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Volume 27, Issue 11
Displaying 1-10 of 10 articles from this issue
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Part V. The Fractionation of Pectolytic Enzymes of Coniothyrium diplodiella (1)Akira ENDO1963 Volume 27 Issue 11 Pages 741-750
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSExperiments have been made on fractionation of the pectolytic enzymes produced by Coniothyrium diplodiella. It has been observed that 30 to 35% of the polygalacturonase (PG) activity of the pectolytic enzymes of the said microorganism is salted out with ammonium sulfate, and this portion contains endo-PG I, endo-PG II and pectin esterase (PE)(with a trace of exo-PG). The endo-PG I accounts for 60 to 65% of the total PG activity, and the endo-PG II, 25 to 30%. Both types of endo-PG scarcely act on pectin, and hydrolyze pectic acid to the extent of 65 to 70%.View full abstractDownload PDF (943K) -
Part VI. The Fractionation of Pectolytic Enzymes of Coniothyrium diplodiella (2)Akira ENDO1963 Volume 27 Issue 11 Pages 751-757
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSOf the pectolytic enzyme produced by Coniothyrium diplodiella, examination has been made on the enzymatic composition of the portion which is not salted out with saturated ammonium sulfate. This portion accounts for 40 to 50% of the total polygalacturonase (PG) activity of such enzymes, and treatment with rivanol and chromatography on Duolite CS-101 and DEAE-cellulose disclosed the presence of two types, endo-PG III and exo-PG, which occupy 60 to 65% and 28 to 30% of the PG activity respectively. Endo-PG III hardly acts on pectin and hydrolyzes pectic acid by no more than 35 to 40% of the total glycosidic bonds. Exo-PG also acts on pectic acid and hydrolyzes it to the extent of 100%.View full abstractDownload PDF (747K) -
Part I. Genetic StudiesKin-ichiro ODA, Nobuyoshi IGUCHI1963 Volume 27 Issue 11 Pages 758-766
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSThe mutant strain X816 synthesizing protease and amylase at high rates was crossed with original strain K.S. which is characteristic of abundant sporulation and stable growth, for the purpose of breeding a new koji mold endowed with both parental merits. Diploid strains obtained from these crosses show the intermeadiate character in general both in the formation of these enzymes and in sporulation.
In this paper, the genetic characters of these diploid strains as well as the mode of changes of these enzyme activities during hybrid formation are described.View full abstractDownload PDF (965K) -
Part II. Biochemical Studies (1)Kin-ichiro ODA1963 Volume 27 Issue 11 Pages 767-772
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSThe mutant X816 synthesizing protease and amylase at high rates was isolated from original strain K. S. by the irradiation of X-ray.
In order to see whether the protease in this mutant is identical with the enzyme in original strain or it is more active enzyme. Studies have been made on the protease isolated from these strains. It was found that the mutant strain synthesized the enzyme protein twice as much as original strain did. And the enzyme appears to be identical with that in original strain with respect to specific activity, electrophoresis, heat sensitivity, sedimentation constant and the elution pattern on DEAE-cellulose chromatography.View full abstractDownload PDF (2507K) -
Part II. Taxonomical Studies on the Amino Acids-producing Bacteria from HydrocarbonsKoichi YAMADA, Joji TAKAHASHI, Kaetu KOBAYASHI1963 Volume 27 Issue 11 Pages 773-783
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSTaxonomical studies on ten strains of hydrocarbon-utilizing bacteria reported in previous paper, which produced various kinds of amino acid, were carried out. They were Achromobacter cycloclastes, Achromobacter delmarvae, Bacillus species, Corynebacterium species, Micrococcus species. Many of them were not identical with the species which are described in Bergey's Manual of 7th Edition.View full abstractDownload PDF (1260K) -
Part II. Identification of Lutease-Producing Streptomyces Strain No.OP-4-5 and Production of Lutease by the KnownNorio NAKAMURA, Osamu TANABE1963 Volume 27 Issue 11 Pages 784-788
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSExamination was made on the morphological and cultural characteristics of the lutease -producing Streptomyces strain No.OP-4-5 isolated from a dust. The strain was identified asStreptomyces griseus. In addition, it was proved that 2 strains of Streptomyces griseus producelutease in a test for lutease production in Streptomyces species. Streptomyces parvus and Streptomycesniveoruber also produce the same enzyme. However, production of the lutease by these4 strains was less than that of produced by Streptomyces griseus strain No.OP-4-5 which was isolated by the authors.View full abstractDownload PDF (2221K) -
Morifusa ETO, Yoshiro KINOSHITA, Takeshi KATO, Yasuyoshi OSHIMA1963 Volume 27 Issue 11 Pages 789-794
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSSeveral saligenin cyclic alkyl phosphates and phosphorothionates were prepared and theirinsecticidal activities were examined. 2-Methoxy-4H-1, 3, 2-benzodioxaphosphoran-2-one andits thiono analog are strong insecticides, the toxicities of which to a number of insects arealmost equal to or superior to parathion. They are less toxic to mouse than parathion.When the length of alkyl radical was increased, the insecticidal activity decreased.View full abstractDownload PDF (727K) -
Part VII. The Structure of a New Tropolone, NootkatinolYoshiyuki HIROSE1963 Volume 27 Issue 11 Pages 795-797
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSA new tropolone, nootkatinol, has been isolated from the wood of Juniperus rigida Sieb. et Zucc. It has been shown to possess the structure I.View full abstractDownload PDF (390K) -
Part II. Ozonolysis Products of Piericidin A DerivativesNobutaka TAKAHASHI, Akinori SUZUKI, Saburo TAMURA1963 Volume 27 Issue 11 Pages 798-805
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSOzonolysis of Hydropiericidin A diacetate gave an acetylated monohydroxy acid, C17H32-34 (OCOCH3)·COOH and its N-methoxycarbonyl amide, C17H32-34 (OCOCH3)·COOHOn the other hand, by ozonolysis of Piericidin A diacetate, an acid C9H12NO3·COOH wasobtained. On the basis of ultraviolet, infrared and NMR spectra and of chemical evidences, the structure (VI) or (VI') was presented to this acid. Thus, the structure (VII) or (VII') was proposed to Piericidin A.View full abstractDownload PDF (1132K) -
Part I. Detection and Purification of Acid-Stable Dextrinizing AmylaseYasuji MINODA, Koichi YAMADA1963 Volume 27 Issue 11 Pages 806-811
Published: 1963
Released on J-STAGE: February 07, 2011
JOURNAL FREE ACCESSWhen black Aspergilli were cultivated in appropriate condition, culture filtrate showeddextrinizing activity even after acid treatment such as pH 2.5, at 37°C for 30 minutes. Itsuggested the existence of acid-stable dextrinizing amylase. To isolate this enzyme paper electrophoreticprocedure was carried out and the spot which showed acid-stable dextrinizingactivity was obtained in addition to α-amylase and glucoamylase spots. This new amylasewas purified by fractional precipitation with ammonium sulfate, rivanol and acetone, and was obtained in a crystalline form.View full abstractDownload PDF (2170K)
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