Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
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Volume 27, Issue 2
Displaying 1-13 of 13 articles from this issue
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  • Studies on Peptidases of Aspergillus oryzae
    Part II. A Survey of Dipeptidase and Aminopolypeptidase Activities of Various Molds, and a Study of Mold Culture Method and Enzyme Extraction
    Tadami AKATSUKA, Masakazu SATO
    1963 Volume 27 Issue 2 Pages 71-75
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.71
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    Screening experiments for dipeptidase and aminopolypeptidase from 40 strains of molds were conducted using Leu-Gly, Gly-Leu, Ala-Gly and Gly-Gly-Leu as substrates.
    The strains of Aspergillus oryzae RO-0129 A-2, IAM-2600 and IAM-2616 showed strong activities of both dipeptidase and aminopolypeptidase.
    Further, optimal condi tions for making culture as well as those for the extractions of the peptidases from the mycerial mats were investigated.
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  • Activation of Enzymes in the Ungerminated Barley Endosperms with Gibberellin
    The Condition Under which α-Amylase Activation was Stimulated in the Intact Endosperms and the Endosperms Flinders
    Harugoro YOMO, Hironobu IINUMA
    1963 Volume 27 Issue 2 Pages 76-79
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.76
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    Barley endosperms (expt. A) and their finders (expt. B) which were obtained by cutting off the endosperms into about eight pieces, were incubated with gibberellin. The conditions under which α-amylase was activated were studied.-Amylase activation was proved to show maximum at 30°C and pH 4.7 in the both cases. Activation by several salts was also found in the both cases, especially in expt. B. Sugar (sucrose) rather retarded this activation. In expt. B α-amylase activation was found to increase in accordance with increasing concentration of gibberellin. In expt. A maximum activation was observed at 1 ppm of gibberellin.
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  • Studies on an Enzyme Capable of Splitting β-D-1, 6-Glucosidic Linkage
    Part I. Isolation of a Lutease-producing Microorganism and Some Properties of Lutease
    Norio NAKAMURA, Osamu TANABE
    1963 Volume 27 Issue 2 Pages 80-87
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.80
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    In the previous paper, it was reported that the higher molecular weight luteose which consisted of β-1, 6-linked D-glucose units was made by Pen. aculeatuin var. apiculatum. The isolation of the microorganism which is able to produce β-D-1, 6-glucanase and some properties of this glucanase were described in this paper. The optimum reaction temperature for this enzyme was at about 40°C, and the optimum pH was at about 6.7. At the maximum degree of the hydrolysis, only D-glucose and gentiobiose were detected, and at this point, the hydrolysis degree of higher molecular weight luteose was about 55% as D-glucose. The formation of β-D-1, 6-glucanase was induced by the addition of higher molecular weight luteose. From the property of this enzyme, the authors proposed the name “lutease” for this enzyme.
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  • Studies on the Metabolism of Aspergilli
    Part I. Substrates of Endogenous Respiration
    Takeji MIZUNUMA
    1963 Volume 27 Issue 2 Pages 88-98
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.88
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    Endogenous respiration of Aspergillus sojae K.S. was studied in terms of biochemical analysis. It was found that the different kind of substrates was utilized for the endogenous respiratoin according to C:N ratio of the agar medium on which the mold was grown. In the mycelial mats grown on the medium of low C:N value, pool amino acids, protein, and nucleic acids were mainly utilized from the beginning while carbohydrate or lipid displayed a minor role. The corresponding amount of ammonia was formed. On the other hand, in the mycelial mats grown on the medium of rather high C:N value, carbohydrate or lipid was the major substrate of endogenous respiration in the early stages of incubation. The utilization of the nitrogenous materials and the accompanying formation of ammonia got to start only after the lapse of several hours of incubation.
