Chemical modifications by ionic liquid-inspired cations improve the activity and the stability of formate dehydrogenase in [MMIm][Me 2PO 4]
The formate dehydrogenase (FDH, EC: 1.2. 1.2) from Candida boidinii was found to be inactivated and unstable in the presence of high concentration (>50%) of the water soluble dimethylimidazolium dimethyl phosphate ([MMIm][Me 2PO 4]) ionic liquid. In order to circumvent this problem, the enzyme wa...
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Veröffentlicht in: | Journal of molecular catalysis. B, Enzymatic Enzymatic, 2010-08, Vol.65 (1), p.73-78 |
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creator | Bekhouche, Mourad Doumèche, Bastien Blum, Loïc J. |
description | The formate dehydrogenase (FDH, EC: 1.2. 1.2) from
Candida boidinii was found to be inactivated and unstable in the presence of high concentration (>50%) of the water soluble dimethylimidazolium dimethyl phosphate ([MMIm][Me
2PO
4]) ionic liquid. In order to circumvent this problem, the enzyme was chemically modified by cations usually present in ionic liquids: cholinium (
1), hydroxyethyl-methylimidazolium (
2) and hydroxypropyl-methylimidazolium (
3) cations were activated with carbonyldiimidazole before being reacted with the FDH leading to a heterogeneous population of 6–7 biocatalysts. FDH modified by (
1) or (
3) led to 3–9 modifications while FDH modified by (
2) led to 6 proteins presenting 7–12 grafted cations. Specific activity of the modified enzymes was decreased by a 2.5–3-fold factor (0.10–0.15
μmol
min
−1
mg
−1) compared to the non-modified FDH (0.33
μmol
min
−1
mg
−1) when assayed in carbonate buffer (pH 9.7, 25
mM). After modification, the FDH still present 0.06
μmol
min
−1
mg
−1 in 70% [MMIm][Me
2PO
4] (v:v) (30–45% of their activity in aqueous buffer) while the native enzyme is inactive at this ionic liquid concentration, proving the efficiency of this strategy. The half-life of the modified enzyme is also increased by a 5-fold factor after modification by (
1) (
t
1/2 of 9 days) and by a 3-fold factor after modification by (
2) or (
3) (
t
1/2 of 6 and 5 days respectively) in aqueous solution. When stored in 37.5% [MMIm][Me
2PO
4] (v:v), both modified and unmodified FDH have an increased half-life (
t
1/2 of 6–9 days). This grafting strategy is found to be good methods to mimic and study the stabilizing effect of ionic liquids on enzymes. |
doi_str_mv | 10.1016/j.molcatb.2010.01.028 |
format | Article |
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Candida boidinii was found to be inactivated and unstable in the presence of high concentration (>50%) of the water soluble dimethylimidazolium dimethyl phosphate ([MMIm][Me
2PO
4]) ionic liquid. In order to circumvent this problem, the enzyme was chemically modified by cations usually present in ionic liquids: cholinium (
1), hydroxyethyl-methylimidazolium (
2) and hydroxypropyl-methylimidazolium (
3) cations were activated with carbonyldiimidazole before being reacted with the FDH leading to a heterogeneous population of 6–7 biocatalysts. FDH modified by (
1) or (
3) led to 3–9 modifications while FDH modified by (
2) led to 6 proteins presenting 7–12 grafted cations. Specific activity of the modified enzymes was decreased by a 2.5–3-fold factor (0.10–0.15
μmol
min
−1
mg
−1) compared to the non-modified FDH (0.33
μmol
min
−1
mg
−1) when assayed in carbonate buffer (pH 9.7, 25
mM). After modification, the FDH still present 0.06
μmol
min
−1
mg
−1 in 70% [MMIm][Me
2PO
4] (v:v) (30–45% of their activity in aqueous buffer) while the native enzyme is inactive at this ionic liquid concentration, proving the efficiency of this strategy. The half-life of the modified enzyme is also increased by a 5-fold factor after modification by (
1) (
t
1/2 of 9 days) and by a 3-fold factor after modification by (
2) or (
3) (
t
1/2 of 6 and 5 days respectively) in aqueous solution. When stored in 37.5% [MMIm][Me
2PO
4] (v:v), both modified and unmodified FDH have an increased half-life (
t
