which showed tendency of decreasing in this stage.
From above mentioned results it appeared that topping treatment made response to the oxidation-reduction potential of leaf tissue fluid.View full abstractDownload PDF (344K) -
Umeo YOSHINO, Nobuji NAKATANI, Yo TOKORO, Kunio YAMAUCHI1966 Volume 40 Issue 1 Pages 52-57
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSRennin and pepsin in rennet were fractionated by DEAF-cellulose chromatography. The activity of pepsin was determined and the significance of pepsin in rennet was investigated. Rennet, dialyzed against 0.1M phosphate buffer (PB) of pH 5.7, was eluted stepwise from DEAE-cellulose column by the eluting solutions (0.1M PB plus 0, 0.1, 0.2 and 0.3M NaCl, and 0.1 N HCl).
Fraction 1, the breakthrough fraction coming down with 0.1M PB, had no activity. About eighty per cent of total milk-clotting activity was recovered in Fraction 3 which was eluted by 0.1M PB plus 0.2M NaCl. Electrophoresis and sedimentation analyses in phosphate buffer of pH 6.62 and ionic strength 0.2 revealed Fraction 3 homogeneous. The specific activity of Fraction 3 was comparable with crystalline rennin. These results show that DEAF-cellulose chromatography is effective to purify rennin from crude rennet. Fraction 5, eluted by 0.1 N HCl, contained one per cent of total milk-clotting activity. By the comparative studies on Fraction 5 and pepsin, Fraction 5 was assumed to contain pepsin.
No significant difference between proteolysis of casein by Fraction 3 (i.e. free of pepsin) and rennet suggested that pepsin, which comprised only one to two per cent of total activity of rennet, had no effect on proteolytic activity of rennet. However, since the amount of pepsin may vary with rennet preparations, the determination of pepsin in each preparation will be necessary to study the role of pepsin in rennet.View full abstractDownload PDF (1428K) -
Masanao OYA, Koichi SETO, Isao SATO1966 Volume 40 Issue 1 Pages 58-60
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSγ-Benzyl-N-carboxy-L-glutamate anhydride and γ-methyl-N-carboxy-D-glutamate anhydride were synthesized by the use of a new recrystallization technique. The polymerization of these monomers was carried aut in o-dichlorobenzene, nitrobenzene and tetrahydrofuran using water, triethylamine and sodium hydroxide as initiator.
In the polymerization of γ-methyl-N-carboxy-D-glutamate anhydride, the molecular weight of the polymer formed did not become higher in proportion to the extent of polymerization forty per cent or more. The polymerization of γ-benzyl-N-carboxy-L-glutamate anhydride in o-dichlorobenzene which is nonsolvent for the polymer led to lower molecular weight of polymer on agitating than the polymerization on the steady state, but the polymerization in nitrobenzene which is a solvent for it led to lower molecular weight of the polymer on agitating than the polymerization on the steady state.View full abstractDownload PDF (206K) -
Shinpei KUYAMA1966 Volume 40 Issue 1 Pages R1-R6
Published: 1966
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (510K)
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