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  • Artificial Food for Oak-Silkworm Raising
    Toshifumi FUKUDA, Yoshikichi HIGUCHI
    1963 Volume 27 Issue 2 Pages 99-102
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.99
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    Oak-silkworms (Anthereae pernyi) were reared from hatching to the adult stage on a diet consisting of powder of dry leaves of oak trees (Quercus dentata T.), ‘Iinako’(powder of parched soy bean), sucrose, agar-agar, sodium dehydroacetate as an antiseptic, and water. Among 100 newly hatched oak-silkworms reared on the diet, 23 spun their cocoons. The weight of the cocoon fibres spun by one worm and the number of the eggs laid down by one moth were 0.34g and 203, respectively, on the average.
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  • Incorporation of 14C-Tyrosine into Soluble Ribonucleic Acid from Baker's Yeast
    Setsuro MATSUSHITA, Fumio IBUKI
    1963 Volume 27 Issue 2 Pages 103-109
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.103
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    The incorporation of 14C-tyrosine into S-RNA catalyzed by a partially purified tyrosine activating enzyme from baker's yeast was observed. The maximum incorporation was shown in the presence of 5μgmoles of ATP, 10μmoles of MgCl2 and 10-100μmoles of KCl in the reaction mixture of total volume of 1ml, at pH 7.8 when 1.2 mg of S-RNA, 0.1μmole of 14C-tyrosine and 400μg of enzyme protein were used. Beyond the concentration of ATP, MgCl2 and KCl described above, the tendency of inhibition was observed. The incorporation was strongly inhibited by pCMB and reactivated by cysteine. Manganese and calciumions were effective as substitutes for magnesium. S-RNA used was prepared from whole baker's yeast cell with phenol, but S-RNA obtained from the supernatant of the ground yeast had lost its incorporating activity.
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  • Degradation of Nucleic Acids and their Related Compounds by Microbial Enzymes
    Part I. On the Distribution of Extracellular Enzymes Capable of Degrading Ribonucleic Acid into 5'-Mononucleotides in Microorganisms
    Kôichi OGATA, Yoshio NAKAO, Seizi IGARASI, Einosuke OMURA, Yukio ...
    1963 Volume 27 Issue 2 Pages 110-115
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.110
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    The distribution in microorganisms of extracellular enzymes which degrade RNA into 5'-mononucleotides was studied. The degradation products of RNA were determined by using 5'-nucleotidase and adenosine deaminase.
    It was found that the enzymes were produced by various microorganisms belonging to Streptomyces, Bacillus, Fungi imperfecti such as Fusarium, Helminthosporium, etc., and Ascomycetes such as Neurospora, Glomerella, Aspergillus, etc.
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  • Degradation of Nucleic Acids and their Related Compounds by Microbial Enzymes
    Part II. On the Distribution of Extracellular Enzymes Capable of Degrading Ribonucleic Acid into 2'-(3')-Mononucleotides or Oligonucleotides in Microorganisms
    Yoshio NAKAO, Koichi OGATA
    1963 Volume 27 Issue 2 Pages 116-120
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.116
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    Degradation of ribonucleic acid (RNA) was investigated with extracellular microbial enzymes capable of hydrolyzing RNA into products other than 5'-mononucleotides. The degradation products were analyzed by using 5'-nucleotidase and non-specific prostatic phopshomonoesterase. It was found that most microorganisms investigated, including Rhodotorula glutinis, Spolobolomyces pararoseus, Helicostylum piriforme, Poria vaporaria, Gibberella fujikuroi, Penicillium citrinum, Aspergillus flavus, and Rhizopus chinensis, produced enzymes which degrade RNA into 2'-(3')-mononucleotides. However, such microorganisms as Candida clausenii, Bacillus cereus, Absidia butleri, Mucor genevensis, Polystictus hirsutus, Polystictus versicolor, and Phycomyces blakeslecanus degraded RNA into oligonucleotides.
    It is not clear whether the oligonucleotides formed from RNA by these microbial enzymes are terminated with 5'-phosphomonoester end group or with 3'-phosphomonoester end group.
