Co-reporter:Andrada But, Aster van Noord, Francesca Poletto, Johan P.M. Sanders, Maurice C.R. Franssen, Elinor L. Scott
Molecular Catalysis 2017 Volume 443(Volume 443) pp:
Publication Date(Web):1 December 2017
DOI:10.1016/j.mcat.2017.09.014
•Oxidation via halogenation by cascade of AOXHp and VCPO.•In cascade reaction of AOXHp-VCPO, MCD reacts (0.0065 mM/min) while Glu does not.•AOXHp is deactivated by HOBr produced by VCPO.•To avoid AOXHp deactivation, the enzymes were separated in two fed-batch reactors.•Enzymatically produced H2O2 enables formation of biobased nitriles at 0.33 mM/min.The chemo-enzymatic cascade which combines alcohol oxidase from Hansenula polymorpha (AOXHp) with vanadium chloroperoxidase (VCPO), for the production of biobased nitriles from amino acids was investigated. In the first reaction H2O2 (and acetaldehyde) are generated from ethanol and oxygen by AOXHp. H2O2 is subsequently used in the second reaction by VCPO to produce HOBr in situ. HOBr is required for the non-enzymatic oxidative decarboxylation of glutamic acid (Glu) to 3-cyanopropanoic acid (CPA), an intermediate in the production of biobased acrylonitrile. It was found that during the one pot conversion of Glu to CPA by AOXHp-VCPO cascade, AOXHp was deactivated by HOBr. To avoid deactivation, the two enzymes were separated in two fed-batch reactors. The deactivation of AOXHp by HOBr appeared to depend on the substrate: an easily halogenated compound like monochlorodimedone (MCD) was significantly converted in one pot by the cascade reaction of AOXHp and VCPO, while conversion of Glu did not occur under those conditions. Apparently, MCD scavenges HOBr before it can inactivate AOXHp, while Glu reacts slower, leading to detrimental concentrations of HOBr. Enzymatically generated H2O2 was used in a cascade reaction involving halogenation steps to enable the co-production of biobased nitriles and acetaldehyde.Download full-size image
Co-reporter:Jose Maria Alonso, Abraham A.M. Bielen, Wouter Olthuis, Servé W.M. Kengen, Han Zuilhof, Maurice C.R. Franssen
Applied Surface Science 2016 Volume 383() pp:283-293
Publication Date(Web):15 October 2016
DOI:10.1016/j.apsusc.2016.05.006
Highlights
- •
Three different oxidases are covalently attached to alkene based SAMs on PtOx.
- •
Attached enzymes remain active and their activity is assessed by chronoamperometry.
- •
Functionalized PtOx allows electron mediator free chronoamperometry measurements.
- •
The thus formed enzyme electrodes are useful as biosensors for glucose and lactate.
- •
Immobilization of human HAOX foresees in vivo lactate monitoring in humans.
Co-reporter:Stijn van der Veen;Norhan Nady;Maurice C. R. Franssen;Han Zuilhof;Remko M. Boom;Tjakko Abee;Karin Schroën
Journal of Applied Polymer Science 2015 Volume 132( Issue 10) pp:
Publication Date(Web):
DOI:10.1002/app.41576
ABSTRACT
The effect of enzyme-catalyzed modification of poly(ethersulfone) (PES) on the adhesion and biofilm formation of two Listeria monocytogenes strains is evaluated under static and dynamic flow conditions. PES has been modified with gallic acid, ferulic acid and 4-hydroxybenzoic acid. The surfaces modified with any of these compounds show up to 70% reduced adhesion of L. monocytogenes under static conditions and up to 95% under dynamic flow conditions compared with unmodified surfaces. Also, under static conditions the formation of biofilms is reduced by ∼70%. These results indicate that the brush structures that are formed by the polymers on the PES surface directly influence the ability of microorganisms to interact with the surface, thereby reducing attachment and biofilm formation of L. monocytogenes. Based on these results, it is expected that enzyme-catalyzed surface modification is a promising tool to reduce microbial adhesion and biofilm formation. © 2014 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2015, 132, 41576.
