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Biomedical subjects

I Chibata

Publications and source records attributed to I Chibata.

At least 37 records · Page 2Linked to original sources
PubMed1980

Evaluation of an infusion solution enriched with branched chain amino acid in parenteral nutrition of rats.

Nutritional effects of an infusion solution enriched with branched chain amino acids (BCAAs) were investigated with young adult rats. Continuous infusion through a central venous cannula was carried out for 7 days with three kinds of solutions: 1) 21.8% glucose (S-1); 2) 18.6% glucose plus 2.50% amino acids based on human milk pattern (S-2), and 3) 18.6% glucose plus 2.58% amino acids enriched with BCAAs (S-3). Rats received daily 50 ml of the solution, containing 45 kcal and 200 mg N in S-2 and S-3. The body weights of rats in the S-2 and S-3 groups were only slightly reduced, while those of the S-1 group were extremely reduced. The rats were in positive nitrogen balance in the S-2 and S-3 groups on days 2-7. Its value was somewhat, but not significantly, larger in the S-3 group than in the S-2 group. The plasma BCAA levels determined 15 minutes after the end of infusion were higher in the S-3 group than in the S-2 group, but there was no significant difference except for the leucine level. The urinary levels of creatinine and 3-methylhistidine, the plasma levels of urea and glucose, and liver lipid content were similar in the S-2 and S-3 groups. The plasma albumin level was somewhat higher in the S-3 group than in the S-2 group. The present data suggest that an infusion solution enriched with BCAAs served to maintain the normal rats in desirable nutritional status.

Amino Acids↗
PubMed1980

Transductional construction of an isoleucine-producing strain of Serratia marcescens.

Strain GIHVLr6426 was isolated as an isoleucine hydroxamate-resistant mutant from the wild-type strain of Serratia marcescens Sr41. This mutant had high activities of threonine deaminase and acetohydroxyacid synthase, both of which were insensitive to feedback inhibition. Genetic analysis revealed that strain GIHVLr6426 carried two regulatory mutations located in the ilv region. Strain T-693, a threonine-producing strain which was previously reported to carry four regulatory mutations for threonine biosynthesis, had an increased activity of acetohydroxyacid synthase. Transductional analysis revealed that one of the four mutations carried by strain T-693 was responsible for constitutive synthesis of both isoleucine and threonine biosynthetic enzymes. Strain GIHVLr6426 into strain T-693. The constructed strain had the six regulatory mutations for threonine and isoleucine biosyntheses, and produced about 25 mg isoleucine ml-1 in a medium containing sucrose and urea.

Genes, Regulator↗
PubMed1980

Excretion of glutathione by methylglyoxal-resistant Escherichia coli.

A methylglyoxal-resistant mutant of Escherichia coli B excreted glutathione into the growth medium, especially during growth on medium containing methylglyoxal. In the presence of methylglyoxal, the total amount of glutathione excreted was increased about 50-fold over that of the wild-type strain. The resistant mutant had high activities of two enzyme systems: a glutathione-forming enzyme system (consisting of gamma-glutamylcysteine synthetase and glutathione synthetase) and a glyoxalase system (consisting of glyoxalase I and glyoxalase II). Methylglyoxal resistance appeared to be due to the simultaneous increase in the activities of these two enzyme systems.

Drug Resistance, Microbial↗
PubMed1980

Production of l-Glutamine by a Penicillin-Resistant Mutant of Flavobacterium rigense.

To establish a practical method for the fermentative production of l-glutamine, cultural conditions for the accumulation of a large amounts of l-glutamine were investigated by using Flavobacterium rigense 703, which was previously reported by us as a l-glutamine-producing mutant. As a result, a yield of 25 mg of l-glutamine per ml was obtained after a 48-h cultivation in a medium containing glucose, yeast extract, (NH(4))(2)-fumarate, KH(2)PO(4), K(2)HPO(4), MgSO(4).7H(2)O, and CaCO(3) (pH 6.4). Accumulation of l-glutamine was dependent upon the concentration of (NH(4))(2)-fumarate, and a suboptimum growth at a relatively high concentration of (NH(4))(2)-fumarate was essential for the maximum production of l-glutamine. At the optimum conditions, glutamic acid was formed as a by-product at a concentration of less than 1 mg/ml, but accumulation of the other amino acids was negligible. The product was isolated from the culture broth and readily purified by anion-exchange chromatography. The pure crystals of l-glutamine obtained in an 80% yield were optically and chromatographically pure.

Journal Article↗
PubMed1979

Immobilization of Escherichia coli cells containing aspartase activity with kappa-carrageenan. Enzymic properties and application for L-aspartic acid production.

