Enzymic synthesis of L-lysine from DL-alpha-amino-epsilon-caprolactam by new microbial strains
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
6816706
DOI
10.1007/bf02876448
Knihovny.cz E-zdroje
- MeSH
- amidohydrolasy metabolismus MeSH
- azepiny metabolismus MeSH
- Cryptococcus enzymologie MeSH
- fosfáty farmakologie MeSH
- glukosa farmakologie MeSH
- isomerasy aminokyselin metabolismus MeSH
- kaprolaktam metabolismus MeSH
- lysin biosyntéza MeSH
- Pseudomonas enzymologie MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- amidohydrolasy MeSH
- aminocaprolactam racemase MeSH Prohlížeč
- azepiny MeSH
- fosfáty MeSH
- glukosa MeSH
- isomerasy aminokyselin MeSH
- kaprolaktam MeSH
- L-alpha-amino-epsilon-caprolactamase MeSH Prohlížeč
- lysin MeSH
The production of L-lysine from DL-alpha-amino-epsilon-caprolactam (DL-ACL) by new strains producing L-alpha-amino-epsilon-caprolactamase and aminocaprolactam racemase is described. Optimal conditions for hydrolysis of L-ACL by Cryptococcus sp. and for racemization of ACL by cells of a strain isolated in nature and identified as Pseudomonas sp. were determined. Synthesis of L-alpha-amino-epsilon-caprolactamase is induced by DL-ACL or L-lysine with the same effectivity. A positive effect of phosphates (potassium salts) on reduction of the induction lag was detected, the synthesis of this enzyme was found to be repressed by glucose and some possibilities of the reversion of this repressive effect were demonstrated. Under conditions optimal for the production of both enzymes a quantitative theoretical conversion of 10% aqueous DL-ACL to L-lysine by a mixture of native cells in a mass ratio of 1 : 2 (producer of ACL-hydrolase to producer of ACL-racemase) occurred in 8 h at 40 degrees C and pH 8.0.
