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Volume 30, Issue 11
Displaying 1-18 of 18 articles from this issue
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Part V. Degradation of Desthiobiotin by MoldsShojiro IWAHARA, Seigo TAKASAWA, Tatsurokuro TOCHIKURA, Koichi OGATA1966 Volume 30 Issue 11 Pages 1069-1075
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSDuring the course of the study on the production of biotin from desthiobiotin by microorganisms, the present authors have found that some strains of molds produced an unknown biotin-vitamer (BS-factor) from desthiobiotin. The present investigation was undertaken to clarify the characteristics of the unknown vitamer. The unknown vitamer produced from desthiobiotin was isolated in crystalline form from culture filtrate of Aspergillus oryzae. The compound isolated was identified as 4-methyl-5-(w-carboxybutyl)-imidazolidone-2 by the physico-chemical procedures.View full abstractDownload PDF (403K) -
Part VI. Biosynthesis of Biotin-Vitamers by Resting Cell System of Bacillus sphaericusShojiro IWAHARA, Tatsurokuro TOCHIKURA, Koichi OGATA1966 Volume 30 Issue 11 Pages 1076-1082
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSThe biosynthesis of biotin-vitamers by resting cell system of Bacillus sphaericus was studied.
It was found that pimelic acid was essential substrate in biosynthesis of biotin-vitamers and that some amino acids and organic acids stimulated the biosynthesis of biotin-vitamers from pimelic acid. Alanine was found to be most effective. It was assumed that, in the presence of pimelic acid, some amino acids, especially alanine, and some organic acids play an important role in the biosynthesis of biotin-vitamers.
The main component of the biotin-vitamers synthesized by the resting cell system was identified as desthiobiotin. The existence of a small amount of unknown biotin-vitamer, an avidin-uncombinable substance, which was assumed to be 7-keto-8-amino-pelargonic acid, was also observed. True biotin was hardly observed in any conditions tested.View full abstractDownload PDF (415K) -
Hiroshi HYODO, Ikuzo URITANI1966 Volume 30 Issue 11 Pages 1083-1086
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSThe marked increase in o-diphenol oxidase activity which developed in incubating slices of sweet potato roots was suppressed by administration of actinomycin D, puromycin and blastcidin S. This suggests that the rise in enzyme activity resulted from de novo synthesis of enzyme protein during incubation. The formation of component III of o-diphenol oxidase which occured in response to cutting, was strongly inhibited by supplying the above chemicals.View full abstractDownload PDF (224K) -
Akio NOBUHARA, Masanao MATSUI1966 Volume 30 Issue 11 Pages 1087-1089
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESS2, 4-Decadien-l-ol and 2, 4-dodecadien-l-ol were synthesized from n-caproaldehyde and caprylaldehyde, respectively and their flavors were shown to be similar to those of chicken meat and chicken fat.View full abstractDownload PDF (204K) -
Part II. Amino Acid Composition, Carbohydrate Component and Some Physical PropertiesNoboru TOMIZUKA, Yasuhide OTA, Koichi YAMADA1966 Volume 30 Issue 11 Pages 1090-1096
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSThe amino acid composition of the purified extracellular lipase from Candida cylindracea was determined by ion-exchange chromatography with the use of an automatic amino acid analyzer, and a high content of hydrophobic amino acid residues was found. The enzyme was a glycoprotein, in which mannose and xylose were contained as carbohydrate com-ponents. Physical properties of the enzyme were the sedimentation coefficient of 4.7×10-13 (cm/sec.)/(dyne/g), the partial specific volume of 0.76ml/g and the intrinsic viscosity of 0.085dl/g, and its molecular weight was discussed.View full abstractDownload PDF (414K) -
Kenji SAKAGUCHI, Shozo KOTANI, Hidekazu SUGINAKA, Yoshiyuki HIRACHI, S ...1966 Volume 30 Issue 11 Pages 1097-1101
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSSeveral species belonging to the genera Pediococcus and Brevibacterium, which have resistant cell walls against the usual cell-disrupting methods, were effectively attacked by new cell-wall lytic enzymes, L3, ti, and ALE which were obtained from a Streptomyces sp., a Flavobacterium sp., and a Staphylococcus sp., respectively. Among them, the L3 enzyme was mostly effective to all pediococcal and brevibacterial strains.View full abstractDownload PDF (228K) -
Part VII. Flavor Components of Manufactured Green TeaTei YAMANISHI, Akio KOBAYASHI, Atsuko UCHIDA, Yoko KAWASHIMA1966 Volume 30 Issue 11 Pages 1102-1105
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSThe essential oil from manufactured green tea was separated into carboxylic, phenolic, carbonyl and alcoholic fractions and analysed by gas chromatography.
