The comformational change of the 11S component of soybean proteins in alkali was measured by ultraviolet difference spectra, optical rotatory dispersion and circular dichroism. The abnormal tyrosyl residues of the 11S component were classified into two types. The first type was normalized when the pH was increased above 11.0, but the second type could not be exposed at pH 12.70. The behavior of the a₀ value in Moffitt-Yang equation suggested that the secondary and tertiary structure of the 11S component were stable, partially. From the cotton effect and CD spectra, it was found that the partially stable secondary structure was a β-structure.

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The conformational change of the 11S component of soybean proteins in acid was measured by ultraviolet difference spectra, optical rotatory dispersion and circular dichroism. Below pH 4, the change of tertiary structure that the tyrosine residues were exposed and the tryptophan residues were barried into the molecule was recognized, and, between pH 2 and 0.64, the change was attained to maximum. The secondary structure, β-structure, of the 11S component was almost stable at pH 1.22.

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Total solid, carbohydrate, and organic acid contents of passion fruit juice were 16.97%, 12.36% and 2.13%, respectively, indicating that carbohydrates and organic acid contents in total solid were 77% and 13% respectively.
The contents of votatile substances obtained by distillation under a reduced pressure from juice were 36ppm. These were separated into acidic fraction and neutral fraction consisting of ester, alcohol and carbonyl compounds. The acid fraction was methylated with diazomethan and the neutral one was saponificated after treatment with saturated sodium bisulfide. Both components were investegated by gas liquid chromatography.
Fourteen peaks were detected from an acid fraction and 43 peaks from a neutral one. Major compounds of these peaks wear assumed as follows: as acids, acetic, propionic, n-butyric and n-caproic, as esters, ethyl butyrate, n-butyl caproate, n-hexyl butyrate, bornyl acetate, n-hexyl caproate and as alcohol, iso-hexyl alcohol, n-hexyl alcohol and DL-α-phenyl ethyl alcohol. Ester and alcohol occupied in the neutral fraction about 92% and 7% respectively, but carbonyl compounds were undetected.

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When seeds of various species were treated with hydrogen peroxide solution, the seeds were inflated in their particular ways, as described in the previous paper.
In order to elucidate the mechanism of the inflation of the seeds, this work has been carried out using peanuts, soybeans, corn, broad beans, and red beans.
The following mechanism is proposed on this phenomenon,
(1) Process of the inflation of the seeds:
Hydrogen peroxide solution, at first, permeates into the seeds through the hilum, embryo, and seed coat, then is decomposed to water and oxygen gas by catalase in the seeds. The oxygen gas which is accumulated in the space between the seed coat and the endosperm, inflates the seeds without the permeation of water into the seeds.
(2) Rate controling factors:
A factor controling the rate of the inflation is the permeability of the seed coat to hydrogen peroxide solution. The extent of the permeability is proportional to the rate of the inflation. Second rate determining factor is the velocity of loosening of the seed coat, when the seed coats of different kinds of seeds show the same extent of permeability.
In spite of the fact that catalase plays an essential role in the inflation, it is not a rate determining factor. It was found by microscopic work that the cytohistological differences of the seed coats were closely related to the rate of inflation.

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The shifting of protein and lipid was investigated from whole soybean to liquid and cream layers of soybean milk according to the isolating method of globular membrane protein from cow milk. Almost lipid, but only few percent of the protein, were shifted to the cream layer and the protein was corresponded to the specific band 5, 10 and 11 on the starch gel electrophoretical pattern (with urea) of whole soybean protein.
Emulsifying capacity of water extract and acid precipitated protein was increased by heating and the heat coagulated protein fraction of the acid precipitated protein was similar to the proteincontained in the cream layer on the gel electrophoretical pattern. Also, the emulsifying capacity of each fractionated protein was investigated and the protein fraction like albumin showed the highest increasement of the capacity by heating.

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The bacteria which produced the enzyme hydrolysing soybean carbohydrates, were screened and identified as Bacillus subtilis sp. The enzyme of this strain was partially purified by DEAESephadex A-50 and Sephadex G-100. The characteristics of the enzymes of B. subtilis No.17 were as follows; The optimum temperature is 37°C, optimum pH is 4.5 to 6.0 The enzyme was stable at less than 37°C, about 60% of the initial enzyme activity remained after it kept 20 hours at pH 6.0. The enzymatic hydrolysate fractionated on Sephadex G-15 column did not contain galactose or arabinose, but the fractions hydrolysed by 1.0N HCl constituted from galactose and arabinose.

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The method is based on the glucose oxidase and catalase reaction, in which the oxidation ofβ-glucose is catalyzed specifically, with subsequent consumption of oxygen. The oxygen consumption was determined by oxygen consumption meter provided with a polarographic platinum electrode with collodion membrane.
For the determination of sucrose, β-fructofuranosidase was used in order to hydrolyze sucrose to glucose and fructose in 0.1M phosphate buffer solution (pH 5.8). This solution was heated in a boiling water bath for one minute to complete the mutarotation of glucose.
The amount of sucrose was calculated from the amount of glucose derived from sucrose determined by the oxygen consumption meter.
The recovery of glucose and sucrose from soft drinks was 96-103% and 98-102%, respectively. Commercial soft drinks were analyzed by this method.

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