The RNAs having template activities were extracted from soluble fraction of the cotyledons of soybean seeds. These were consisted of two major components, 9s and 18s (High molecular weight RNA, H-RNA). Both components have template activities in the E. coli S-30 system. H-RNA was found in the precipitate fraction when the so-called soluble fraction was centrifuged for 2hr at 198, 000×g. H-RNA increased remarkably in kernels during ripening process and seems to be preserved in the seeds.

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A protease from the lotus seed (Nelumbo nucifera Gaertn) was purified by acid-treatment, ammonium sulfate-fractionation, ethylalcohol-fractionation, TEAE-cellulose-treatment and Sephadex G-100gel-filtration.
The enzyme was purified about 870-fold and was homogeneous in electrophoretic and ultracentrifugal analyses.
Purified lotus seed protease is an acid protease with a pH optimum at 3.8 toward urea-denatured casein. It is active for casein and hemoglobin. But other proteins such as edestin, zein, lotus seed globulin and soybean casein are slightly hydrolyzed and egg albumin is hardly hydrolyzed. This enzyme is most stable at pH 4.0 below 40°C. The enzyme is not a thiol protease, and its activity was completely inhibited by potassium permanganate, remarkably inhibited by sodium dodecylsulfate and accelerated by hydrogen peroxide.

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The growth of M. japonica in hexadecane or decane medium was markedly improved by dialysis culture and there existed a “growth-inhibitory factor” in the dialyzable material. This material inhibited the growth in hydrocarbon medium but not in glucose containing medium. Free fatty acids excreted extracellularly by dialysis culture in hexadecane medium were mostly palmitic, myristic and lauric acids in the culturing chamber, but almost exclusively lauric acid was found in the dialyzable material. These acids, assimilated themselves by the organism, inhibited the growth in hexadecane medium but did so only weakly in glucose. It was concluded that lauric acid was at least partly an active principle of “growth-inhibitory factor” in the dialyzable material in hexadecane medium.

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Some properties and kinetics of yeast nucleotide pyrophosphatase were studied in comparison with those of 5'-nucleotidase.
It was concluded that the two enzyme activities exist in a single protein molecule, though their active sites are not completely identical.

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As xylanase-producing microorganisms, 64 strains belonging to the genus Streptomyces were isolated from the barn-yard manures, silages and litters collected in Hokkaido district. Among these isolates the strain 102-1-4, which was found to be a new species under taxonomical studies and named Streptomyces xylophagus nov. sp., had the most outstanding ability for the enzyme production. In addition to the isolates, 38 strains of Streptomyces and 480 strains of filamentous fungi which have been preserved in our culture collection were also examined on their ability to produce the enzyme. 1) Among the strains of Streptomyces tested, only two strains, St. albogriseolus IAM 0031 and St. olivaceus IAM 0025 were found to have the ability, but their abilities were less than that of St. xylophagus nov. sp. 2) Out of 480 strains of fungi tested, Chaetomium, Schyzophyllum, Trametes, Echinodontium, Alternaria, Cepharosporium, Cercospora, Gibberella, Glomerella and Macrosporium produced the enzyme. Especially, Ch. trilaterale 2264 was the most excellent.

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6-Pentyl-α-pyrone, 6-propyl-α-pyrone and 4-decenoic acid-δ-lactone were prepared, and the nature of their flavors was investigated. Unsaturated lactones having the best flavorous nature as a butter or butter cake flavor among the lactones having double bond at various site, were 2-ene-δ-lactones which have a double bond at the α-position of the lactone ring and α-pyrones which have two double bonds at the α- and γ-positions. The flavor of 4-deceno-δ-lactone which has a double bond at the γ-position was the worst of them.

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Heat induced changes in solubility of casein against Ca ion and micelle stabilizing ability of k-casein were observed. Solubility of whole casein solution containing some additives against Ca ion showed characteristic changes by heating for 30min at 80°_??_150°. Closely resembled changes were observed in ability of k-casein which stabilize α₈-casein against Ca ion by heating at 80°_??_140°. Presence of some additives in k-casein accelerated the depression of stabilizing ability. α₈-Casein became less sensitive to precipitation by Ca ion with higher heating temperature. These results indicate that heat induced changes in solubility of whole casein have close relation with changes in stabilizing ability of k-casein and Ca sensitivity of other casein components.

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When 10^-3M cysteine solution was irradiated in the presence of glucose at the concentration of ten-fold of cysteine, the G-values of products produced from cysteine were similar to those from 10^-3M cysteine solution. On the other hand, the yield ofcarbonyl compound from glucose was suppressed completely by interaction between cysteine and radicals which are secondarily produced from glucose.
Methionine could not suppress the yield of carbonyl compound from glucose, and, Gvalues of products from methionine varied in comparison with those from solution containing methionine only.
From the results using e^-aq scavenger, it was concluded that oxidation to methionine sulfoxide and cleavage to α-aminobutyric acid was caused by OH and e^-_aq attack, respectively.

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The induced formation of uricase by the cultured cells of Streptomyces sp. and the effect of purine bases on the enzyme formation were studied. The microorganism was grown in media containing urate and/or purine bases (adenine, guanine, hypoxanthine or xanthine) and the development of the uricase activity of the cells were measured at intervals. The disappearance of urate and purine bases from the media was also determined. Without the purine bases, the production of uricase was significantly low even in the presence of urate and the disappearance of urate from the medium was in a slow rate. Upon the addition of hypoxanthine or xanthine in the presence of urate, a significant increase in the uricase activity of the cells and a concomitant rapid decrease of urate in the medium were observed. The purine bases added to the media were incorporated into the cells at a relatively early period of the culture and appeared to be converted into urate within the cells. The repression of uricase formation in the cultured cells and the derepression by the addition of the purine bases were discussed.

