Journal
FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
Volume 10, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fbioe.2022.1001726
Keywords
Aspergillus flavus; xylitol; dehydrogenase; thermostability; L-xylulose
Funding
- National Research Foundation of Korea (NRF) - Ministry of Science, ICT & Future Planning [NRF-2021R1A2B5B03002728]
- NRF - Korean government (MSIT) [2022M3A9I5015091, 2022M3A9I3082366]
- Ministry of Science & ICT (MSIT), Republic of Korea [2022M3A9I3082366] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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This article presents a study on a NAD(+)-dependent xylitol dehydrogenase (AfXDH) from A. flavus, including its enzymatic activity, thermal stability, and application in l-xylulose production.
An NAD(+)-dependent xylitol dehydrogenase from A. flavus (AfXDH) was cloned and successfully expressed in Escherichia coli. AfXDH gene sequence revealed an open reading frame of 1,110 bp, encoding a polypeptide of 369 amino acids with a calculated molecular mass of 38,893 Da. Among various polyols, sorbitol and xylitol were preferred substrates of AfXDH with K-m values of 16.2 and 16.9 mM, respectively. AfXDH showed the highest activity in Tris-glycine-NaOH buffer (pH 9.5) at 50 & DEG;C; it required Zn2+ or Mn2+ for enzyme activity. The half-life at 40? and half denaturation temperature (T-1/2) was 200 min and 45?, respectively. Bioinformatic analyses along with biochemical properties confirmed that AfXDH belonged to the medium-chain dehydrogenase/reductase family. AfXDH exhibits higher thermostability and k ( cat ) values than those of other XDHs. The feasibility of using AfXDH in l-xylulose production was demonstrated. AfXDH, when coupled with Streptococcus pyogenes NADH oxidase, efficiently converted xylitol to l-xylulose with 97% yield, suggesting its usefulness for the industrial l-xylulose production from xylitol.
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