Characterization of a novel thermostable l-rhamnose isomerase from Thermobacillus composti KWC4 and its application for production of d-allose. (February 2017)
- Record Type:
- Journal Article
- Title:
- Characterization of a novel thermostable l-rhamnose isomerase from Thermobacillus composti KWC4 and its application for production of d-allose. (February 2017)
- Main Title:
- Characterization of a novel thermostable l-rhamnose isomerase from Thermobacillus composti KWC4 and its application for production of d-allose
- Authors:
- Xu, Wei
Zhang, Wenli
Tian, Yuqing
Zhang, Tao
Jiang, Bo
Mu, Wanmeng - Abstract:
- Graphical abstract: Highlights: Ad -allose-producing L-RI was characterized from T. composti KWC4. T. composti L-RI showed maximum activity at 65 °C and pH 7.5. It displayed promising thermostability and a relatively wide pH spectrum. T m of T. composti L-RI was increased by 3 °C in presence of Mn 2+ . It produced 23.30%d -allose as the sole product fromd -allulose. Abstract: d -Allose was considered as a kind of rare sugars with testified potential medicinal and agricultural benefits.l -Rhamnose isomerase (L-RI, EC 5.3.1.14), an aldose-ketose isomerase, played a significant part in producing rare sugar. In this article, a thermostabled -allose-producing L-RI was characterized from a thermotolerant bacterium, Thermobacillus composti KWC4. The recombinant L-RI was activated obviously in the presence of Mn 2+ with an optimal pH 7.5 and temperature 65 °C. The Michaelis-Menten constant ( K m ), turnover number ( k cat ) and catalytic efficiency ( k cat / K m ) forl -rhamnose were 33.8 mM, 1189.8 min −1 and 35.2 min −1 mM −1, respectively. At a higher temperature, Mn 2+ played a pivotal role in strengthening the thermostability of T. composti L-RI. The differential scanning calorimetry (DSC) results showed the denaturing temperature ( T m ) of T . composti L-RI was increased by 3 °C in presence of Mn 2+ . Although the T . composti L-RI displayed the optimum substrate asl -rhamnose, it could also effectively catalyze the isomerization betweend -allulose andd -allose. When theGraphical abstract: Highlights: Ad -allose-producing L-RI was characterized from T. composti KWC4. T. composti L-RI showed maximum activity at 65 °C and pH 7.5. It displayed promising thermostability and a relatively wide pH spectrum. T m of T. composti L-RI was increased by 3 °C in presence of Mn 2+ . It produced 23.30%d -allose as the sole product fromd -allulose. Abstract: d -Allose was considered as a kind of rare sugars with testified potential medicinal and agricultural benefits.l -Rhamnose isomerase (L-RI, EC 5.3.1.14), an aldose-ketose isomerase, played a significant part in producing rare sugar. In this article, a thermostabled -allose-producing L-RI was characterized from a thermotolerant bacterium, Thermobacillus composti KWC4. The recombinant L-RI was activated obviously in the presence of Mn 2+ with an optimal pH 7.5 and temperature 65 °C. The Michaelis-Menten constant ( K m ), turnover number ( k cat ) and catalytic efficiency ( k cat / K m ) forl -rhamnose were 33.8 mM, 1189.8 min −1 and 35.2 min −1 mM −1, respectively. At a higher temperature, Mn 2+ played a pivotal role in strengthening the thermostability of T. composti L-RI. The differential scanning calorimetry (DSC) results showed the denaturing temperature ( T m ) of T . composti L-RI was increased by 3 °C in presence of Mn 2+ . Although the T . composti L-RI displayed the optimum substrate asl -rhamnose, it could also effectively catalyze the isomerization betweend -allulose andd -allose. When the reaction reached equilibrium, the sole productd -allose was produced from D-alluose by T. composti L-RI. … (more)
- Is Part Of:
- Process biochemistry. Volume 53(2017)
- Journal:
- Process biochemistry
- Issue:
- Volume 53(2017)
- Issue Display:
- Volume 53, Issue 2017 (2017)
- Year:
- 2017
- Volume:
- 53
- Issue:
- 2017
- Issue Sort Value:
- 2017-0053-2017-0000
- Page Start:
- 153
- Page End:
- 161
- Publication Date:
- 2017-02
- Subjects:
- Thermobacillus composti KWC4 -- l-Rhamnose isomerase -- Thermostability -- d-Allose
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.2016.11.025 ↗
- 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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