Seventeen alchols, two carbonyls, seven acids and two phenolic compounds were identified on the basis of their relative retention times and aroma of effluents by comparing with authentic compounds.
The quantities of these compounds were also determined by gas chromatography.
Four alcohols (present in rather high amounts), two caronyls, three esters and two phenols have remained unidentified.View full abstractDownload PDF (196K) -
Part III. Synthesis and Structures of N-AryloxyacylazolesMichihiko OCHIAI, Toshiya KAMIKADO1966 Volume 30 Issue 11 Pages 1106-1111
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSWith the aim of obtaining plant growth regulators, we have synthesized 1-aryloxy-acylbenzimidazoles, 1-aryloxyacylindazoles, 2-aryloxyacyl-4, 5, 6, 7-tetrahydroindazoles and 1-aryloxyacylbenzotriazoles by the acylation of azoles, and I-aryloxyacyl-4, 5, 6, 7-tetrahydro-indazoles by the reaction of aryloxyacylhydrazines with 2-(hydroxymethylene)cyclohexanone. The structures of these compounds are discussed on the basis of nuclear magnetic re-sonance data.View full abstractDownload PDF (273K) -
Part I. On the Enyzmatic Inactivation of Colistin by Bacillus colistinusMikiko ITO, Tokujiro AIDA, Yasuo KOYAMA1966 Volume 30 Issue 11 Pages 1112-1118
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSColistinase, an enzyme inactivating colistin, which appeared in a fermented broth of Bacillus colistinus attending with decay of colistin production was studied. The enzyme was partially purified and also chromatographed by DEAE-cellulose column. It was a heat labile, mostly basic protein, had optimum pH at 9.0 and was active against peptide anti-biotics such as colistin and polymyxin and also against casein. Bacterial proteinase, Nagarse, exhibited colistinase activity exclusively among tested proteinases and immunochemical studies revealed that colistinase was identical with bacterial proteinase Nagarse.View full abstractDownload PDF (1265K) -
Part III. Endo-polygalacturonase of Aspergillus saitoiMakari YAMASAKI, Tsuneo YASUI, Kei ARIMA1966 Volume 30 Issue 11 Pages 1119-1128
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSEndo-polygalacturonase (endo-PG) of Aspergillus saitoi was purified through ammonium sulfate fractionation, Amberlite IRC-50 column chromatography, and several combinations of Sephadex column chromatography.
The purified endo-PG, which was almost homogeneous ultracentrifugally and electro-phoretically, had the sedimentation constant of 2.2 S and the absorption maximum at 277mμ. Its optimum pH and temperature were 4.8_??_5.0 and 45°C, respectively, and it was most stable between pH 4.0 and 6.0, but over 90% of the activity was lost at 50°C for 10 min.
