As a counterwork for preventing phage growth in industrial L-glutamic acid fermen-tation, the screening of effective chemical agents was carried out. Of the sixty chemicals such as surface-active agents, antibiotics, organic acids, dyestuffs and others, citrate, oxalate and tri- or tetrapolyphosphate showed the selective inhibition for phage growth. The concentrations of these chemicals required to inhibit phage growth were 5×10^-2M for citrate or oxalate, and 0.l% for tri- or tetrapolyphosphate, respectively.
Application of these selected chemicals to L-glutamic acid fermentation resulted in the complete inhibition of phage growth without affecting on L-glutamic acid production. These results show that the addition of citrate, oxalate, sodium tri- or tetrapolyphosphate to the medium is a promising mean for preventing phage infection in the plant.

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Inhibitory action of sodium tripolyphosphate (Na-TPP) to P-phages growth was studied. Na-TPP had no phagicidal action, did not prevent adsorption of phage and inhibited for-mation of infected cells. Furthermore, no phase yield occurred when Na-TPP was added within 5 min of infection, but addition after that time resulted in normal phage growth. DNA synthesis of infected cells was blocked by Na-TPP added early in the latent period (within 5 min), but addition after that time failed to block its synthesis. RNA synthesis of infected cells was not affected even when Na-TPP was added at various times in the latent period. Furthermore, 72 per cent of 32P-labeled phage P-1 adsorbed in the medium containing Na-TPP was separated by the blendor treatment, but only 12 per cent was separated when adsorbed in the absence of Na-TPP. These results indicate that Na-TPP inhibits the injection of phage DNA into the host cell.

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F-1 β-glucan, the main component of water soluble non-starchy polysaccharides from naked barley endosperm, has been subjected to degradation with cellulases from Trichoderma viride and Trametes sanguinea. The former cellulase converted F-1 β-glucan to D-glucose, cellobiose, 4-O-β-laminaribiosyl-D-glucose and 4²-O-β-laminaribiosyl-cellobiose as main pro-ducts. From the latter preparation four fractions of cellulase were separated. Their hydrolysing mechanisms against F-1 β-glucan differed from each other. Thus, it was suggested that the hydrolysing mechanism of cellulase was different when its origin or fraction in the same origin differed.
Cellulase from Trichoderma viride was almost similar to those from Streptomyces spearated by Parrish et al. and from Aspergillus niger by Stone et al. about the hydrolysing mechanism on barley β-glucans, though a small difference was found.

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The electrophoretically pure preparation of cytochrome c from Thiobacillus thiooxidans was obtained. The absorption spectrum exhibited maxima at 415, 521 and 550mμ in reduced form. The various properties of the cytochrome were very close to these of mammalian cytochrome c, i. e., absorption spectrum, electrophoretic pattern, isoelectric point and E₀'.

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Electrophoretically homogenous preparation of NADPH-cytochrome c oxidoreductase was isolated from the soluble fraction of Thiobacillus thiooxidans. The purification of the enzyme was carried out using the fractionation with ammonium sulfate, the treatment with Amberlite IRC-50 and the disk electrophoresis.

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A mixture of 0.8M D-xylose and 0.8M glycine, when heated at 100°C, showed inhibi-tory effect against autoxidation of 40% ethanol solution of linoleic acid. The antioxidant activity increased in proportion to color intensity of browning reaction solution, whereas reductones formed during the browning process showed little contribution to the activity. Nondialyzable melanoidin fraction of browning solution also showed a positive activity. Consequently, it was considered that melanoidin pigment would play an important role in the antioxidant activity.

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In sterilized skim milk or sterilized l0% solution of dry skim milk at 120°C for 15 min, Lactobacillus bulgaricus, Lactobacillus helveticus and Streptococcus lactis were cultivated for 7 days at given temperature.
Both NCN (non casein type nitrogen) content and pH in each culture of lactic acid bacteria were rapidly decreased until 2 days after cultivation. But NCN content increased and the pH change got small after 3 days cultivation.
Caseins prepared from the cultures of these three kinds of lactic acid bacteria were examined electrophoretically. From the results of electrophoresis of these caseins, we have concluded that β-casein could be hydrolyzed by these lactic acid bacteria. And, it seemed that α-casein could not be hydrolyzed by these lactic acid bacteria.
Rennet easily hydrolyzed casein treated with L. bulgaricus and L. helveticus but hardly hydrolyzed that treated with S. lactis compared with control-casein. Caseins treated with L. bulgaricus and L. helveticus were hydrolyzed easier than control-casein.

