<P>A putative D-lyxose isomerase from Dictyoglomus turgidum was purified with a specific activity of 19 U/mg for D-lyxose isomerization by heat treatment and affinity chromatography. The native enzyme was estimated as a 42 kDa dimer by gel-filtr...
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https://www.riss.kr/link?id=A107661823
2012
-
SCI,SCIE,SCOPUS
학술저널
1079-1085(7쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
<P>A putative D-lyxose isomerase from Dictyoglomus turgidum was purified with a specific activity of 19 U/mg for D-lyxose isomerization by heat treatment and affinity chromatography. The native enzyme was estimated as a 42 kDa dimer by gel-filtr...
<P>A putative D-lyxose isomerase from Dictyoglomus turgidum was purified with a specific activity of 19 U/mg for D-lyxose isomerization by heat treatment and affinity chromatography. The native enzyme was estimated as a 42 kDa dimer by gel-filtration chromatography. The activity of the enzyme was highest for D-lyxose, suggesting that it is a D-lyxose isomerase. The maximum activity of the enzyme was at pH 7.5 and 75°C in the presence of 0.5 mM Co(2+), with a half-life of 108 min, K(m) of 39 mM, and k(cat) of 3,570 1/min. The enzyme is the most thermostable D-lyxose isomerase among those characterized to date. It converted 500 g D-xylulose/l to 380 g D-lyxose/l after 2 h. This is the highest concentration and productivity of D-lyxose reported thus far.</P>
Construction of an expression system for the secretory production of recombinant 관-agarase in yeast.
Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans.
A hydrophilic and hydrophobic organic solvent mixture enhances enzyme stability in organic media.