The purified enzyme was a typical endo-PG, and hydrolyzed about 60% and 17% of glycosidic linkage of polygalacturonic acid and pectin, respectively. This enzyme preparation had no pectinesterase, trans-eliminase, and apple juice-clarifying activities, but macerated potato tuber slices singly.View full abstractDownload PDF (3061K) -
Takashi NARA, Toshio KOMURO, Masanaru MISAWA, Shukuo KINOSHITA1966 Volume 30 Issue 11 Pages 1129-1132
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSWhen a fermentation medium consisting of the high concentration of K2HPO4 and KH2PO4 and glucose as a sole carbon source is autoclaved in the alkaline side, an unknown sugar is formed. This sugar is identified as psicose by paper chromatography and high-voltage paper electrophoresis. The notion that weak alkali causes the isomerization of reducing sugar could account for the formation of psicose in the medium. It is thus concluded that psicose is chemically formed from glucose in the alkaline side and in the high concentration of K2HPO4 and KH2PO4 during autoclaving.View full abstractDownload PDF (229K) -
Kyoko SAIO, Tokuji WATANABE1966 Volume 30 Issue 11 Pages 1133-1138
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSWith the purpose of separation and isolation of protein bodies from soybean, soybean seeds were homogenized in oil and fractionated by successively adjusting densities of extracts with carbon tetrachloride. Isolated protein bodies consist of about 10% nitrogen, 0.8% phosphorus, 8.5% sugar, 7% ash and 0.5% RNA. Over 93% of protein in the bodies is found as particle-bound protein which is insoluble in 15% Carbowax 6000 solution but soluble in 10% sodium chloride solution. Protein bodies in intact cells, isolated bodies and those treated with Carbowax 6000 solution were respectively observed by electron-microscopy.View full abstractDownload PDF (2617K) -
Hiroshi ONISHI, Toshiyuki SUZUKI1966 Volume 30 Issue 11 Pages 1139-1144
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSThe polyalcohol production from the pentoses such as D-xylose, L-arabinose and D-ribose by various genera and species of yeasts was examined. Candida polymorpha dis-similated aerobically these three pentoses and produced xylitol from D-xylose, L-arabinitol from L-arabinose and ribitol from D-ribose at good yield of 30_??_40% of sugar consumed. The result suggests that these polyalcohols would be major products from pentoses by yeasts, but some unidentified minor polyalcohols were also produced.View full abstractDownload PDF (302K) -
Masaaki UCHIYAMA, Masamichi OHHASHI, Masanao MATSUI1966 Volume 30 Issue 11 Pages 1145-1151
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSThe condensation of acetylsalicylchloride with the morpholine enamine of cyclohexanone in the presence of triethylamine gave an adduct which was converted into tetrahydro-xanthone (X) by treating with aqueous pyridine containing piperidine. The reaction was applied to condensation of the pyrrolidine enamine (VI) of 6, 7-dimethoxychroman-3-one with acetyl tubaic acid chloride to afford dehydrorotenone (II).View full abstractDownload PDF (373K) -
Part I. Structure of HeliangineShinobu IRIUCHIJIMA, Shimpei KUYAMA, Nobutaka TAKAHASHI, Saburo TAMURA1966 Volume 30 Issue 11 Pages 1152-1163
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSThe evidences which allow to assign the partial structures (a, b and c) for heliangine, C20H26O6, are described. The chemical and spectroscopic data obtained for this compound are interpreted in terms of the structure I, which has been preliminarily proposed by the authors, as well as of the structure II established by X-ray analysis conducted by Nishikawa et al.View full abstractDownload PDF (764K) -
Part XV. Some Physicochemical Properties and Substrate Specificity of Neutral Protease of Bacillus subtilis var. amylosacchariticusDaisuke TSURU, Heizo KIRA, Takehiko YAMAMOTO, Juichiro FUKUMOTO1966 Volume 30 Issue 11 Pages 1164-1169
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSSome physical and chemical properties and substrate specificity were investigated of the neutral protease obtained from B. amylosacchariticus, a strain of saccharogenic a-amylase-producing Bacillus subtilis. The molecular weight and sedimentation coefficient of the pro-tease were estimated to be 33, 800 and 3.02, respectively, by ultracentrifugal analyses, and alanine was identified as an amino-terminal amino acid of the enzyme by the Sanger's method. The enzyme showed more broad specificity than the neutral protease of liquefying α-amylase-producing B. subtilis, when tested with synthetic peptides, and hippuryl-L-leucin-amide was the best substrate among 42 compounds tested. On a long incubation, the enzyme hydrolyzed several proteins in a degree of 10 to 25% as peptide bond cleavage.View full abstractDownload PDF (1249K) -
Part IV Sialic Acid Content of Some Biological MaterialsKonoshin ONODERA, Shigehiro HIRANO, Hiroko HAYASHI1966 Volume 30 Issue 11 Pages 1170-1172
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSDownload PDF (168K) -
Katsumi IMADA, Kiyoshi SATO, Shunichiro OGA, Kazuo ASANO1966 Volume 30 Issue 11 Pages 1173-1174
Published: 1966
Released on J-STAGE: November 27, 2008
JOURNAL FREE ACCESSDownload PDF (89K)
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