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Siolipin has shown three biological activities; (1) hemolytic action for rabbit erythrocyte, (2) acceleration of fibrin clot formation, (3) antibacterial activity on Bacillus subtilis PCI-219 grown on a synthetic medium (1%glucose, 0.1%KH₂PO₄, 0.1%(NH₄)₂HPO₄, 0.5%NaCl, 0.04%MgSO₄•7H₂O, 1.5%agar). The antibacterial activity of siolipin was reversed by L-histidine, L-cysteine etc.

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With all glucobioses (eleven types) as acceptors, Leuconostoc mesenteroides (NRRL B-512) was grown on a sucrose medium. The trisaccharides produced were analyzed for their yields, and the trisaccharide structures were determined after separation on a column.
The yield of the tri-and higher-saccharides indicated that isomaltose (28%) was the most efficient acceptor and maltose (24%) was next. With the other eight glucobioses, oligosaccharides were obtained in 3_??_15% yield. Among these sugars, α, β-trehalose (15%) and β, β-trehalose (11%) were efficient acceptors next to maltose, but α, α-trehalose was inert.
In every case, except for cellobiose, α-glucosyl transfer occurred to the position 6 of non-reducing moiety of glucobiose.
The sugars produced contained five new trisaccharides which were isolated as pure compounds.

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This paper deals with the contribution of protein components in soybean seeds to the physical properties of tofu-gel. Results obtained in tofu-making, using crude 11S and 7S components from defatted soybean meal, indicated that there presented significant difference between tofu-gels from crude 11S and 7S, namely, the tofu-gel from crude 11S was remarkably harder than that from crude 7S. And it has been recognized that the proportion of 11S to 7S in total protein of soybean seeds considerably differed among varieties and that the difference of the proportion might be related to the physical properties of tofu-gel prepared.

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In order to obtain fungous myrosinase, Aspergillus sydowi IFO 4284 was cultured on a medium containing mustard seed extract for 2 weeks. Myrosinase in the broth was purified about 150 fold by precipitation with ammonium sulfate and chromatography on DEAE-cellulose and DEAE-Sephadex. Comparison of thioglucosidase and sulfatase activities of the myrosinase preparation using pH-activity, pH-stability and temperature-stability curves revealed no differences from each other. The chromatograms of the two activities on DEAE-Sephadex showed good agreement. Consequently, the myrosinase produced by Aspergillus sydowi was concluded to be a single β-thioglucosidase, not a mixture of thioglucosidase and sulfatase.

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Tne effects of various reagents on Aspergillus sydowi myrosinase were studied.
The enzymatic activity was stimulated by cobalt (II), zinc (II) and magnesium ions and inhibited by mercury (II), iron (II) and copper (II) ions. However, metal-complexing agents, SH reagents and diisopropylfluorophosphate showed no effects on enzymatic activity. In contrast to plant myrosinase, this enzyme was neither activated nor inhibited by any concentrations of L-ascorbate. Glucose and salicin were competitive inhibitors for the enzyme. High concentrations of sodium chloride inhibited the enzyme.
From the inhibition modes of sugars and β-glucosides and from that of sodium chloride against the enzyme, _??_ similarity of the enzyme to, β-glucosidases was shown.

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β-Glucosidase activity of fungous myrosinase was confirmed using p-nitrophenyl β-glucoside as a substrate. This activity was revealed to be due to the myrosinase itself. Experimental results indicated a resemblance of fungous myrosinase to β-glucosidases similar to plant myrosinase. The relationship between fungous and plant myrosinases to the β-glucosidases are discussed from the view of the substrate specificity of these enzymes. The conclusions are that distinction between plant and fungous myrosinases and the β-glucosidases are not as strict as previously thought, and the myrosinases should be considered β-glucosidases highly specialized for the hydrolysis of mustard oil glucoside.

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As already reported, Corynebacterium hydrocarboclastus S10B1 was able to accumulate a good deal of L-glutamate in a thiamine-deficient medium at the sole expense of n-alkanes, but unable to form L-glutamate in a thiamine-sufficient medium though an abundant cell growth was observed.
α-Ketoglutaric acid and DL-alanine were found to be produced in the same thiamine-deficient medium in which L-glutamate was accumulated. Both products formed from n-tetradecane by this organism were isolated from culture broth, purified and identified. The optimum concentration of thiamine in the culture medium was 3 to 5μg per liter for their production. The maximum yields of α-ketoglutaric acid and DL-alanine reached 16 g and 1.5g per liter in the calcium carbonate-added medium, respectively. However, the addition of more than 30μg per liter of thiamine extremely repressed their accumulation.

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The change of salt distribution of skimmilk during frozen storage at -7°C and its reversion after thawing were investigated. Losses of ultrafiltrable calcium, inorganic phosphate and citrate were indicated. A part of insolubilized calcium and citrate reversed to a soluble form after thawing, but insolubilized phosphate hardly reversed when the storage period was prolonged. Comparison on the changes in skimmilk and in its dialyzate suggested that the insolubilization of salt constituents in milk due to frozen storage involved the interaction of these constituents with calcium caseinate phosphate complex.

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