Co-reporter:Dr. Marloes Schurink;Dr. Suzanne Wolterink-vanLoo;Dr. John vanderOost;Dr. Theo Sonke;Dr. Maurice C. R. Franssen
ChemCatChem 2014 Volume 6( Issue 4) pp:1073-1081
Publication Date(Web):
DOI:10.1002/cctc.201300785
Abstract
The 2-keto-3-deoxygluconate aldolases (KDGAs) isolated from Sulfolobus species convert pyruvate and glyceraldehyde reversibly into 2-keto-3-deoxygluconate and -galactonate. As a result of their high thermostability and activity on nonphosphorylated substrates, KDGA enzymes have potential as biocatalysts for the production of building blocks for fine chemical and pharmaceutical applications. Up to now, wild-type enzymes have only shown moderate stereocontrol for their natural reaction. However, if a set of azido-functionalized aldehydes were applied as alternative acceptors in the reaction with pyruvate, the stereoselectivity was strongly increased to give enantiomeric or diastereomeric excess values up to 97 %. The Sulfolobus acidocaldarius KDGA displayed a higher stereoselectivity than Sulfolobus solfataricus KDGA for all tested reactions. The azido-containing products are useful chiral intermediates in the synthesis of nitrogen heterocycles.
Co-reporter:Maurice C. R. Franssen, Peter Steunenberg, Elinor L. Scott, Han Zuilhof and Johan P. M. Sanders
Chemical Society Reviews 2013 vol. 42(Issue 15) pp:6491-6533
Publication Date(Web):21 Mar 2013
DOI:10.1039/C3CS00004D
Oils, fats, carbohydrates, lignin, and amino acids are all important raw materials for the production of biorenewables. These compounds already play an important role in everyday life in the form of wood, fabrics, starch, paper and rubber. Enzymatic reactions do, in principle, allow the transformation of these raw materials into biorenewables under mild and sustainable conditions. There are a few examples of processes using immobilised enzymes that are already applied on an industrial scale, such as the production of High-Fructose Corn Syrup, but these are still rather rare. Fortunately, there is a rapid expansion in the research efforts that try to improve this, driven by a combination of economic and ecological reasons. This review focusses on those efforts, by looking at attempts to use fatty acids, carbohydrates, proteins and lignin (and their building blocks), as substrates in the synthesis of biorenewables using immobilised enzymes. Therefore, many examples (390 references) from the recent literature are discussed, in which we look both at the specific reactions as well as to the methods of immobilisation of the enzymes, as the latter are shown to be a crucial factor with respect to stability and reuse. The applications of the renewables produced in this way range from building blocks for the pharmaceutical and polymer industry, transport fuels, to additives for the food industry. A critical evaluation of the relevant factors that need to be improved for large-scale use of these examples is presented in the outlook of this review.
Co-reporter:Peter Steunenberg, Maarten Sijm, Han Zuilhof, Johan P. M. Sanders, Elinor L. Scott, and Maurice C. R. Franssen
The Journal of Organic Chemistry 2013 Volume 78(Issue 8) pp:3802-3813
Publication Date(Web):March 27, 2013
DOI:10.1021/jo400268u
A methodology has been developed for an efficient and selective lipase-catalyzed aza-Michael reaction of various amines (primary and secondary) with a series of acrylates and alkylacrylates. Reaction parameters were tuned, and under the optimal conditions it was found that Pseudomonas stutzeri lipase and Chromobacterium viscosum lipase showed the highest selectivity for the aza-Michael addition to substituted alkyl acrylates. For the first time also, some CLEAs were examined that showed a comparable or higher selectivity and yield than the free enzymes and other formulations.
Co-reporter:Norhan Nady, Karin Schroën, Maurice C.R. Franssen, Mohamed S. Mohy Eldin, Han Zuilhof, Remko M. Boom
Journal of Membrane Science 2012 Volumes 394–395() pp:69-79
Publication Date(Web):15 March 2012
DOI:10.1016/j.memsci.2011.12.024
We here report on the performance of poly(ethersulfone) membranes modified with 4-hydroxybenzoic acid and gallic acid as substrates, and using laccase as biocatalyst under several modification conditions. The average flux of the base membrane was never reduced more than 20% (mostly below 10% reduction) by modification with 4-hydroxybenzoic acid, and not more than 9% for gallic acid. The mechanical and thermal properties of the membrane were not adversely affected by the modification method. For 4-hydroxybenzoic acid, longer modification times (i.e., hours) and higher substrate concentrations lead to modified membranes with a better protein repellence. The reaction with gallic acid is faster, but less effective in terms of the resulting protein repellence.In conclusion, the laccase-catalyzed modification of poly(ethersulfone) membranes is a mild method with low environmental impact that leads to effective protein repellence while keeping the bulk properties of the base membrane intact. This makes laccase-catalyzed modification an interesting alternative for currently used membrane modification methods.
