Nippon Nōgeikagaku Kaishi

Cellular Localization and Properties of Glutaminase in Aspergillus oryzae

Atsumi TERAMOTO, Masao ISHIGE, Takeshi FURUYA, Kazuo UCHIDA, Hiroshi Y ...

1985Volume 59Issue 3 Pages 245-251
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.245

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About 30% of intracellular activity of glutaminase in Aspergillus oryzae No. 27 was found in free form and the remaining activity in bound form. During protoplast formation, mycelium glutaminase was released in the solubilized cell wall fraction. Glutaminase activity in lysed protoplasts was about 500-fold lower than that found in the solubilized cell wall fraction. These data indicate that most glutaminase was located at the cell surface, including the cell wall and the periplasm. Therefore we presume that intracellular free glutaminase exists in the periplasm or is bound loosely to the cell wall and that the intracellular bound glutaminase is bound tightly to the cell wall. The intracellular free form of glutaminase was definitively different from intracellular bound glutaminase in sensitivity to sodium chloride and sodium fluoride, and in recovery after acetone treatment at different pH values

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Isolation and Identification of Chitinolytic Bacteria

Yasuyuki TAKIGUCHI, Noriaki NAGAHATA, Kenzo SHIMAHARA

1985Volume 59Issue 3 Pages 253-258
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.253

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A screenig test was carried out for chitin-decomposing bacteria which assimilated native chitin as the sole carbon source. In 484 samples from soil, fresh water and sea water, 7 strains of chitinolytic bacteria were isolated. E-139 and E-383 a which exhibited the highest chitin-liquefying activity were identified as Pseudomonas aeruginosa and Vibrio anguillaurm, respectively.
These strains dissolved decalcified prawn cuticles in the medium in 3 or 4 days.
E-383 a exhibited-higher chitin-saccharifying and β-N-acetylglucosaminidase activities than E-139.

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Rheological Factors in Alcoholic Fermentation of Grains Heated at Low Temperature

Nobuya MATSUMOTO, Osamu FUKUSHI, Hajime YOSHIZUMI

1985Volume 59Issue 3 Pages 259-264
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.259

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Rheological studies were conducted on suspensions of ground maize, non-glutinous rice, rye, milo, glutinous rice, small fox-tail millet, barnyard millet and common millet with an amylograph. The transition temperature of the maize suspension (yellow dent) was 75°C, and at temperatures above 85°C the viscosity increased dramatically. The maximum viscosity occurred at 93°C. The Theological characteristics of maize suggest that heating below 85°C produces a mash viscosity suitable for transportation.

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Small Scale Alcoholic Fermentation of Grains Heated at Low Temperature

Nobuya MATSUMOTO, Osamu FUKUSHI, Hajime YOSHIZUMI

1985Volume 59Issue 3 Pages 265-269
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.265

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The relationship between cooking conditions and fermentation was investigated on a small scale with maize, milo, non-glutinous rice, small fox-tail millet, barnyard millet and common millet. Fermentation of the maize (yellow dent) mash cooked at low temperature (80°C) was equal to that of mash cooked at 120°C. Low temperature cooking was also successfully carried out on a plant scale in pilot studies. It was estimated that low temperature cooking on an industrial scale would reduce energy consumption by about 50% compared with conventional high temperature (140_??_180°C) cooking.

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Industrial Scale Alcoholic Fermentation of Maize Heated at Low Temperature

Nobuya MATSUMOTO, Osamu FUKUSHI, Osamu FUKUDA, Shigeru INOUE, Hajime Y ...

1985Volume 59Issue 3 Pages 271-277
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.271

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Industrial scale alcoholic fermentation was induced in maize (yellow dent) by low temperature heating (80°C). The mash volume was approximately 120 kl per mashing unit. The results were compared with a conventional high temperature cooking system (140°C). The fermentation efficiency of the low temperature cooking system was equal to that of the high temperature cooking system. The low temperature cooking system reduced heavy fuel oil consumption by about 40%.

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Repression of the By-Product in Enzymatic Production of L-Aspartic Acid

Hideaki YUKAWA, Terukazu NARA, Masato TERASAWA, Yoshihiro TAKAYAMA

1985Volume 59Issue 3 Pages 279-285
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.279

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Conditions were investigated for a high yield of L-aspartic acid by thermal inactivation of intracellular fumarase. The optimal concentrations were established for inactivation of fumarase without a decrease in aspartase activity. Both L-aspartic acid and calcium chloride protected against thermal inactivation of aspartase activity in intact cells. The residual activity of intracellular fumarase was negligible. After the cells were incubated at 45°C for 5 hr in a mixture consisting of 2 (mol) ammonia, 750 (mM) calcium chloride and 0. 08 (%, w/v) detergent Tween 20. Treatment for inactivation of intracellular fumarase resulted in stabilization of intracellular aspartase.

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Oxidative Dimerization of α-Pyran

Hideo ETOH, Atsuko NISHIYAMA, Kazuo INA, Masanobu IGUCHI

1985Volume 59Issue 3 Pages 287-290
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.287

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Oxidative coupling of α-pyran (1) was examined. Oxidation of α-pyran (1) with manganic tris-(acetylacetonate) resulted in cleavage of the pyran skeleton to three diene dimers (5a, 5b and 6). On the other hand, treatment of α-pyran (1) with vanadium tetrachloride and anodic oxidation gave pyran dimers (7a_??_c and 8a, 8b), respectively.

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Development of the Noncooking and Low Temperature Cooking Systems for Alcoholic Fermentation of Grains

Nobuya MATSUMOTO, Hajime YOSHIZUMI, Susumu MIYATA, Shigeru INOUE

1985Volume 59Issue 3 Pages 291-299
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.291

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[title in Japanese]

[in Japanese]

1985Volume 59Issue 3 Pages 327-329
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.327

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[title in Japanese]

[in Japanese]

1985Volume 59Issue 3 Pages 329-331
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.329

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[title in Japanese]

[in Japanese]

1985Volume 59Issue 3 Pages 331-333
Published: 1985
Released on J-STAGE: November 21, 2008

DOIhttps://doi.org/10.1271/nogeikagaku1924.59.331

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