Abstract:
:An extremely thermostable UDP-GlcNAc pyrophosphorylase has been purified from Thermus caldophilus GK24 by chromatographic methods including ion-exchange, hydrophobic interaction, and affinity chromatographies. The specific activity of the enzyme was enriched 41.8-fold, with a recovery of 2%. The molecular mass of the enzyme was 41 kDa by SDS/PAGE and 45 kDa by gel-filtration chromatography. The activity was maximum at 86 degrees C and its half-life at 95 degrees C was 30 min. Its optimum pH was 6.9 in the presence of Mg2+ ions. A biochemical study showed that UDP-GlcNAc pyrophosphorylase activity could be enhanced by fructose 1-phosphate, a precursor of UDP-GlcNAc. The enzyme showed a broad substrate specificity with sugar 1-phosphates, including glucose 1-phosphate, GlcNAc-1-P and xylose 1-phosphate. The enzyme was therefore named UDP-sugar pyrophosphorylase. The N-terminal and internal peptide sequences were determined and compared with known sequences from various sources. It was found that N-terminal sequence is similar to that of UDP-GlcNAc and UDP-glucose pyrophosphorylases from other bacterial sources.
journal_name
Biotechnol Appl Biochemjournal_title
Biotechnology and applied biochemistryauthors
Kim JS,Koh S,Shin HJ,Lee DS,Lee SYsubject
Has Abstractpub_date
1999-02-01 00:00:00pages
11-7eissn
0885-4513issn
1470-8744journal_volume
29 ( Pt 1)pub_type
杂志文章abstract::This paper is concerned with the optimization of submerged culture conditions for mycelial growth and exo-biopolymer production by Auricularia polytricha by one-factor-at-a-time and uniform design (UD) methods. First, the one-factor-at-a-time method was adopted to investigate the effects of environmental factors (i.e....
journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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