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Particle weights of caseins prepared from fermented milk by lactic acid bacteria, Streptococcus cremoris, Streptococcus lactis, Lactobacillus bulgaricus and Lactobacillus helveticus, and of hydrolyzed casein by rennet, trypsin or pepsin were measured according to the light scattering experiment.
Particle weights of various treated caseins were larger than that of raw native casein at both pH 7.0 and 12.0. And the heating caused the polymerization of casein to large particle.

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The activity ratio of glucose isomerization to glucose-6-phosphate isomerization was practically constant during the course of purification of the enzyme, and it was impossible to separate the two isomerizing activities by means of Sephadex G-150 and DEAE-Sephadex column chromatographies. Furthermore, the similarlity in pH stability and thermal stability, and the competitive inhibition by 6-phosphogluconate were observed in both isomerizing reactions. In kinetic experiments, however, Michaelis constants (Km) were calculated to be 1.6M for the arsenate-requiring glucose isomerization, and 1.4×10^-3M for the glucose-6-phosphate isomerization. These results indicate that the arsenate-requir-ing glucose- and the arsenate-independent glucose-6-phosphate-isomerizing reactions are catalyzed by the same enzyme, and that the glucose-isomerizing enzyme is a glucose phosphate isomerase itself.

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Sweet potato starch, available commercially, was found to contain originally about 25mg% of the insoluble starch particles (ISSP), which could not be liquefied with bacterial alpha-amylase under the best known liquefaction process and remained as the residue.
Some of the sweet potato starch which is considered to be difficult to liquefy in dextrose manufacture, often contains about 60mg% of this material. The different species of starch are arranged in the increasing order to the ISSP content as follows: potato starch<sweet potato starch<rice starch<corn and wheat starch. The average amount of ISSP content in corn starch is about 229mg%.
By treating the sweet potato starch slurry at 55°_??_60°C, the ISSP content in the slurry was remarkably increased, and when potato starch (16% moisture) was heated in a pressure vessel with live steam of 115°_??_127°C, the ISSP content was increased to about 3000mg%. ISSP content of sweet potato starch was also increased by the liquefaction with bacterial alpha-amylase, when the operation temperature was between 70°_??_80°C.

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Antiphage properties of many kinds of chemicals such as antibiotics, surface-active agents and chelating agents were examined on Brevibacterium lactofermentum No. 2256-phage P465 system using double-layer agar method, as a part of the basic study, for pre-venting phage infection in the industrial fermentation.
A great majority of inhibitors which were selected were usually nonspecific and inhibited also bacterial growth. Among about 200 chemicals tested, 5 antibiotics such as chloramphenicol and tetracycline, 6 chelating agents such as phytic acid and 19 surface-active agents such as PEG monoester and POE alkyl ether showed the selective inhibitions for phage infection at the concentrations which did not affect bacterial growth, or at the subbactericidal concentrations that suppressed bacterial growth slightly.
Of the above chemicals which showed selective inhibitions for phage infection, a possible mechanism of chelating agents chiefly of phytic acid was investigated. When 0.1 to 0.2%, of phytic acid was present in the medium, the effect of inhibition was most remarkable; this could be applied to the actual phage-infected L-glutamic acid fermentation. Phytic acid had no direct phagocidal action, nor did it inhibit the late step of the phage multiplication; but it prevented the adsorption of phages, which required inorganic co-factors such as Mg²⁺ or Ca²⁺ in this step, to the host bacteria. Moreover, a part of the infected bacteria was made incapable of forming plaques in the presence of phytic acid. These results suggested that the chelation between Mg²⁺ or Ca
and phytic acid would remove the metal ions essential for phage adsorption and prevent the phage adsorption and infection of phage DNA, consequently, the phage infection.

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The effect of the non-ionic surface-active agents (SAA) on the infection of phage P465 of Br. lactofermentum was examined by adsorption and one-step growth experiments as a part of the basic study on the prevention of phage-infection in the industrial fermentation. Among various SAA tested, polyoxyethylene stearyl ether (POE-SE), polyethylene glycol monooleate (PEG-MO) and polyoxyethylene sorbitan monostearate (Tween 60) had remark-ably demonstrated the selective inhibition of phage infection.
The effect of the above three SAA was apparently restricted to the initial adsorption step of phage infection, for the phage already adsorbed would not be affected by exposure to SAA. However, the results of one-step growth experiment indicated that Tween 60 inhibited not only the phage-adsorption, but also the maturation of phage already adsorbed in the host cells. The rate of the inhibition was found to be directly related to the concentration of agent. And, the most effective adsorption-inhibition was exhibited at the critical micelle concentration of SAA. The concentration as used in our experiments did not affect the viability of either phages or the host cells.
The results also indicated that the inhibition of phage-adsorption was due to the action of SAA on the surface of the bacterial cells rather than on the phage. This is supported by the observation that preincubation of phage with SAA did not affect either the sub-sequent adsorption rate or the plaque-forming ability of the phage. In contrast with above, a short-term exposure of bacterial cells to SAA caused an apparent change to the cell surface which was only partially restored by washing repeatedly. Moreover, the inhibitory effect of SAA on phage-adsorption appears quite specific in the phage-host system.

