Enhanced isomerization of rare sugars by ribose-5-phosphate isomerase A from Ochrobactrum sp. CSL1

Wang, Rong; Xu, Xinqi; Yao, Xuemei; Tang, Hengtao; Ju, Xin; Li, Liangzhi

doi:10.1016/j.enzmictec.2021.109789

Cited by 6 publications

(2 citation statements)

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“…To construct strains containing target enzymes, pET28a and Escherichia coli BL21 (DE3) were leveraged as the vector and host as reported previously 28 . The genes of OsRpiB mutant (GenBank: QBY26076.1 with a double mutation R94N/N137Q), d ‐arabinose dehydrogenase gene from Gluconobacter sp.…”

Section: Methodsmentioning

confidence: 99%

“…To construct strains containing target enzymes, pET28a and Escherichia coli BL21 (DE3) were leveraged as the vector and host as reported previously. 28 The genes of OsRpiB mutant (GenBank: QBY26076.1 with a double mutation R94N/N137Q), D-arabinose dehydrogenase gene from Gluconobacter sp. JX-05 (GenBank: KY499714.1), glucose dehydrogenase (GDH) gene from Bacillus megaterium IWG3 (GenBank: AAA22475.1), and ketoreductase gene from Saccharomyces cerevisiae S288C (GenBank: NP_010159.1) were synthesized by Sangon Biotech, ligated into pET-28a vectors and transformed into E. coli competent cells.…”

Section: Preparation Of Recombinant Enzymes In Escherichia Colimentioning

confidence: 99%

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Development of an enzymatic cascade to systematically utilize lignocellulosic monosaccharide

Tang

Chen

Yu³

et al. 2022

J Sci Food Agric

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BACKGROUND The fermentation valorization of two main lignocellulosic monosaccharides, glucose and xylose, is extensively developed; however, it is restricted by limited yield and process complexity. An in vitro enzymatic cascade reaction can be an alternative approach. RESULTS In this study, a three‐stage, five‐enzyme cascade was developed to convert pretreated biomass to valuable chemicals. First, a ribose‐5‐phosphate isomerase B mutant isomerized xylose to d‐xylulose with high substrate specificity, and a d‐arabinose dehydrogenase continued to reduce d‐xylulose to d‐arabitol. Simultaneously, glucose was utilized for the coenzyme regeneration catalyzed by a glucose dehydrogenase, generating useful gluconic acid and achieving 73% of total conversion rate after 36 h. Then, six kinds of pretreated biomass lignocellulose were hydrolyzed by cellulase and hemicellulase, and corn cob was identified as the initial substrate for providing the highest monosaccharide content. A 65% conversion rate of the lignocellulosic xylose was obtained after 24 h. CONCLUSIONS This study presents a proof of concept to convert main lignocellulosic monosaccharides systematically by an enzymatic cascade at stoichiometric ratio. © 2022 Society of Chemical Industry.

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Section: Methodsmentioning

confidence: 99%

Section: Preparation Of Recombinant Enzymes In Escherichia Colimentioning

confidence: 99%