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Volume 54, Issue 10
Displaying 1-12 of 12 articles from this issue
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Yuziro SAKURAUCH, Eisho KONDO1980 Volume 54 Issue 10 Pages 837-844
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSThe lethal effect of high electric fields on Escherichia coli K-12 IAM-1264 and on spore of Bacillus subtilis IAM-1169 has been studied.
Electric field strength was more weak than spark discharge, and added to suspension of the organisms by the series of direct current pulses.
The lethal effect was influenced by the electric field strength, the capacity, the number of discharges and the viscosity of the solution. The spore of Bacillus subtilis was more difficult to inactivate than Escherichia coli. From this experiment, the equation for inactivation of microorganisms was obtained:
dn/dt=-k'ndε/dt
where n is the number of microorganisms in unit volume, and ε, the electric energy added to the test solution per unit volume at time t. If it is assumed that the total electric energy is converted to kinetic energy of ions in aqueous medium, the inactivation equation is:
n=n0e-k1/2 αE2C/η2
where n0 is the initial viable number of microorganisms in unit volume t=0 sec; E, electric field strength V/cm; C, electric capacity; α, addition number of electric pulse; η, viscosity of the solution and k, the constant.View full abstractDownload PDF (608K) -
Tamaki NARITA, Masakazu TSUTSUMI, Asao MATSUOKA, Tadao WATANABE1980 Volume 54 Issue 10 Pages 845-848
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSStaphylococcus aureus IFO 3060 is a salt-tolerant bacterium that can grow in medium containing from 0% to 15% NaCl. S. aureus grown in 5% NaCl medium accumulated large quantities of intracellular free proline. The addition of cholate to the medium resulted in an increase in the proportion of intracellular free proline to proline in protein fraction.
On the other hand, the incorporation of proline into cells of S. aureus was inhibited by adding cholate to 5% NaCl medium. The content of the intracellular free proline decreased to half as a result of inhibition. Furthermore, previous paper showed that the salt-tolerance of S. aureus was markedly weakened by adding cholate to the medium.
These results suggest that accumulated proline plays an important role in the mechanism of the osmoregulation of S. aureus. Lowering the function of the osmoregulation system by decreasing of free proline may weaken the salt-tolerance of S. aureus.View full abstractDownload PDF (283K) -
Hirozo KUSUNOSE, Masayoshi SAWAMURA1980 Volume 54 Issue 10 Pages 849-855
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSA hot water-soluble polysaccharide was isolated from the endosperm of the ripe seed of Astragalus sinicus L. and fractionated with ethanol to obtain purified galactomannan, whose homogeneity was ascertained by DEAF-cellulose column chromatography and sedimentation analysis. The specific rotation of the galactomannan was [α]18D+61.5 (c=1.1, H2O), and its molar ratio of D-galactose to D-mannose was 1:2.3. The molecular weight was estimated to be 15, 900 by hypoiodometry and gel filtration on Sephadex G-75. On oxidation of the galactomannan 1.18 moles of periodate per mole of hexose residue were consumed, accompanying the formation of 0.31 moles of formic acid. The products of this galactomannan by Smith degradation were glycerol, erythritol and D-mannose in a molar ratio of 2.5:4.5:1.
The specific rotation of fully methylated galactomannan was [α]18D+48 (c=0.8, CHCl3). The methylated galactomannan gave the following sugars by hydrolysis: 2, 3, 4, 6-tetra-O-methyl-D-mannose, 2, 3, 4, 6-tetra-O-methyl-D-galactose, 2, 4, 6-tri-O-, 2, 3, 6-tri-O- and 2, 3-di-O-methyl-D-mannose, in an approximate molar ratio of 1:30:12:24:30. The results were obtained from gas chromatography of alditol acetate derivatives of methylated sugars, of hydrolysates. From these results it is suggested that the chemical structure of galactomannan from seeds of Astragalus sinicus L. may be composed of a main chain consisting of (1→4) and (1→3)-linked β-D-mannose residues with side chains consisting of single β-D-galactose residues linked to the main chain through (1→6) bonds.View full abstractDownload PDF (1430K) -
Yoshiharu MATSUBARA, Kenji ISHII1980 Volume 54 Issue 10 Pages 857-863
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDehydroascorbic acid (DHA) was heated with nucleotides, nucleosides or bases in 0.01 N HCl at 98°C for 8 hr, and the browning of the reaction mixture was measured at 480 nm. Of five nucleotides, five nucleosides and four bases examined, browning was relatively strong with 5'-adenylic acid, 5'-guanylic acid, adenosine, guanosine and adenine.
