Abstract：
:The araA gene encoding an L-arabinose isomerase (L-AI) from the acido-thermophilic bacterium Acidothermus cellulolytics ATCC 43068 was cloned and overexpressed in Escherichia coli. The open reading frame of the L-AI consisted of 1,503 nucleotides encoding 501 amino acid residues. The recombinant L-AI was purified to homogeneity by heat treatment, ion-exchange chromatography, and gel filtration. The molecular mass of the enzyme was estimated to be approximately 55 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified enzyme was optimally active at 75 degrees C and pH 7.5. It required divalent metal ions, either Mn(2+) or Co(2+), for both enzymatic activity and thermostability improvement at higher temperatures. The enzyme showed relatively high activity and stability at acidic pH. It exhibited over 90% of its maximal activity at pH 6.0 and retained 80% of activity after 12 h incubation at pH 6.0. Catalytic property study showed that the enzyme had an interesting catalytic efficiency. Its apparent K (m), V (max), and catalytic efficiency (k (cat)/K (m)) for D-galactose was 28.9 mM, 4.9 U/mg, and 9.3 mM(-1) min(-1), respectively. The enzyme carried out the isomerization of D-galactose to D-tagatose with a conversion yield over 50% after 12 h under optimal conditions, suggesting its potential in D-tagatose production.
journal_name
Appl Microbiol Biotechnoljournal_title
Applied microbiology and biotechnologyauthors
Cheng L,Mu W,Zhang T,Jiang Bdoi
10.1007/s00253-009-2322-zsubject
Has Abstractpub_date
2010-04-01 00:00:00pages
1089-97issue
4eissn
0175-7598issn
1432-0614journal_volume
86pub_type
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