Myo-inositol facilitators IolT1 and IolT2 enhance d-mannitol formation from d-fructose in Corynebacterium glutamicum
Reduction of d-fructose to d-mannitol by whole-cell biotransformation with recombinant resting cells of Corynebacterium glutamicum ATCC13032 requires the coexpression of mdh and fdh, which encode mannitol and formate dehydrogenases, respectively. However, d-mannitol formation is limited by the uptak...
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| Veröffentlicht in: | FEMS microbiology letters 2009, Vol.290 (2), p.227-235 |
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| creator | Bäumchen, Carsten Krings, Eva Bringer, Stephanie Eggeling, Lothar Sahm, Hermann |
| description | Reduction of d-fructose to d-mannitol by whole-cell biotransformation with recombinant resting cells of Corynebacterium glutamicum ATCC13032 requires the coexpression of mdh and fdh, which encode mannitol and formate dehydrogenases, respectively. However, d-mannitol formation is limited by the uptake of d-fructose in its unphosphorylated form, because additional expression of the sugar facilitator from Zymomonas mobilis resulted in a significantly increased productivity. Here we identified similarities of the myo-inositol transporters IolT1 and IolT2 of C. glutamicum to the sugar facilitator of Z. mobilis. The myo-inositol transporter genes were both individually overexpressed and deleted in recombinants expressing mdh and fdh. Biotransformation experiments showed that the presence and absence, respectively, of IolT1 and IolT2 significantly influenced d-mannitol formation, indicating a d-fructose transport capability of these transporters. For further evidence, a C. glutamicumΔptsF mutant unable to grow with d-fructose was complemented with a heterologous fructokinase gene. This resulted in restoration of growth with d-fructose. Using overexpressed iolT1, mdh and fdh, d-mannitol formation obtained with C. glutamicum was 34.2 g L⁻¹, as opposed to 16 g L⁻¹ formed by the strain overexpressing only mdh and fdh, showing the suitability of myo-inositol transporters for d-fructose uptake to obtain d-mannitol formation by whole-cell biotransformation with C. glutamicum. |
| doi_str_mv | 10.1111/j.1574-6968.2008.01425.x |
| format | Article |
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However, d-mannitol formation is limited by the uptake of d-fructose in its unphosphorylated form, because additional expression of the sugar facilitator from Zymomonas mobilis resulted in a significantly increased productivity. Here we identified similarities of the myo-inositol transporters IolT1 and IolT2 of C. glutamicum to the sugar facilitator of Z. mobilis. The myo-inositol transporter genes were both individually overexpressed and deleted in recombinants expressing mdh and fdh. Biotransformation experiments showed that the presence and absence, respectively, of IolT1 and IolT2 significantly influenced d-mannitol formation, indicating a d-fructose transport capability of these transporters. For further evidence, a C. glutamicumΔptsF mutant unable to grow with d-fructose was complemented with a heterologous fructokinase gene. This resulted in restoration of growth with d-fructose. Using overexpressed iolT1, mdh and fdh, d-mannitol formation obtained with C. glutamicum was 34.2 g L⁻¹, as opposed to 16 g L⁻¹ formed by the strain overexpressing only mdh and fdh, showing the suitability of myo-inositol transporters for d-fructose uptake to obtain d-mannitol formation by whole-cell biotransformation with C. glutamicum.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2008.01425.x</identifier><identifier>PMID: 19054080</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biological Transport ; Biotransformation ; Corynebacterium glutamicum ; Corynebacterium glutamicum - chemistry ; Corynebacterium glutamicum - genetics ; Corynebacterium glutamicum - metabolism ; Fructokinase ; Fructose ; Fructose - metabolism ; Inositol ; Inositol - metabolism ; Mannitol ; Mannitol - metabolism ; Membrane Transport Proteins - chemistry ; Membrane Transport Proteins - genetics ; Membrane Transport Proteins - metabolism ; Microbiology ; Molecular Sequence Data ; Recombinants ; Restoration ; Sequence Alignment ; Sequence Deletion ; Sugar ; sugar transport ; whole-cell biotransformation ; Zymomonas mobilis</subject><ispartof>FEMS microbiology letters, 2009, Vol.290 (2), p.227-235</ispartof><rights>2008 Federation of European Microbiological Societies. 