Whole cells of Escherichia coli having high aspartase (L-asparate ammonialyase, EC 4.3.1.1) activity were immobilized by entrapping into a kappa-carrageenan gel. The obtained immobilized cells were treated with glutaraldehyde or with glutaraldehyde and hexamethylenediamine. The enzymic properties of three immobilized cell preparations were investigated, and compared with those of the soluble aspartate. The optimum pH of the aspartase reaction was 9.0 for the three immobilized cell preparations and 9.5 for the soluble enzyme. The optimum temperature for three immobilized cell preparations was 5--10 degrees C higher than that for the soluble enzyme. The apparent Km values of immobilized cell preparations were about five times higher than that of the soluble enzyme. The heat stability of intact cells was increased by immobilization. The operational stability of the immobilized cell columns was higher at pH 8.5 than at optimum pH of the aspartase reaction. From the column effluents, L-aspartic acid was obtained in a good yield.

Ammonia-Lyases↗
PubMed1979

Immobilization of aminoacylase by adsorption to tannin immobilized on aminohexyl cellulose.

The immobilization of aminoacylase (N-acylamino acid amidohydrolase, EC 3.5.1.14) was investigated by using tannin immobilized on aminohexyl cellulose. The most active immobilized aminoacylase was obtained when aminoacylase was adsorbed to the immobilized tannin in a weak alkaline medium containing sodium chloride and n-butanol at 37 degrees C. The activity of the immobilized tannin-aminoacylase complex per unit volume was five times higher than that of the DEAE-Sephadex-aminoacylase complex used for industrial production of L-amino acids in our plants. The half-life of the immobilized tannin-aminoacylase complex was 20 days under continuous operation at a high concentration of substrate; on the contrary, that of the DEAE-Sephadex-aminoacylase complex was 0.5 days.

Adsorption↗
PubMed1979

Continuous production of NADP by immobilized Brevibacterium ammoniagenes cells.

Whole cells of Brevibacterium ammoniagenes IAM 1645 having the polyphosphate NAD-kinase were successfully immobilized in a polyacrylamide gel lattice. The immobilized cells were activated by treatment with organic solvents or detergents. The pH optimum of the immobilized cells for the production of NADP was 7.0, and divalent metal ions were required to maintain the elevated activity of polyphosphate NAD-kinase. Highly pure NADP was continuously produced in high yield by the immobilized cell column. The half-life of this column was about eight days.

Brevibacterium↗
PubMed1979

Immobilization of enzymes and microbial cells using carrageenan as matrix.

Conditions for the gelation k-carrageenan, which is a new polymer for immobilization of enzymes and microbial cells, were investigated in detail. k-Carrageenan was easily induced to gel by contact with metal ions, amines, amino acid derivatives, and water-miscible organic solvents. By using this property of k-carrageenan, the immobilization of enzymes and microbial cells was investigated. Several kinds of enzymes and microbial cells were easily immobilized with high enzyme activities. Immobilized preparations were easily tailor-made to various shape such as cube, bead, and membrane. The obtained immobilized preparations were stable, and columns packed with them were used for continuous enzyme reaction for a long period. Their operational stabilities were enhanced by hardening with glutaraldehyde and hexamethylenediamine.

Amidohydrolases↗
PubMed1979

Production of L-serine by Sarcina albida.

Conditions for the production of microbial L-serine hydroxymethyltransferase and for the conversion of glycine to L-serine were studied. A number of microorganisms were screened for their abilities to form and accululate L-serine from glycine, and Sarcina albida was selected as the best organism. Enzyme activity in this organism as high as 0.12 U/ml could be produced in shaken cultures at 30 degrees C in a medium containing glucose, ammonium sulfate, glycine, yeast extract, and inorganic salts. L-Serine was produced most efficiently by shaking cells at 30 degrees C in a reaction mixture containing 20% glycine, 5 X 10(-3) M formaldehyde, and 3 X 10(-4) M pyridoxal phosphate in yields of 22 mg of broth in 5 days. L-Serine was easily isolated in 84% yields by ion-exchange resin.

Bacteria↗
PubMed1979

L-Glutamine formation by Flavobacterium rigense.

A penicillin-resistant mutant of Flavobacterium rigense designated as strain 703, FERM-P no. 3628, was obtained after ultraviolet treatment of F. rigense FERM-P no. 3556. The parent strain produces 0-2-hydroxypropylhomoserine from 1,2-propanediol. The mutant was found to be a good producer of L-glutamine. The physiological characteristics of strain 703 were different from the general group of L-glutamic acid-producing bacteria. Strain 703 required L-tryptophan and thiamine but not biotin for its growth. L-Glutamine formation on a specific basis, however, was independent of L-tryptophan and thiamine. Biotin and penicillin were also not effective. Only ammonium fumarate acted as an effective factor on L-glutamine formation. Accumulation of L-glutamine by strain 703 was 10 mg/ml at 30 degrees C for 48 h in a chemically defined medium containing 3% diammonium fumarate.

Flavobacterium↗
PubMed1979

Stimulation of L-asparate beta-decarboxylase formation by L-glutamate in Pseudomonas dacunhae and Improved production of L-alanine.