Co-reporter:Norhan Nady, Karin Schroën, Maurice C.R. Franssen, Remco Fokkink, Mohamed S. Mohy Eldin, Han Zuilhof, Remko M. Boom
Journal of Colloid and Interface Science 2012 Volume 378(Issue 1) pp:191-200
Publication Date(Web):15 July 2012
DOI:10.1016/j.jcis.2012.04.019
Poly(ethersulfone) (PES) can be modified in a flexible manner using mild, environmentally benign components such as 4-hydroxybenzoic acid and gallic acid, which can be attached to the surface via catalysis by the enzyme laccase. This leads to grafting of mostly linear polymeric chains (for 4-hydroxybenzoic acid, and for gallic acid at low concentration and short modification time) and of networks (for gallic acid at high concentration and long exposure time). The reaction is stopped at a specific time, and the modified surfaces are tested for adsorption of BSA, dextrin and tannin using in-situ reflectometry and AFM imaging.At short modification times, the adsorption of BSA, dextrin and tannin is significantly reduced. However, at longer modification times, the adsorption increases again for both substrates. As the contact angle on modified surfaces at short modification times is reduced (indicative of more hydrophilic surfaces), and keeps the same low values at longer modification times, hydrophilicity is not the only determining factor for the measured differences. At longer modification times, intra-layer reactivity will increase the amount of cross-linking (especially for gallic acid), branching (for 4-hydroxybenzoic acid) and/or collapse of the polymer chains. This leads to more compact layers, which leads to increased protein adsorption.The modifications were shown to have clear potential for reduction of fouling by proteins, polysaccharides, and polyphenols, which could be related to the surface morphology.Graphical abstractHighlights► Enzyme-catalyzed modification can be used to design antifouling surfaces. ► BSA, dextrin, and tannin repellence by laccase-catalyzed modified PES surfaces. ► No direct relationship between fouling of a surface and its hydrophilicity. ► Surface morphology is important for effective foulant repellence.
Co-reporter:Paul M. Könst, Maurice C. R. Franssen, Elinor L. Scott and Johan P. M. Sanders
Green Chemistry 2011 vol. 13(Issue 5) pp:1167-1174
Publication Date(Web):15 Feb 2011
DOI:10.1039/C0GC00564A
Using the biorefinery concept, L-arginine could become widely available from biomass waste streams via the nitrogen storage polypeptide cyanophycin. In our pursuit to develop a route from biobased L-arginine to 1,4-diaminobutane, one of the monomers in nylon-4,6, we were previously successful in the stabilization and immobilization of Bacillus subtilisarginase. In the present study, we investigated the stabilization and immobilization of Trypanosoma bruceiornithine decarboxylase (EC 4.1.1.17) (TbODC) for its application in the decarboxylation of L-ornithine, the final step in the envisioned route towards 1,4-diaminobutane. The stability observed for TbODCin vitro was substantially improved upon addition of dithiothreitol (DTT), which not only has a stabilizing, but also an activating effect. For optimal TbODC performance, the pH should be controlled at pH 8 and the ionic strength should be kept to a minimum. The temperature for optimal productivity is 40 °C. Immobilization of TbODC on Sepabeads EC-HFA was most successful, leading to an almost three-fold improvement in operational stability as compared to the soluble enzyme. Overall, we demonstrated that by optimization of reaction conditions and covalent immobilization the productivity of TbODC was vastly improved, opening up possibilities for its application in the biobased production of 1,4-diaminobutane.
