Nippon Nōgeikagaku Kaishi
Online ISSN : 1883-6844
Print ISSN : 0002-1407
ISSN-L : 0002-1407
Volume 53, Issue 3
Displaying 1-9 of 9 articles from this issue
  • Takashi YAMANOBE, Yoshiyuki TAKASAKI
    1979 Volume 53 Issue 3 Pages 77-80
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Various kinds of starches, which were previously liquefied by Bacillus subtilis α-amylase, were hydrolysed by a mixture of β-amylase and pullulanase of B. cereus var. mycoides. The liquefied starches were effectively saccharified by the hydrolases. The maximum yield of maltose from starches liquefied to a DE value of 1_??_2 was about 87_??_88%, and the incubation conditions of pH 6.0_??_8.0 and 55°C for 30 hr using 5% solution of liquefied starch were best for saccharification of the liquefied starch. Starches were liquefied by acid and saccharified by β-amylase and pullulanase, and the yields of maltose were compared with above results. However, no significant difference in the yield of maltose was observed between two starch liquefaction methods.
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  • Kazue TATSUGUCHI, Tomoko SETOKUCHI, Jiro YAMADA, Tadao WATANABE
    1979 Volume 53 Issue 3 Pages 81-86
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Antimicrobial actions of trialkyltin compounds on Escherichia coli JE 1011 and its NS mutants were investigated.
    1. Triethyltin chloride (TET) revealed antimicrobial action similarly on JE 1011 and NS mutants, and tripropyltin chloride (TPT) showed more activity on NS mutants than on JE 1011, however tributyltin chloride (TBT) was effective only on NS mutants.
    2. Partition coefficient of TET, TPT and TBT were 2.5, 22 and 49, respectively, indicating that the more carbon number in alkyl chain of the compounds, the more hydrophobic. Partition was determined in the 1-octanol/0.05M sodium phosphate buffer (pH 7.0) system at 20°C.
    3. LPS and protein were rapidly released from JE 1011 treated with EDTA. Antimicrobial action on JE 1011 was increased in the case of TPT and TBT by EDTA treatment of the cells, especially in TBT, but not in TET.
    4. From these results and data on the LPS of these strains, it was suggested that outer membrane of JE 1011 was permeability barrier for TPT and TBT which were more hydrophobic than TET.
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  • (1) Crude Enzyme and Unadsorbed Fraction on CM-Cellulose
    Tatsuo FUJIKAWA, Kojiro KOYABU, Masafuto WADA
    1979 Volume 53 Issue 3 Pages 87-95
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Enzymes contained in hepatopancreas of abalone were investigated from a viewpoint of structural study of fucoidan. Results obtained were as follows.
    1. Fucoidan sulfatase activity together with fucoidanase activity were observed in a fraction (crude enzyme) precipitated from 30 to 50% saturation of ammonium sulfate.
    2. Each activity was separated into two fractions, unadsorbed and adsorbed fraction on CM-Cellulose at pH 5.0. Both activities of the unadsorbed fraction were eluted in the same elution range (Enzyme I) from DEAE-Cellulose column by gradient elution. Separation of both activities and inhibition either of them by using acid, alkali, or heat were unsuccessful.
    3. Rate of reducing sugar formation was decreased with reaction period in case of the crude enzyme, while it remained constant during reaction in case of Enzyme I. Decreased rate of sulfate ion formation was observed in both cases.
    4. Sugars formed by the crude enzyme were almost fucose. However, sugars formed by Enzyme I were primarily neutral oligosaccharides, and their polymerization degree showed a tendency to diminish with reaction period.
    From the above evidence, it is considered that fucoidanase which degrades fucoidan to oligosaccharide, but not to fucose, and fucoidan sulfatase are existent in Enzyme I, and that, therefore, a method of investigation for partial degradation of fucoidan will be available by these enzymes.
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  • Yoshinori ITOH, Yoshiyuki MORISHITA, Kageaki AIBARA
    1979 Volume 53 Issue 3 Pages 97-102
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Bacteria isolated from mixed culture originated from rat feces having aflatoxin B1-degrading potency were examined in vitro for degrading aflatoxin B1 after three day incubation. They were composed of four strains of Clostridium sp., three strains of Bacteroides sp. and three strains of Catenabacterium sp. for anaerobes and a strain of Pseudomonas aeruginosa, a strain of Proteus mirabilis, three strains of Streptococcus sp. and a strain of Escherichia coli for aerobes. P. mirabilis Y 2 degraded 50.9% of initial concentration of aflatoxin B1 in 72 hr, three strains of Catenabacterium sp., P. aeruginosa Y 1, Streptococcus sp. Y 5 degraded 25.0_??_35.5 % and the anaerobes other than Catenabacterium sp., Streptococcus sp. Y 4, Streptococcus sp. Y 6 and E. coli Y 8, 12.4-22.0%. Combinations of P. mirabilis Y 2 plus each strain of the Streptococcus sp. degraded 85.6_??_100% of aflatoxin B1 and a combination of all strains of the aerobes degraded 78.8% but all other combinations degraded less than 54.0%. P. aeruginosa Y 1 alone and the combination of P. aeruginosa Y 1 plus P. mirabilis Y 2, that of P. aeruginosa Y 1 plus Streptococcus sp. Y 4 and that of all six strains formed from aflatoxin B1 a very small amount of a new substance with bright-blue fluorescence and Rf value of 0.39 compared with 0.42 for aflatoxin B1 and 0.34 for B2 on thin-layer chromatography plate. Formation of the new fluorescent substance seemed to be concerned with P. aeruginosa Y 1.
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  • Tadao HASEGAWA, Norikazu MATSUMOTO, Takao SUZUKI
    1979 Volume 53 Issue 3 Pages 103-105
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    We have already obtained findings that the amino acids composed of acetyl-L-methionine and L-serine could accelerate the hair growth of rabbits. The effects of light as a physical factor were particularly investigated in the current studies, in which the experimental rabbits were given the hair tonic containing the above amino acids and exposed to lamp light (14L:10D), natural light and darkness, respectively.
    As the result, a photoperiodic stimulation was observed in both the artificial and natural lights. The darkness was definitely effective for the unfavorable growth of hair. The hair root in a group of rabbits given an amino acid solution had grown in the order of lamp light, natural and darkness with a significant difference of 5% between the light and the darkness.
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  • Norikazu MATSUMOTO, Tadao HASEGAWA, Takao SUZUKI
    1979 Volume 53 Issue 3 Pages 107-109
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
    Investigations were carried out on the effects of light alone not having been affected with the variation of amino acid. The result obtained 2 weeks after the start of experiments was that the hair weight was most heavy under the natural light and next came those under the lamp light and the darkness in order.
    However, the weight had changed in the order of the lamp light, natural light and darkness after 3 weeks. The hair weight was heavier in the order of the lamp light, natural light and darkness, although it showed an almost same trend in the final stage.
    Despite the similar growth condition of rabbits under the natural and lamp lights, the body weight had slightly decreased under the darkness. The hair quality of rabbits on the final day of experiments was observed by a scanning electron microscope. A distance between the epidermis scales was most wide under the hamp light. Under the natural light it was wider than that under the darkness.
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  • 1979 Volume 53 Issue 3 Pages N39
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
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  • Mitsuo CHINO
    1979 Volume 53 Issue 3 Pages R1-R8
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
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  • N. Y.
    1979 Volume 53 Issue 3 Pages N27-N29
    Published: 1979
    Released on J-STAGE: November 21, 2008
    JOURNAL FREE ACCESS
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