When DHA (1 mmol) was heated with adenine or adenosine (1 mmol) in 4ml of glacial acetic acid or a mixture of glacial acetic acid and methanol, a reaction product (Rf 0.16 fraction or Rf 0.14 fraction)of DHA with adenine or adenosine was formed and separated by thin-layer chromatography. These fractions were visible under UV light and were positive to ammoniacal AgNO3. The Rf 0.14 fraction was also positive to aniline phthalate. By heating in 2 N HCl at 98°C, the Rf 0.16 fraction or Rf 0.14 fraction yielded adenine, DHA (enol) and a degradation product of DHA or adenosine, adenine, ribose, DHA (enol) and a degradation product of DHA. Also, the peak at 316nm (Rf 0.16 fraction) or shoulder at 305nm (Rf 0.14 fraction) in their UV spectra disappeared. Glycine was formed from these fractions by acid hydrolysis, suggesting that these fractions involved an adenine moiety. From these findings, DHA was found to react with adenine or adenosine to form the reaction product.View full abstractDownload PDF (491K) -
Hiromu KAMEOKA, Seiji HASHIMOTO1980 Volume 54 Issue 10 Pages 865-869
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSSteam volatile oils were obtained from Brassica raga L. var laciniitolia Kitamura collected in different districts. The oils were prepared by steam distillation from the leaves and stems. Each volatile oil was chemically separated into two fractions, and each fraction was investigated by IR, NMR, GC-MS and GLC.
The characteristic major components were 4-pentenonitrile, 5-hexenonitrile, 3-phenylpropiononitrile, 3-butenyl isothiocyanate, 4-pentenyl isothiocyanate, 5-methylthiopentanonitrile and 6-methylthiohexanonitrile. The minor components were dimethyl trisulfide, n-hexyl isothiocyanate, 2-phenylethyl isothiocyanate, 4-methylthiobutanonitrile, 7-methylthioheptanonitrile, 4-methylthiobutyl isothiocyanate and 5-methylthiopentyl isothiocyanate.View full abstractDownload PDF (324K) -
Kin-ichi MATSUSHIMA, Ken NIHO, Kyo SHIMADA1980 Volume 54 Issue 10 Pages 871-873
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSSeventy five strains of various species of Penicillium were analyzed for the nature of their proteolytic enzymes which were produced in wheat bran culture. These studies led to the conclusion that the proteolytic enzyme system of penicillia can generally be characterized as being rich in acid proteinase and poor in alkaline- and neutral proteinase. A few strain of penicillia, which has proteolytic enzyme system consisting mostly of alkaline proteinase, was found to locate only in asymmetrica section but not in monoverticillata and biverticillata symmetrica section.View full abstractDownload PDF (830K) -
Kin-ichi MATSUSHIMA, Ikuhisa MORI, Naruto ITO, Kyo SHIMADA1980 Volume 54 Issue 10 Pages 875-876
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSSeventy-nine strains of the isolated fungi which are capable of growing on the agar plate of pH 1.5 (acid-tolerant fungi) and 74 strains of the isolates which are capable of growing on the agar plate of pH 10 (alkaline-tolerant fungi) were analyzed for the nature of proteolytic enzymes which were produced in wheat bran culture. Most of acid-tolerant fungi had proteolytic enzyme system consisting almost solely of acid proteinase and most of alkalinetolerant fungi had proteolytic enzyme system consisting almost solely of alkaline proteinase.View full abstractDownload PDF (595K) -
Regulation of Extracellular α-Amylase Production and Cloning of α-Amylase Genes of Bacillus subtilisKunio YAMANE1980 Volume 54 Issue 10 Pages 877-883
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (562K) -
Shigeo YOSHIDA1980 Volume 54 Issue 10 Pages 885-892
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (561K) -
[in Japanese], [in Japanese]1980 Volume 54 Issue 10 Pages 913-917
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (2612K) -
N. Y.1980 Volume 54 Issue 10 Pages 919-921
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (279K) -
[in Japanese]1980 Volume 54 Issue 10 Pages 921-923
Published: 1980
Released on J-STAGE: November 21, 2008
JOURNAL FREE ACCESSDownload PDF (1101K)
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