The colored compound produced by the reaction of periodate oxidation product of quinic acid with sodium nitroprusside and piperazine can be used as a quantitative measure of the quinic acid. The curve is linear for the acid examined in the range of 25 to 150μg of quinic acid per 1ml. Hence, the reaction provides a convenient method for the determination of the micro quantities of quinic acid obtained from tobacco extracts fractionated by chromatography on paper or ion exchange-resin column. The content of quinic acid in flue-cured tobacco was 0.23 per cent to dry matter.

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The quaternary system K₂SO₄-MgSO₄-Mg(OH)₂-H₂O and the associated systems (a) K₂SO₄-Mg(OH)₂-H₂O and (b) MgSO₄-Mg(OH)₂-H₂O were investigated at 100° Though isotherm (a) exhibited nothing new, isotherm (b) exhibited basic magnesium sulfate, MgSO₄-5Mg(OH)₂•3H₂O, as the solid phase. The solid phases of quaternary isotherm were the new basic triple salt K₂SO₄•2MgSO₄•Mg(OH)₂•2H₂O, Iangbeinite, basic magnesium sulfate, kieserite and potassium sulfate.

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1) The microbiological transformation of 17α-hydroxydesoxycorticosterone to hydrocortisone, epi-hydrocortisone, 17α, 19-dihydroxy-desoxycorticosterone and minor unknown products by Corticium sasakii (Shirai) Matsumoto, has been demonstrated.
2) The above hydroxy-derivatives of the steroid were produced to the same degree by the resting-cell method as by the growing-cell method.
3) The steroid oxidizing activity of this fungus was stable and parallel with the weight of the mycelium.
4) As one of the medium components, several sugars were examined, starches, sucrose and glucose being found suitable for fungus growth. During incubation the hydrogen-ion concentration of the medium hardly shifted, regardless of the kind of sugars.

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As a part of the studies intending to clarify biological significance of the presence of acylase, enzymatic activity which hydrolyzes acyl amino acids, its activity in yeast was investigated. As 4 results, the occurrence in yeast of acylase activity was confirmed for the first time.
In order to study the enzymatic properties of this acylase activity, experiments were carried out with the enzyme preparation from brewer's yeast. As a result of the investigation, yeast acylase was found to be able to hydrolyze a number of acyl amino acids, of these chloroacetyl derivatives especially readily, as in the case of previously studied acylase activity in other sources such as mold acylase. Several observations on the influence of metal ions and inhibitors, optical specificity and others were also presented.

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Condensation of piperonal with diethyl piperonylsuccinate afforded α-(3, 4-methylenedioxy-phenyl-hydroxymethyl)-β-(3, 4-methylenedioxybenzyl)-succinic acid, m. p. 173_??_5°C. Dehydration with p-toluenesulfonic acid or acetic anhydride gave two kinds of α-piperonylidene-β-piperonyl succinic anhydrides, m. p. 167-8°C and 115-7°C, respectively. Reduction of α-piperonylidene-β-piperonyl-succinic acid thioethyl methyl ester by Raney Ni catalyst followed by saponification and lactonization afforded α, β-dipiperonyl butyrolactone, m. p. 107_??_8°C, and a small amount of α-piperonylidene-β-piperonyl-butyrolactone, m. p. 154_??_5.5°C.

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In order to elucidate the genetic background of sugar metabolism by Aspergillus oryzae, three kinds of metabolic mutants were prepared by induced mutation. Though these mutant strains generally produced a few ferric chloride-positive substance, it is not yet known whether the substance is a precursor of kojic acid or not. The heterocaryons between a kojic acid producer and a hetero-fermentative-type strain produced kojic acid in the same amount as the parental producer, while the heterocaryons between a kojic acid producer and a respiratory-type strain produced a less amount of kojic acid. Selection of fitter-type nuclei during the course of propagation is considered to be a possible reason.

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A crystalline substance (Factor-D), by which the activity of Factor-E in promoting the germination of rice plant seeds could be increased synergistically, was isolated from the active crude syrup from which Factor-E was also isolated. This Factor-D has been proved by synthesis to be 1-methyl-2, 4-imidazoledione (1-methyl hydantoin). This substance has not been isolated from culture filtrates of any microorganisms.

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Both rennet and pepsin are used as a coagulant in cheese-making process. The proteolytic action of these two milk-coagulating enzymes was studied. In this report, results of the experiments on the development of the opalescence in sodium-caseinate solution by two enzymes are reported. Some properties of the opalescent materials and the change in the distribution of nitrogen and phosphorus are also included.
These experiments show the difference of the mode of proteolytic action on casein by rennet and by pepsin, which may be concerned with the ripening of cheese.

