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000004648 0247_ $$2DOI$$a10.1016/j.jbiotec.2009.03.010
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000004648 041__ $$aeng
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000004648 084__ $$2WoS$$aBiotechnology & Applied Microbiology
000004648 1001_ $$0P:(DE-HGF)0$$aGuterl, K.$$b0
000004648 245__ $$aUneven Twins: Comparison of two enantiocomplementary hydroxynitrile lyases with  a/ß--hydrolase fold
000004648 260__ $$aAmsterdam [u.a.]$$bElsevier Science$$c2009
000004648 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000004648 440_0 $$03109$$aJournal of Biotechnology$$v141$$x0168-1656$$y3
000004648 500__ $$aThe authors thank Julich Chiral Solutions/Codexis for providing MeHNL-DNA and MeHNL-Cys81Ala expressing E. coli cells, Astrid Wirtz for HPLC measurements and Sabine Kruschinski for technical assistance. This work was partially supported by the BMBF in frame of project "Biokatalytische Hydrocyanierung & Hydroformylierung (BioHydroForm) FKZ 0313402C" and by the Deutsche Forschungsgemeinschaft in frame of the research training group "BioNoCo" GK 1166.
000004648 520__ $$aHydroxynitrile lyases (HNLs) are applied in technical processes for the synthesis of chiral cyanohydrins. Here we describe the thorough characterization of the recently discovered R-hydroxynitrile lyase from Arabidopsis thaliana and its S-selective counterpart from Manihot esculenta (MeHNL) concerning their properties relevant for technical applications. The results are compared to available data of the structurally related S-HNL from Hevea brasiliensis (HbHNL), which is frequently applied in technical processes. Whereas substrate ranges are highly similar for all three enzymes, the stability of MeHNL with respect to higher temperature and low pH-values is superior to the other HNLs with alpha/beta-hydrolase fold. This enhanced stability is supposed to be due to the ability of MeHNL to form tetramers in solution, while HbHNL and AtHNL are dimers. The different inactivation pathways, deduced by means of circular dichroism, tryptophan fluorescence and static light scattering further support these results. Our data suggest different possibilities to stabilize MeHNL and AtHNL for technical applications: whereas the application of crude cell extracts is appropriate for MeHNL, AtHNL is stabilized by addition of polyols. In addition, the molecular reason for the inhibition of MeHNL and HbHNL by acetate could be elucidated, whereas no such inhibition was observed with AtHNL.
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000004648 588__ $$aDataset connected to Web of Science, Pubmed
000004648 65320 $$2Author$$aAsymmetric carboligation
000004648 65320 $$2Author$$aCyanohydrins
000004648 65320 $$2Author$$aEnzyme catalysis
000004648 65320 $$2Author$$aEnzyme stability
000004648 65320 $$2Author$$aOxynitrilase
000004648 650_2 $$2MeSH$$aAcetonitriles: metabolism
000004648 650_2 $$2MeSH$$aAldehyde-Lyases: chemistry
000004648 650_2 $$2MeSH$$aAldehyde-Lyases: genetics
000004648 650_2 $$2MeSH$$aAldehyde-Lyases: metabolism
000004648 650_2 $$2MeSH$$aAmino Acid Sequence
000004648 650_2 $$2MeSH$$aArabidopsis: enzymology
000004648 650_2 $$2MeSH$$aArabidopsis: genetics
000004648 650_2 $$2MeSH$$aEnzyme Stability
000004648 650_2 $$2MeSH$$aEscherichia coli: genetics
000004648 650_2 $$2MeSH$$aHevea: enzymology
000004648 650_2 $$2MeSH$$aHevea: genetics
000004648 650_2 $$2MeSH$$aHydrogen-Ion Concentration
000004648 650_2 $$2MeSH$$aHydrolases: genetics
000004648 650_2 $$2MeSH$$aManihot: enzymology
000004648 650_2 $$2MeSH$$aManihot: genetics
000004648 650_2 $$2MeSH$$aMolecular Sequence Data
000004648 650_2 $$2MeSH$$aPlant Proteins: genetics
000004648 650_2 $$2MeSH$$aPlant Proteins: metabolism
000004648 650_2 $$2MeSH$$aRecombinant Proteins: genetics
000004648 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000004648 650_2 $$2MeSH$$aStereoisomerism
000004648 650_2 $$2MeSH$$aSubstrate Specificity
000004648 650_2 $$2MeSH$$aTemperature
000004648 650_2 $$2MeSH$$aTime Factors
000004648 650_7 $$00$$2NLM Chemicals$$aAcetonitriles
000004648 650_7 $$00$$2NLM Chemicals$$aPlant Proteins
000004648 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000004648 650_7 $$0532-28-5$$2NLM Chemicals$$amandelonitrile
000004648 650_7 $$0EC 3.-$$2NLM Chemicals$$aHydrolases
000004648 650_7 $$0EC 4.1.2.-$$2NLM Chemicals$$aAldehyde-Lyases
000004648 650_7 $$2WoSType$$aJ
000004648 7001_ $$0P:(DE-HGF)0$$aAndexer, J.N.$$b1
000004648 7001_ $$0P:(DE-HGF)0$$aSehl, T.$$b2
000004648 7001_ $$0P:(DE-HGF)0$$avon Langermann, J.$$b3
000004648 7001_ $$0P:(DE-HGF)0$$aFrindi-Wosch, I.$$b4
000004648 7001_ $$0P:(DE-Juel1)VDB72840$$aRosenkranz, T.$$b5$$uFZJ
000004648 7001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b6$$uFZJ
000004648 7001_ $$0P:(DE-HGF)0$$aGruber, K.$$b7
000004648 7001_ $$0P:(DE-HGF)0$$aKragl, U.$$b8
000004648 7001_ $$0P:(DE-HGF)0$$aEggert, T.$$b9
000004648 7001_ $$0P:(DE-Juel1)131522$$aPohl, M.$$b10$$uFZJ
000004648 773__ $$0PERI:(DE-600)2016476-2$$a10.1016/j.jbiotec.2009.03.010$$gVol. 141$$q141$$tJournal of biotechnology$$v141$$x0168-1656$$y2009
000004648 8567_ $$uhttp://dx.doi.org/10.1016/j.jbiotec.2009.03.010
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