1/2 of 6–9 days). This grafting strategy is found to be good methods to mimic and study the stabilizing effect of ionic liquids on enzymes.</description><identifier>ISSN: 1381-1177</identifier><identifier>EISSN: 1873-3158</identifier><identifier>DOI: 10.1016/j.molcatb.2010.01.028</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Biochemistry ; Biochemistry, Molecular Biology ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; Chemical modification ; Formate dehydrogenase (FDH) ; Fundamental and applied biological sciences. Psychology ; Ionic liquid ; Life Sciences ; Methods. Procedures. Technologies ; Stability</subject><ispartof>Journal of molecular catalysis. B, Enzymatic, 2010-08, Vol.65 (1), p.73-78</ispartof><rights>2010 Elsevier B.V.</rights><rights>2015 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c373t-a8b6b3139b7bd6d6b72fd53e90fb306fffcc444cbf2e13b4d20d86d1eda28f3a3</citedby><cites>FETCH-LOGICAL-c373t-a8b6b3139b7bd6d6b72fd53e90fb306fffcc444cbf2e13b4d20d86d1eda28f3a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.molcatb.2010.01.028$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,309,310,314,780,784,789,790,885,3550,23930,23931,25140,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22891398$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00590389$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bekhouche, Mourad</creatorcontrib><creatorcontrib>Doumèche, Bastien</creatorcontrib><creatorcontrib>Blum, Loïc J.</creatorcontrib><title>Chemical modifications by ionic liquid-inspired cations improve the activity and the stability of formate dehydrogenase in [MMIm][Me 2PO 4]</title><title>Journal of molecular catalysis. B, Enzymatic</title><description>The formate dehydrogenase (FDH, EC: 1.2. 1.2) from
Candida boidinii was found to be inactivated and unstable in the presence of high concentration (>50%) of the water soluble dimethylimidazolium dimethyl phosphate ([MMIm][Me
2PO
4]) ionic liquid. In order to circumvent this problem, the enzyme was chemically modified by cations usually present in ionic liquids: cholinium (
1), hydroxyethyl-methylimidazolium (
2) and hydroxypropyl-methylimidazolium (
3) cations were activated with carbonyldiimidazole before being reacted with the FDH leading to a heterogeneous population of 6–7 biocatalysts. FDH modified by (
1) or (
3) led to 3–9 modifications while FDH modified by (
2) led to 6 proteins presenting 7–12 grafted cations. Specific activity of the modified enzymes was decreased by a 2.5–3-fold factor (0.10–0.15
μmol
min
−1
mg
−1) compared to the non-modified FDH (0.33
μmol
min
−1
mg
−1) when assayed in carbonate buffer (pH 9.7, 25
mM). After modification, the FDH still present 0.06
μmol
min
−1
mg
−1 in 70% [MMIm][Me
2PO
4] (v:v) (30–45% of their activity in aqueous buffer) while the native enzyme is inactive at this ionic liquid concentration, proving the efficiency of this strategy. The half-life of the modified enzyme is also increased by a 5-fold factor after modification by (
1) (
t
1/2 of 9 days) and by a 3-fold factor after modification by (
2) or (
3) (
t
1/2 of 6 and 5 days respectively) in aqueous solution. When stored in 37.5% [MMIm][Me
2PO
4] (v:v), both modified and unmodified FDH have an increased half-life (
t
1/2 of 6–9 days). This grafting strategy is found to be good methods to mimic and study the stabilizing effect of ionic liquids on enzymes.</description><subject>Biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chemical modification</subject><subject>Formate dehydrogenase (FDH)</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Ionic liquid</subject><subject>Life Sciences</subject><subject>Methods. Procedures. Technologies</subject><subject>Stability</subject><issn>1381-1177</issn><issn>1873-3158</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNqFkMtqGzEUhofQQtK0j1DQposuxtFlPKNZlWDaJmCTLpJVCEKXo_qYmZErqQY_Q1-6mjrJtqtz-Pl-ifNV1UdGF4yy9mq3GMNgdTYLTktG2YJyeVZdMNmJWrClfFN2IVnNWNedV-9S2lFKOWPyovqz2sKIVg9kDA592TKGKRFzJGWiJQP--o2uxintMYIjLwCO-xgOQPIWiLYZD5iPRE_uX5CyNjjMSfDEhzjqDMTB9uhi-AmTTkBwIo-bze349LgBwn_ckebpffXW6yHBh-d5WT18-3q_uqnXd99vV9fr2opO5FpL0xrBRG8641rXmo57txTQU28Ebb331jZNY43nwIRpHKdOto6B01x6ocVl9fn07lYPah9x1PGogkZ1c71Wc0bpsqdC9gdW2OWJtTGkFMG_FhhVs321U8_21WxfUaaK_dL7dOrtdSp2fdSTxfRa5lz25YKZ-3LioBx8QIgqWYTJgiu2bVYu4H9--gsAcaAI</recordid><startdate>20100801</startdate><enddate>20100801</enddate><creator>Bekhouche, Mourad</creator><creator>Doumèche, Bastien</creator><creator>Blum, Loïc J.