D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization

The NAD(P)-dependent alcohol dehydrogenase (ADH) gene was cloned from Gluconobacter frateurii NBRC 3264 and expressed in Escherichia coli BL21 star (DE3). The expressed enzyme was purified and the characteristics were investigated. The results showed that this ADH can convert allitol into D-allulose...

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Autores principales: Wen, Xin, Lin, Huibin, Ning, Yuhang, Liu, Guangwen, Ren, Yilin, Li, Can, Zhang, Chengjia, Lin, Jianqun, Song, Xin, Lin, Jianqiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Microbiology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9083112/
https://www.ncbi.nlm.nih.gov/pubmed/35547110
http://dx.doi.org/10.3389/fmicb.2022.870168
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author Wen, Xin
Lin, Huibin
Ning, Yuhang
Liu, Guangwen
Ren, Yilin
Li, Can
Zhang, Chengjia
Lin, Jianqun
Song, Xin
Lin, Jianqiang
author_facet Wen, Xin
Lin, Huibin
Ning, Yuhang
Liu, Guangwen
Ren, Yilin
Li, Can
Zhang, Chengjia
Lin, Jianqun
Song, Xin
Lin, Jianqiang
author_sort Wen, Xin
collection PubMed
description The NAD(P)-dependent alcohol dehydrogenase (ADH) gene was cloned from Gluconobacter frateurii NBRC 3264 and expressed in Escherichia coli BL21 star (DE3). The expressed enzyme was purified and the characteristics were investigated. The results showed that this ADH can convert allitol into D-allulose (D-psicose), which is the first reported enzyme with this catalytic ability. The optimum temperature and pH of this enzyme were 50°C and pH 7.0, respectively, and the enzyme showed a maximal activity in the presence of Co(2+). At 1 mM Co(2+) and allitol concentrations of 50, 150, and 250 mM, the D-allulose yields of 97, 56, and 38%, respectively, were obtained after reaction for 4 h under optimal conditions, which were much higher than that obtained by using the epimerase method of about 30%.
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spelling pubmed-90831122022-05-10 D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization Wen, Xin Lin, Huibin Ning, Yuhang Liu, Guangwen Ren, Yilin Li, Can Zhang, Chengjia Lin, Jianqun Song, Xin Lin, Jianqiang Front Microbiol Microbiology The NAD(P)-dependent alcohol dehydrogenase (ADH) gene was cloned from Gluconobacter frateurii NBRC 3264 and expressed in Escherichia coli BL21 star (DE3). The expressed enzyme was purified and the characteristics were investigated. The results showed that this ADH can convert allitol into D-allulose (D-psicose), which is the first reported enzyme with this catalytic ability. The optimum temperature and pH of this enzyme were 50°C and pH 7.0, respectively, and the enzyme showed a maximal activity in the presence of Co(2+). At 1 mM Co(2+) and allitol concentrations of 50, 150, and 250 mM, the D-allulose yields of 97, 56, and 38%, respectively, were obtained after reaction for 4 h under optimal conditions, which were much higher than that obtained by using the epimerase method of about 30%. Frontiers Media S.A. 2022-04-25 /pmc/articles/PMC9083112/ /pubmed/35547110 http://dx.doi.org/10.3389/fmicb.2022.870168 Text en Copyright © 2022 Wen, Lin, Ning, Liu, Ren, Li, Zhang, Lin, Song and Lin. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Wen, Xin
Lin, Huibin
Ning, Yuhang
Liu, Guangwen
Ren, Yilin
Li, Can
Zhang, Chengjia
Lin, Jianqun
Song, Xin
Lin, Jianqiang
D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization
title D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization
title_full D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization
title_fullStr D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization
title_full_unstemmed D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization
title_short D-Allulose (D-Psicose) Biotransformation From Allitol by a Newly Found NAD(P)-Dependent Alcohol Dehydrogenase From Gluconobacter frateurii NBRC 3264 and the Enzyme Characterization
title_sort d-allulose (d-psicose) biotransformation from allitol by a newly found nad(p)-dependent alcohol dehydrogenase from gluconobacter frateurii nbrc 3264 and the enzyme characterization
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9083112/
https://www.ncbi.nlm.nih.gov/pubmed/35547110
http://dx.doi.org/10.3389/fmicb.2022.870168
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