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In order to decide whether or not, the chemical properties of myosin B extracted, isolated, and prepared from rabbit, veal, cow, and horse meat have been altered during aging, experiments were carried out on salting out, viscosity, ATP-sensitivity, and the AT-Pase of myosin B solution.
The results obtained are as follows:
(1) Salting out experiments showed that there is no difference of myosin B to be observed in accordance with the kinds of animals tested. However, in the salting out procedure of AMS and AML solutions, the concentration of ammonium sulfate at the maximum precipitating region was found to be different. The concentration of ammonium sulfate in the salting out of myosin B was altered with the aging of meats; especially, in the case of AMS the maximum precipitating region seemed to approach that of myosin.
(2) Among all the kinds of animal meats tested, intrinsic viscosity of AML was higher than that of AMS, and intrinsic viscosity of myosin B was altered with the aging of meats. Intrinsic viscosity of the myosin B solution seemed to be different according to the kind of meat, i, e., that of myosin B from rabbit being high, while that obtained from cow meat was low.
(3) The ATP-sensitivity of AML was higher than that of AMS. The ATP-sensi-tivity of AMS became very low as aging proceeded. From this result, it was considered that AMS turns to assume a high ratio of myosin in the constitution of actomyosin, and comes to resemble myosin during aging.
(4) With the aging of meats, the optimum pH for ATPase of myosin B from rabbit and veal meat turned to the acidic side. At the neutral optimum pH, enzymatic activity showed a tendency to decrease during aging. Immediately after slaughter, the activity of ATPase of AMS became higher than that of AML, but the inverse relation was maintained during aging process.
Immediately after slaughter, the optimum pH for enzymatic activity of AMS from rabbit were found to be 7.3 and 10.2, activity at pH 10.2 being higher than that at pH 7.3. However no difference was observed at both of these pH values in ATPase activity of AMS from veal immediately after slaughter.

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(1) When samples containing E. coli irradiated with gamma-ray were incubated at 37°C or 25°C, no difference on the survival of the strain was observed in both cases and the same survival was also recognized in case of the preserving procedure carried out in an icebox for 24 hours prior to incubation at 37°C.
(2) Prior to gamma-ray irradiatien, when the strains incubated at 37°C for 24 hours were preserved in an ice-box at 0°C for a period as long as 23 days, no difference on gamma-ray resistivity of the strain was found. However, the survival obtained from the strain stocked at room temperature, 18°C, for a period as long as 24 days was higher than that of the strain stocked for a shorter period.
(3) There was no difference on survival of E. coli at the concentration of 10² cell/ml caused by gamma-ray irradiation, when the medium also contained heat sterilized cells of the same strain at the concentration of 10⁷ cell/ml.
(4) No difference on survival of E. coli was caused by gamma-ray irradiation, when the medium contained glucose, lactose or fructose in the amount of 8%.
(5) The survival obtained from the medium at the pH value of 6.4 adjusted with HCL was almost identical with that of the pH 7.0 medium. However, when the pH value of the medium decreased to 6.1, survival obtained from the medium was higher than that in the medium of pH 7.0 or 6.4.
(6) When tartaric acid, citric acid or succuic acid was added to each medium, the survival-ratios obtained from the medium containing one kind of the chemicals were higher than that of the normal medium containing no organic acid. In these cases, tendencies of such protective effects as previously mentioned were more distinct than in the case of the medium containing HCL at the same pH value, 6.1.

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The soluble enzyme preparation which can synthesize L-ascorbic acid from D-glucuronic acid, D-galacturonic acid and diacetone-2-keto-L-gulonic acid was obtained from green peas seedling. During dialysis of this preparation, a loss of activity was however caused and it was irreversibly generated by any addition of the dialyzed solution, boiled enzyme solution and boiled yeast extract. The experiments were carried out without dialysis and further purification. The active fraction showed its sedimentation constant as s_t =2.2×10^-13, indicating a relatively lower molecular weight of protein.
The optimum pH and temperature of the soluble enzyme was pH 5.8-6.2 and 33° respectively. The enzyme was relatively stable at 50° for a short period of heating, but was rapidly inactivated at 100° Inhibition was observed with iodoacetate, CuCl₂ and HgCl₂; KCN and also NaF slightly inhibited at 10^-3M, while 2, 4-dinitrophenol showed no inhibition to this preparation.

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