Heterologous expression and characterization of novel 2-Deoxy-d-ribose-5-phosphate aldolase (DERA) from Pyrobaculum calidifontis and Meiothermus ruber. (May 2019)
- Record Type:
- Journal Article
- Title:
- Heterologous expression and characterization of novel 2-Deoxy-d-ribose-5-phosphate aldolase (DERA) from Pyrobaculum calidifontis and Meiothermus ruber. (May 2019)
- Main Title:
- Heterologous expression and characterization of novel 2-Deoxy-d-ribose-5-phosphate aldolase (DERA) from Pyrobaculum calidifontis and Meiothermus ruber
- Authors:
- Lou, Xiao-cong
Zheng, Cheng-cai
Chen, Wen-qi
Ma, Yuan-xin
Mkingule, Idefonce
He, Fei-fan
Fei, Hui - Abstract:
- Graphical abstract: Highlights: Two novel 2-Deoxy-d -ribose-5-phosphate aldolase(DERA) were explored. DERAPyc ( P. calidifontis )exhibited higher aldehyde tolerance than DERAMet ( M. ruber ). The hydrophobic interactions was responsible for the aldehyde tolerance of DERAPyc . Abstract: To overcome the deficiency in which 2-Deoxy-d -ribose-5-phosphate aldolase (DERA) exhibits low levels of catalytic efficiency in aldol reactions and poor tolerance for high concentrations of aldehyde, two novel deoC genes encoding DERAPyc and DERAMet were identified in Pyrobaculum calidifontis and Meiothermus ruber that had heterologous expression in E. coli BL21. The specific activities toward 2-Deoxy-d -ribose-5-phosphate (DR5P) of DERAPyc and DERAMet were 13.6 ± 0.1 and 85.2 ± 0.7 U/mg, respectively. Almost 56.2% (DERAPyc ) and 21.7% (DERAMet ) of their activity remained after being incubated for 6 h in 300 mM acetaldehyde at 25℃. In addition, the DR5P concentration in the reaction catalyzed by DERAPyc and DERAMet was almost 0.31 and 2.63 times the amount catalyzed by DERAEco after reacting for 6 h, respectively. These results suggest that these two novel DERAs with a high tolerance for a high concentration of aldehyde have the potential to be widely used in industrial settings.
- Is Part Of:
- Process biochemistry. Volume 80(2019)
- Journal:
- Process biochemistry
- Issue:
- Volume 80(2019)
- Issue Display:
- Volume 80, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 80
- Issue:
- 2019
- Issue Sort Value:
- 2019-0080-2019-0000
- Page Start:
- 35
- Page End:
- 42
- Publication Date:
- 2019-05
- Subjects:
- Pyrobaculum calidifontis -- Meiothermus ruber -- 2-Deoxy-d-ribose-5-phosphate aldolase -- Aldehyde tolerant -- DR5P production
Biochemical engineering -- Periodicals
Biotechnology -- Periodicals
Biochemistry -- periodicals
Biotechnology -- periodicals
Chemical Engineering -- periodicals
Génie biochimique -- Périodiques
Biotechnologie -- Périodiques
Biochemical engineering
Biotechnology
Periodicals
660.63 - Journal URLs:
- http://www.sciencedirect.com/science/journal/13595113 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.procbio.2019.02.006 ↗
- Languages:
- English
- ISSNs:
- 1359-5113
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6849.983500
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- 9817.xml