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  • Anthocyanase and Anthocyanins Occurring in Eggplant, Solanum melongena L
    Part II. Isolation and Identification of chlorogenic Acid and Related Compounds from Eggplant
    Sadao SAKAMURA, Yataro OBATA
    1963 Volume 27 Issue 2 Pages 121-127
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.121
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    From the eggplant fruits, chlorogenic acid, neochlorogenic acid and caffeic acid have been isolated and identified. Enzymic experiments show that their O-dihydroxyphenolic compounds can be the browning substrates in the fruit flesh, on the other hand chlorogenic acid accelerates the decoloration of nasunin (delphinidin-glycoside) and enables to decolorize pelargonidin-3-glucoside by the anthocyanase.
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  • Cell Bound α-Amylase in Aspergillus oryzae
    Part III. Fixation of Exocellular α-Amylase to Mycelia
    Kenzo TONOMURA, Katsumichi IWAMA, Fusae FUTAI, Osamu TANABE
    1963 Volume 27 Issue 2 Pages 128-132
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.128
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    It has been found that exocellular α-amylase could be fixed to mycelia of Aspergillus oryzae at an acidic pH region and fixed α-amylase was released reversely at an alkaline pH region. The fixation has more remarkably been observed in mycelia obtained from a phosphate deficient medium where endocellular accumulation of α-amylase occurs more easily than in an ordinary mycelia which secrete a large amount of α-amylase into medium. Bound form of α-amylase was more resistant to low pH and less active than the free form. The results appear to support the previous suggestion that a large quantity of endocellular α-amylase might be located on mycelial surface of the mold.
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  • Studies on the Polymorphism of L-Glutamic Acid
    Part V. Crystallization of L-Glutamic Acid in β-form
    Yoshiki SAKATA, Hiromasa MARUYAMA, Kuniharu TAKENOUCHI
    1963 Volume 27 Issue 2 Pages 133-142
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.133
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    The β-crystal formation of L-glutamic acid in the seeded solution was investigated; and it was found that the growth rate of the seed crystals in a-axis direction was nearly as large as that of the α-crystal, but the growth rate in b- and c-axes was little recognized. The activation energy of the crystallization process of the β-crystal in a-axis direction was calculated from the growth rate constants determined at various temperatures, and 6-7kcal/mol was obtained. On the assumption that the crystallization of β-crystal growth was controlled by the diffusional operation, the thickness of the laminar film was calculated from the growth rate constant and the estimated value of the diffusional constant. The calculated value of the thickness was much greater than the value reported by Nernst; therefore, the crystallization process should be controlled by the surface reaction. The co-existence of a small quantity of amino acids caused a great reduction in the growth rate of the β-crystal.
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  • Methylation of Heparin, Heparitinsulfate, and Hexa, Tetra and Trisaccharides from Hyaluronic Acid
    Konoshin ONODERA, Shigehiro HIRANO
    1963 Volume 27 Issue 2 Pages 143-149
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.143
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    The methylations of heparin, heparitinsulfate, and three oligosaccharides (hexa, tetra and trisaccharides) from hyaluronic acid were carried out. Theoretical amounts of methoxyl group were obtained from the oligosaccharides and the desulfated product of carboxylreduced heparitinsulfate, but not from heparin and heparitinsulfate. The acid hydrolysis of the methylated trisaccharide confirms that the structure is β-D-glucopyranosyl uronic acid-(1→3)-2-acetamido-2-deoxy-β-D-glucopyranosyl-(1→4)-D-glucopyranosyl uronic acid.
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  • Syntheses of Halophenyl-γ-iodopropargyl Ethers which have High Antifungal Activity
    Shigeo SEKI, Ken NISHIHATA, Tadayuki NAKAYAMA, Hiroshi OGAWA
    1963 Volume 27 Issue 2 Pages 150-151
    Published: 1963
    Released on J-STAGE: February 07, 2011
    DOIhttps://doi.org/10.1271/bbb1961.27.150
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