A method for the determination of pyruvate carboxylase activity during the glutamic acid fermentation with Corynebacterium glutamicum

1999 ◽  
Vol 39 (1) ◽  
pp. 91-96 ◽  
Author(s):  
Davin Uy ◽  
Stéphane Delaunay ◽  
Jean-Marc Engasser ◽  
Jean-Louis Goergen
Keyword(s):  
Glutamic Acid ◽  
Corynebacterium Glutamicum ◽  
Pyruvate Carboxylase ◽  
Acid Fermentation ◽  
Carboxylase Activity

Importance of Phosphoenolpyruvate Carboxylase of Corynebacterium glutamicum during the Temperature Triggered Glutamic Acid Fermentation

1999 ◽  
Vol 1 (4) ◽  
pp. 334-343 ◽  
Author(s):  
S. Delaunay ◽  
D. Uy ◽  
M.F. Baucher ◽  
J.M. Engasser ◽  
A. Guyonvarch ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Corynebacterium Glutamicum ◽  
Phosphoenolpyruvate Carboxylase ◽  
Acid Fermentation

scholarly journals Effect of Pyruvate Carboxylase Overexpression on the Physiology of Corynebacterium glutamicum

2002 ◽  
Vol 68 (11) ◽  
pp. 5422-5428 ◽  
Author(s):  
Mattheos A. G. Koffas ◽  
Gyoo Yeol Jung ◽  
Juan C. Aon ◽  
Gregory Stephanopoulos
Keyword(s):  
Corynebacterium Glutamicum ◽  
Pyruvate Carboxylase ◽  
Carbon Sources ◽  
Acid Synthesis ◽  
Aspartate Kinase ◽  
Growth Enhancement ◽  
Lysine Production ◽  
Carboxylase Activity ◽  
Amino Acid Synthesis ◽  
Permeabilized Cells

ABSTRACT Pyruvate carboxylase was recently sequenced in Corynebacterium glutamicum and shown to play an important role of anaplerosis in the central carbon metabolism and amino acid synthesis of these bacteria. In this study we investigate the effect of the overexpression of the gene for pyruvate carboxylase (pyc) on the physiology of C. glutamicum ATCC 21253 and ATCC 21799 grown on defined media with two different carbon sources, glucose and lactate. In general, the physiological effects of pyc overexpression in Corynebacteria depend on the genetic background of the particular strain studied and are determined to a large extent by the interplay between pyruvate carboxylase and aspartate kinase activities. If the pyruvate carboxylase activity is not properly matched by the aspartate kinase activity, pyc overexpression results in growth enhancement instead of greater lysine production, despite its central role in anaplerosis and aspartic acid biosynthesis. Aspartate kinase regulation by lysine and threonine, pyruvate carboxylase inhibition by aspartate (shown in this study using permeabilized cells), as well as well-established activation of pyruvate carboxylase by lactate and acetyl coenzyme A are the key factors in determining the effect of pyc overexpression on Corynebacteria physiology.

scholarly journals Development of gluconeogenesis in neonatal rat liver. Effect of premature delivery

1967 ◽  
Vol 105 (3) ◽  
pp. 1229-1233 ◽  
Author(s):  
D. Yeung ◽  
I. T. Oliver
Keyword(s):  
Rat Liver ◽  
Pyruvate Carboxylase ◽  
Neonatal Rat ◽  
Assay Method ◽  
Premature Delivery ◽  
Carboxylase Activity ◽  
Significant Linear Correlation ◽  
Foetal Rat ◽  
Rapid Appearance

1. An assay method for the determination of phosphopyruvate carboxylase activity is described in which improved sensitivity is obtained by separation of the enzyme from interfering pyruvate kinase by zone sedimentation. 2. The molecular weight of rat liver phosphopyruvate carboxylase determined by zone sedimentation is about 68000. 3. Premature delivery of rat foetuses by uterine section results in the rapid appearance of phosphopyruvate carboxylase, but hexose diphosphatase and pyruvate carboxylase, already present in the foetal rat liver, are not significantly affected, and glucose 6-phosphatase activity is only slightly affected. 4. The rate of incorporation of [14C]pyruvate into glucose by liver slices is also greatly increased by premature delivery and there is a highly significant linear correlation between this process and the phosphopyruvate carboxylase activity.

Modeling the growth of Corynebacterium glutamicum under product inhibition in l-glutamic acid fermentation

2005 ◽  
Vol 25 (2) ◽  
pp. 173-178 ◽  
Author(s):  
Noor Salam Khan ◽  
Indra Mani Mishra ◽  
R.P. Singh ◽  
Basheshwer Prasad
Keyword(s):  
Glutamic Acid ◽  
Corynebacterium Glutamicum ◽  
Product Inhibition ◽  
Acid Fermentation

Enhanced L-glutamic acid production by immobilized Corynebacterium glutamicum X680 using Response Surface Methodology

2021 ◽  
Vol 16 (12) ◽  
pp. 87-94
Author(s):  
Subhadeep Ganguly ◽  
Smaranika Pattnaik
Keyword(s):  
Response Surface Methodology ◽  
Glutamic Acid ◽  
Response Surface ◽  
Corynebacterium Glutamicum ◽  
Acid Production ◽  
Immobilized Cells ◽  
Lower Amount ◽  
Acid Fermentation ◽  
Statistical Tool ◽  
Glutamic Acid Production

L-glutamic acid is a non-essential amino acid largely used as flavor enhancer and food additive. It also has several therapeutic applications. Fermentation has gained superiority over its chemical synthesis as it produced stereo-specific isomer. Corynebacterium glutamicum is mostly used microorganism for Lglutamic acid fermentation. The study was dealing with optimization of L-glutamic acid production by immobilized mutant Corynebacterium glutamicum X680 in calcium alginate beads using response surface methodology as effective statistical tool. Among several parameters studied, pH, inoculums size, incubation time, concentration of sodium alginate, agitation and cell:alginate ration showed the most significant effect. Immobilized cells produced significantly (p<0.01) lower amount of L-glutamic acid (24.3mg/ml) compared to the production by free cells (27.6mg/ml). However, reusability of the beads minimized production cost and hence conferred benefit as far as the market economy is concerned.

Improved Cleanup and Derivatization for Gas Chromatographic Determination of Monosodium Glutamate in Foods

1983 ◽  
Vol 66 (6) ◽  
pp. 1528-1531 ◽  
Author(s):  
Hiroshi Nakanishi
Keyword(s):  
Glutamic Acid ◽  
Acid Derivative ◽  
Monosodium Glutamate ◽  
Chromatographic Determination ◽  
Flame Ionization Detection ◽  
Gas Chromatograph ◽  
Flame Ionization ◽  
Acetone Water ◽  
Chromatographic Procedure

Abstract A gas chromatographic procedure is described for determining monosodium glutamate (MSG) in several types of food. A sample is extracted with acetone- water (1 + 1). Acetone is evaporated and an aliquot of the extract is buffered with 1M NH4OH-1M NH4CI pH 9 solution, and chromatographed directly on a column of QAE Sephadex A-25 that has been pretreated with the same buffer. MSG is eluted with 0.1N HC1, and a portion of the eluate is evaporated to dryness and reacted with dimethylformamide( DMF)-dimethylacetal to form the glutamic acid derivative, which is injected into a gas chromatograph and measured by flame ionization detection. Recoveries of MSG from sample fortified at 5-500 mg ranged from 92.8 to 100%.

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