The formation of L-asparate beta-decarboxylase by Pseudomonas dacunhae was compared on media containing a variety of organic acids and amino acids as a carbon source. Although the enzyme was formed constitutively when the organism was grown on basal medium or on that containing tricarboxylic acid cycle intermediates, it was induced twofold by L-glutamate and repressed one-tenth by L-serine. L-Glutamine, L-proline, L-leucine, glycine, and L-threonine also showed induction effects lower than that of L-glutamate. L-Glutamate derepressed the serine effect. This glutamate effect was observed effect was observed with other microoganisms, e.g., Achromobacter pestifer and Achromobacter liquidum. Since the intermediates from L-glutamate metabolism had no effect, this induction effect was specific to L-glutamate. The formation of some glutamate-related enzymes was measured and is discussed in relation to the formation of L-asparate beta-decarboxylase. L-Asparate beta-decarboxylase was purified to an electrophoretically homogenous state from L-glutamate-grown cells of P. dacunhae, and some properties were compared with those of the enzyme from fumarate-grown cells. The two enzymes were identical in disc electrophoresis, molecular weight, and some enzymatic properties. The industrial production of L-alanine from L-aspartic acid acid was improved by using the culture broth with highly induced L-asparate beta-decarboxylase (9.4 U/ml of broth).

Alanine↗
PubMed1979

Participation of lysine-sensitive aspartokinase in threonine production by S-2-aminoethyl cysteine-resistant mutants of Serratia marcescens.

S-2-Aminoethyl cysteine (AEC) reduced both growth rate and final growth level of Serratia marcescens Sr41. The growth inhibition was completely reversed by lysine. AEC inhibited the activity of lysine-sensitive aspartokinase to a lesser extent than lysine. The AEC addition to the medium lowered not only the level of lysine-sensite aspartokinase but also those of homoserine dehydrogenase and threonine deaminase, whereas lysine repressed the aspartokinase alone. To select mutations releasing lysine-sensitive aspartokinase from feedback controls, AEC-resistant colonies were isolated from strains HNr31 and HNr53, both of which were previously found to excrete threonine on the minimal plates but not on the plates containing excess lysine. Two of 280 resistant colonies excreted large amounts of threonine. Strains AECr174 and AECr301, derived from strains HNr31 and HNr53, respectively, lacked both feedback inhibition and repression of lysine-sensitive aspartokinase. These strains produced about 7 mg of threonine per ml in the medium containing glucose and urea.

Aspartate Kinase↗
PubMed1979

Transductional construction of a threonine-producing strain of Serratia marcescens.

A threonine-producing strain of Serratia marcescens Sr41 was constructed according to the following process. Thr- strain E-60 was derived from strain HNr59 having constitutive levels of threonine-sensitive aspartokinase and homoserine dehydrogenase. Thr+ transductant T-570 was constructed from strain E-60 and phage grown on strain HNr21 having feedback-resistant threonine-sensitive aspartokinase and homoserine dehydrogenase. This transductant lacked both feedback inhibition and repression for the two enzymes. Thr- strain N-11 was derived from strain AECr174 lacking feedback inhibition and repression of lysine-sensitive aspartokinase. Subsequently, the threonine region of strain T-570 was transduced into strain N-11. One of the THR+ transductants, strain T-693, produced markedly high levels of the two aspartokinases and homoserine dehydrogenase, which were insensitive to feedback inhibition. This strain produced about 25 mg of threonine per ml in the medium containing sucrose and urea.

Aspartate Kinase↗
PubMed1979

Conversion of Glycerol to Dihydroxyacetone by Immobilized Whole Cells of Acetobacter xylinum.

Enzymatic production of dihydroxyacetone (DHA) was studied by immobilization of the whole cells of acetic acid bacteria capable of oxidizing glycerol to DHA. Acetobacter xylinum A-9 cells immobilized in a polyacrylamide gel were selected as the most favorable enzyme preparation. The enzymatic properties of immobilized cells converting glycerol to DHA were investigated and compared with those of intact cells. The optimum pH for the immobilized cells was broad (4.0 to 5.5), whereas the intact cells had a narrow pH optimum at 5.5. The thermal stability of the immobilized cells was somewhat higher than that of the intact cells. Apparent K(m) values for glycerol with both intact and immobilized cells were about equal, 6.3 x 10 to 6.5 x 10 M. The complete conversion of glycerol to DHA was achieved within 40 h under optimum conditions, and pure crystalline DHA was readily isolated from the reaction mixture with over 80% yield.

Journal Article↗
PubMed1979

Plasma aspartate levels in rats following administration of monopotassium aspartate via three routes.

Plasma aspartate levels were measured after potassium aspartate administration through different routes to rats of various ages. The changes in plasma levels were most significant with intraperitoneal injection. Dose- and age-related responses to aspartate load were obtained. The present data suggest that a marked elevation of plasma aspartate levels may result in neuronal necrosis. By comparing the plasma aspartate levels with the results on hypothalamic lesion (Okaniwa et al., 1979), plasma peak value associated with the lesion was estimated in each case of various administration routes and rat ages.

Administration, Oral↗