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The influence of low casein diet on the pattern of in vivo incorporation of ³²P-ortho-phosphate into individual phosphatides of rat liver mitochondria was investigated.
The composition of the mitochondrial phosphatides showed no difference between low casein and high casein diet fed rats. On the contrary, incorporation of ³²P into lecithin was greater in rats fed a low casein diet than that in rats fed a high casein diet. The mean value was about three fold higher.

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A number of compounds structurally related to phenylphenols were systematically synthesized as herbicides. Some of nitro-substituted derivatives show strong activity in pre-emergence test. The herbicidal activity of this series appears to relate with the pK-value of the compound.

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Herbicidal activities of chloro-substituted phenylphenols were investigated. The de-rivatives of o-phenylphenol and p-phenylphenol exhibited different selective toxicity between radish and rice, the latter appeared to have a specific inhibitory activity against the root growth of rice. As an attempt to analyze the correlation of herbicidal activity and chemical structure, the dissociation constant and the substituent constant π were ap-plied in this investigation. The herbicidal activity correlated linearly with pK-value.

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The existence of the inactive precursors of yeast proteinases B and C was confirmed in the autolysate of baker's yeast and they were named as pro-proteinases B and C, re-spectively. The active and inactive forms of proteinase C were two distinct proteins, separable by chromatographical procedures. The two precursors were markedly activated by incubation at pH 5 or by treatment with denaturing agents, e. g. urea, dioxane, acetone and certain alcohols.
These activations were also observed with extracts from acetone-dried cells and from mechanically destructed cells, but the activation of proteinase A was not demonstrated under any conditions tested. Therefore, it was assumed that most of proteinases B and C exist in vivo as inactive precursors, whereas proteinase A originally exists in an active form.

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Pro-proteinase C, the latent form of yeast proteinase C, was partially purified from the autolysate of baker's yeast. It was strongly activated by incubation at pH 5 or by treatment with urea or dioxane. The former activation was prevented by treatment to inactivate yeast proteinase A, which coexisted with the pro-enzyme in the present prepa-ration, but was promoted by addition of purified proteinase A. Thus, it was confirmed that A could activate pro-proteinase C. Furthermore, it was found that activation could be caused by extremes in pH or by heating to 55_??_60°C, accompanied by the simultane-ous destruction of the enzyme produced. Pro-proteinase C was stable over a range of pH 5 to 8 after 60 min incubation at 50°C.

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Among the threonine dehydratase activities in liver of rat fed on basal diet (B-group), lysine added diet (L-group) and threonine added diet (T-group), a following relationship was found: AB_??_AL<AT, where AB, AL and AT were the activities of B-, L- and T-group, respectively. The types of the activity increase in L- or T-group were investigated by examining the possibility of the cause-the existence of activators in L- or T-group (I), the existence of inhibitors in B-group (II), the activation of the latent enzyme in L- or T-group (III), and the induction of the dehydratase by biosynthesis in L- or T-group (IV). Addition of various amounts of liver homogenate of L- or T-group to a given amount of that of B-group gave a result as would be obtained in cases where neither activators nor inhibitors existed in the liver (I and II). No correlationship was found between the activity and the preincubation time, which denied the presence of the latent enzyme which would easily change into the active form by preincubation (III). Actinomycin D administered to rats inhibited the increase of the dehydratase activity of L- or T-group by about 504 (IV). On the other hand, preliminary experiments using hypophysectomized or adrenal-ectomized rats showed the results of AB_??_AL_??_AT. Both results may suggest the possibility that the increase of the dehydratase activity is ascribed to the induction of this enzyme through biosynthesis, and perhaps through endocrine systems.

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In comparing the aroma concentrates from various types of black tea by the use of gas chromatography (GLC), differences of aroma pattern were recognized among these black tea of Ceylon, India, Peru, Formosa and Japan.
One of the typical differences, by which the variety would be characterized, appeared in the proportion of linalool (include its oxides) to geraniol and phenylethanol. Further-more the ratio of the total area of peaks before and after linalool seemed to have some relation with the variety of black tea.
Also, top note of black tea aroma was compared by head space vapor analyses.

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