L-lysine biosynthesis with the strain Corynebacterium glutamicum 10-20/60. Non-standard nitrogen sources.
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چکیده
منابع مشابه
Fermentative Production of Lysine by Corynebacterium glutamicum from Different Carbon Sources
Production of lysine by Corynebacterium glutamicum (PTCC 1532) from different agricultural by-products (molasses and pulpy waste date) was compared to glucose as raw materials. For this purpose, ammonium sulphate was selected as a constant nitrogen source. The effect of different nitrogen sources was also investigated with glucose as a constant carbon source. The production of L-lysine was exam...
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The aromatic amino acids are synthesized via a common biosynthetic pathway. A tryptophan-producing mutant of Corynebacterium glutamicum was genetically engineered to produce tyrosine or phenylalanine in abundance. To achieve this, three biosynthetic genes encoding the first enzyme in the common pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DS), and the branch-point enzymes chor...
متن کاملLysine uptake and exchange in Corynebacterium glutamicum.
Resting cells of Corynebacterium glutamicum (ATCC 13032) accumulate [14C]lysine by a transport system with a relatively high affinity (10 microMs) and a low maximum velocity (0.15 nmol/min per mg [dry weight]). Uptake of lysine was not inhibited by uncouplers or by ionophores affecting the ion gradients and the energetic state of the cell. Analysis of intracellular amino acid concentrations dur...
متن کاملEngineering of Corynebacterium glutamicum with an NADPH-generating glycolytic pathway for L-lysine production.
A sufficient supply of NADPH is a critical factor in l-lysine production by Corynebacterium glutamicum. Endogenous NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) of C. glutamicum was replaced with nonphosphorylating NADP-dependent glyceraldehyde 3-phosphate dehydrogenase (GapN) of Streptococcus mutans, which catalyzes the reaction of glyceraldehyde 3-phosphate to 3-phosphoglycer...
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ژورنال
عنوان ژورنال: Kvasny Prumysl
سال: 1985
ISSN: 0023-5830
DOI: 10.18832/kp1985007