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[Catalytic properties of induced L-lysine-alpha-oxidase].

Authors
  • Potapova, O L
  • Smirnova, I P
  • Vesa, V S
  • Bykova, O M
  • Laugalene, N F
Type
Published Article
Journal
Voprosy medit︠s︡inskoĭ khimii
Publication Date
Jan 01, 1992
Volume
38
Issue
1
Pages
9–13
Identifiers
PMID: 1441300
Source
Medline
License
Unknown

Abstract

Regulation of biosynthesis of L-lysine-alpha-oxidase from Trichoderma sp using biostimulators was studied. Specific activity of L-lysine-alpha-oxidase was increased 2.7-fold in presence of biostimulators; this occurred due to induction of the enzyme, properties of which were described previously. Catalytic and physico-chemical properties of the enzyme studied were not altered after addition of stimulators into the cultivation medium of the producing strain. Small amounts of L-lysine-alpha-oxidase isozyme were detected in the medium during cultivation; the isozyme was less active and had lower molecular mass as compared with the enzyme studied.

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