[Biochemical response of recombinant Hansenula polymorpha strains to oversynthesis of homologous dioxyacetone kinase and bacterial beta-galactosidase]. / Biokhimicheskii otvet rekombinantnykh shtammov Hansenula polymorpha na sverkhsintez gomoloichnoi dioksiatsetonkinazy i bakterial'noi beta-galaktozidazy.
Prikl Biokhim Mikrobiol
; 32(1): 110-5, 1996.
Article
en Ru
| MEDLINE
| ID: mdl-8637840
ABSTRACT
Changes in the activities of key enzymes responsible for utilization of methanol by recombinant strains of methylotrophic yeasts H. polymorpha R22-2B and H. polymorpha LAC-56 grown in a chemostat are described. The strain R22-2B displaying a high activity of dioxyacetone kinase had also a high activity of formaldehyde dehydrogenase, which increased the rate of dissimilation of formaldehyde. There was a decrease in ATP concentration in the strain LAC-56 oversynthesizing beta-galactosidase from Escherichia coli; this effect decreased the rate of assimilation of formaldehyde.
Buscar en Google
Bases de datos:
MEDLINE
Asunto principal:
Pichia
/
Beta-Galactosidasa
/
Glicerol Quinasa
Idioma:
Ru
Revista:
Prikl Biokhim Mikrobiol
Año:
1996
Tipo del documento:
Article