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However, d-mannitol formation is limited by the uptake of d-fructose in its unphosphorylated form, because additional expression of the sugar facilitator from Zymomonas mobilis resulted in a significantly increased productivity. Here we identified similarities of the myo-inositol transporters IolT1 and IolT2 of C. glutamicum to the sugar facilitator of Z. mobilis. The myo-inositol transporter genes were both individually overexpressed and deleted in recombinants expressing mdh and fdh. Biotransformation experiments showed that the presence and absence, respectively, of IolT1 and IolT2 significantly influenced d-mannitol formation, indicating a d-fructose transport capability of these transporters. For further evidence, a C. glutamicumΔptsF mutant unable to grow with d-fructose was complemented with a heterologous fructokinase gene. This resulted in restoration of growth with d-fructose. Using overexpressed iolT1, mdh and fdh, d-mannitol formation obtained with C. glutamicum was 34.2 g L⁻¹, as opposed to 16 g L⁻¹ formed by the strain overexpressing only mdh and fdh, showing the suitability of myo-inositol transporters for d-fructose uptake to obtain d-mannitol formation by whole-cell biotransformation with C. glutamicum.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological Transport</subject><subject>Biotransformation</subject><subject>Corynebacterium glutamicum</subject><subject>Corynebacterium glutamicum - chemistry</subject><subject>Corynebacterium glutamicum - genetics</subject><subject>Corynebacterium glutamicum - metabolism</subject><subject>Fructokinase</subject><subject>Fructose</subject><subject>Fructose - metabolism</subject><subject>Inositol</subject><subject>Inositol - metabolism</subject><subject>Mannitol</subject><subject>Mannitol - 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Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bäumchen, Carsten</au><au>Krings, Eva</au><au>Bringer, Stephanie</au><au>Eggeling, Lothar</au><au>Sahm, Hermann</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Myo-inositol facilitators IolT1 and IolT2 enhance d-mannitol formation from d-fructose in Corynebacterium glutamicum</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2009</date><risdate>2009</risdate><volume>290</volume><issue>2</issue><spage>227</spage><epage>235</epage><pages>227-235</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><abstract>Reduction of d-fructose to d-mannitol by whole-cell biotransformation with recombinant resting cells of Corynebacterium glutamicum ATCC13032 requires the coexpression of mdh and fdh, which encode mannitol and formate dehydrogenases, respectively. However, d-mannitol formation is limited by the uptake of d-fructose in its unphosphorylated form, because additional expression of the sugar facilitator from Zymomonas mobilis resulted in a significantly increased productivity. Here we identified similarities of the myo-inositol transporters IolT1 and IolT2 of C. glutamicum to the sugar facilitator of Z. mobilis. The myo-inositol transporter genes were both individually overexpressed and deleted in recombinants expressing mdh and fdh. Biotransformation experiments showed that the presence and absence, respectively, of IolT1 and IolT2 significantly influenced d-mannitol formation, indicating a d-fructose transport capability of these transporters. For further evidence, a C. glutamicumΔptsF mutant unable to grow with d-fructose was complemented with a heterologous fructokinase gene. This resulted in restoration of growth with d-fructose. Using overexpressed iolT1, mdh and fdh, d-mannitol formation obtained with C. glutamicum was 34.2 g L⁻¹, as opposed to 16 g L⁻¹ formed by the strain overexpressing only mdh and fdh, showing the suitability of myo-inositol transporters for d-fructose uptake to obtain d-mannitol formation by whole-cell biotransformation with C. glutamicum.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>19054080</pmid><doi>10.1111/j.1574-6968.2008.01425.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2009, Vol.290 (2), p.227-235 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological Transport Biotransformation Corynebacterium glutamicum Corynebacterium glutamicum - chemistry Corynebacterium glutamicum - genetics Corynebacterium glutamicum - metabolism Fructokinase Fructose Fructose - metabolism Inositol Inositol - metabolism Mannitol Mannitol - metabolism Membrane Transport Proteins - chemistry Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism Microbiology Molecular Sequence Data Recombinants Restoration Sequence Alignment Sequence Deletion Sugar sugar transport whole-cell biotransformation Zymomonas mobilis |
| title | Myo-inositol facilitators IolT1 and IolT2 enhance d-mannitol formation from d-fructose in Corynebacterium glutamicum |
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