</creator><general>Elsevier B.V</general><general>Elsevier</general><general>Elsevier [1995, vol. 1, iss. 1-2016, vol. 134]</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope></search><sort><creationdate>20100801</creationdate><title>Chemical modifications by ionic liquid-inspired cations improve the activity and the stability of formate dehydrogenase in [MMIm][Me 2PO 4]</title><author>Bekhouche, Mourad ; Doumèche, Bastien ; Blum, Loïc J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c373t-a8b6b3139b7bd6d6b72fd53e90fb306fffcc444cbf2e13b4d20d86d1eda28f3a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Biochemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Bioconversions. Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chemical modification</topic><topic>Formate dehydrogenase (FDH)</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Ionic liquid</topic><topic>Life Sciences</topic><topic>Methods. Procedures. Technologies</topic><topic>Stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bekhouche, Mourad</creatorcontrib><creatorcontrib>Doumèche, Bastien</creatorcontrib><creatorcontrib>Blum, Loïc J.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of molecular catalysis. B, Enzymatic</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bekhouche, Mourad</au><au>Doumèche, Bastien</au><au>Blum, Loïc J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chemical modifications by ionic liquid-inspired cations improve the activity and the stability of formate dehydrogenase in [MMIm][Me 2PO 4]</atitle><jtitle>Journal of molecular catalysis. B, Enzymatic</jtitle><date>2010-08-01</date><risdate>2010</risdate><volume>65</volume><issue>1</issue><spage>73</spage><epage>78</epage><pages>73-78</pages><issn>1381-1177</issn><eissn>1873-3158</eissn><abstract>The formate dehydrogenase (FDH, EC: 1.2. 1.2) from
Candida boidinii was found to be inactivated and unstable in the presence of high concentration (>50%) of the water soluble dimethylimidazolium dimethyl phosphate ([MMIm][Me
2PO
4]) ionic liquid. In order to circumvent this problem, the enzyme was chemically modified by cations usually present in ionic liquids: cholinium (
1), hydroxyethyl-methylimidazolium (
2) and hydroxypropyl-methylimidazolium (
3) cations were activated with carbonyldiimidazole before being reacted with the FDH leading to a heterogeneous population of 6–7 biocatalysts. FDH modified by (
1) or (
3) led to 3–9 modifications while FDH modified by (
2) led to 6 proteins presenting 7–12 grafted cations. Specific activity of the modified enzymes was decreased by a 2.5–3-fold factor (0.10–0.15
μmol
min
−1
mg
−1) compared to the non-modified FDH (0.33
μmol
min
−1
mg
−1) when assayed in carbonate buffer (pH 9.7, 25
mM). After modification, the FDH still present 0.06
μmol
min
−1
mg
−1 in 70% [MMIm][Me
2PO
4] (v:v) (30–45% of their activity in aqueous buffer) while the native enzyme is inactive at this ionic liquid concentration, proving the efficiency of this strategy. The half-life of the modified enzyme is also increased by a 5-fold factor after modification by (
1) (
t
1/2 of 9 days) and by a 3-fold factor after modification by (
2) or (
3) (
t
1/2 of 6 and 5 days respectively) in aqueous solution. When stored in 37.5% [MMIm][Me
2PO
4] (v:v), both modified and unmodified FDH have an increased half-life (
t
1/2 of 6–9 days). This grafting strategy is found to be good methods to mimic and study the stabilizing effect of ionic liquids on enzymes.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><doi>10.1016/j.molcatb.2010.01.028</doi><tpages>6</tpages></addata></record> |
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subjects | Biochemistry Biochemistry, Molecular Biology Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Chemical modification Formate dehydrogenase (FDH) Fundamental and applied biological sciences. Psychology Ionic liquid Life Sciences Methods. Procedures. Technologies Stability |
title | Chemical modifications by ionic liquid-inspired cations improve the activity and the stability of formate dehydrogenase in [MMIm][Me 2PO 4] |
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