Co-reporter:Norhan Nady, Karin Schroën, Maurice C. R. Franssen, Barend van Lagen, Sukumaran Murali, Remko M. Boom, Mohamed S. Mohyeldin, and Han Zuilhof
ACS Applied Materials & Interfaces 2011 Volume 3(Issue 3) pp:801
Publication Date(Web):February 23, 2011
DOI:10.1021/am101155e
Poly(ethersulfone) (PES) membranes are widely used in industry for separation and purification purposes. However, the drawback of this type of membranes is fouling by proteins. For that reason, modification of PES membranes has been studied to enhance their protein repellence. This paper presents the first example of enzyme-catalyzed modification of PES membranes. Various phenolic acids (enzyme substrates) were bound to a membrane under very mild conditions (room temperature, water, nearly neutral pH) using only laccase from Trametes versicolor as catalyst. The extent of modification, monitored, for example, by the coloration of the modified membranes, can be tuned by adjusting the reaction conditions. The most significant results were obtained with 4-hydroxybenzoic acid and gallic acid as substrates. The presence of a covalently bound layer of 4-hydroxybenzoic acid on the grafted membranes was confirmed by X-ray photoelectron spectroscopy (XPS), infrared reflection absorption spectroscopy (IRRAS), and NMR. In the case of gallic acid, PES membrane modification is mainly caused by adsorption of enzymatically formed homopolymer. The ionization potential of the substrates, and the electronic energies and spin densities of the radicals that are intermediates in the attachment reaction were calculated (B3LYP/6-311G(d,p)) to determine the reactive sites and the order of reactivity of radical substrates to couple with the PES membrane. The calculated order of reactivity of the substrates is in line with the experimental observations. The calculated spin densities in the phenolic radicals are highest at the oxygen atom, which is in line with the formation of ether linkages as observed by IRRAS. The liquid fluxes of the modified membranes are hardly influenced by the grafted layers, in spite of the presence of a substantial and stable new layer, which opens a range of application possibilities for these modified membranes.Keywords: enzyme-catalyzed modification; laccase; phenolic acid; poly(ethersulfone) membrane; protein repellence; surface modification
Co-reporter:PaulM. Könst;Pedro M.C.C.D. Turras;Maurice C.R. Franssen;ElinorL. Scott;Johan P.M. Sers
Advanced Synthesis & Catalysis 2010 Volume 352( Issue 9) pp:1493-1502
Publication Date(Web):
DOI:10.1002/adsc.201000034
Abstract
L-Ornithine could serve as an intermediate in the biobased production of 1,4-diaminobutane from L-arginine. Using the concept of biorefinery, L-arginine could become widely available from biomass waste streams via the nitrogen storage polypeptide cyanophycin. Selective hydrolysis of L-arginine to L-ornithine is difficult to perform chemically, therefore the stabilization and immobilization of Bacillus subtilis arginase (EC 3.5.3.1) was studied in a continuously stirred membrane reactor system. Initial pH of the substrate solution, addition of L-aspartic acid and reducing agents all appeared to have an effect on the operational stability of B. subtilis arginase. A remarkably good operational stability (total turnover number, TTN=1.13⋅108) at the pH of arginine free base (pH 11.0) was observed, which was further improved with the addition of sodium dithionite to the substrate solution (TTN>1⋅109). B. subtilis arginase was successfully immobilized on three commercially available epoxy-activated supports. Immobilization on Sepabeads EC-EP was most promising, resulting in a recovered activity of 75% and enhanced thermostability. In conclusion, the stabilization and immobilization of B. subtilis arginase has opened up possibilities for its application in the biobased production of nitrogen-containing chemicals as an alternative to the petrochemical production.
Co-reporter:Paul M. Könst, Maurice C. R. Franssen, Elinor L. Scott and Johan P. M. Sanders
Green Chemistry 2009 vol. 11(Issue 10) pp:1646-1652
Publication Date(Web):31 Jul 2009
DOI:10.1039/B902731A
β-Alanine could serve as an intermediate in the biobased production of nitrogen containing chemicals from L-aspartic acid. Following the biorefinery concept, L-aspartic acid could become widely available from biomass waste streams via the nitrogen storage polypeptide cyanophycin. Since α-decarboxylation of L-aspartic acid is difficult to perform chemically, the applicability of Escherichia coliL-aspartate α-decarboxylase (EC 4.1.1.11) (ADC) for the production of β-alanine was studied. With an increasing activity up to 90 °C and maintaining its activity upon storage for 24 hours at 60 °C, ADC showed a remarkably high thermostability. ADC has an optimum at pH 7.5 and starts to lose activity upon storage below pH 6. An inhibiting effect by β-alanine was not observed. Immobilization on Sepabeads EC-EP and EC-HFA epoxy supports did not result in an increased thermostability, but did improve operational stability. Nonetheless, enzyme inactivation occurs during catalysis, probably caused by irreversible transamination of the catalytically essential pyruvoyl group.
Co-reporter:Tijs M. Lammens, Daniela De Biase, Maurice C. R. Franssen, Elinor L. Scott and Johan P. M. Sanders
Green Chemistry 2009 vol. 11(Issue 10) pp:1562-1567
Publication Date(Web):24 Jul 2009
DOI:10.1039/B913741F
Glutamic acid is an important constituent of waste streams from biofuels production. It is an interesting starting material for the synthesis of nitrogen containing bulk chemicals, thereby decreasing the dependency on fossil fuels. On the pathway from glutamic acid to a range of molecules, the decarboxylation of glutamic acid to γ-aminobutyric acid (GABA) is an important reaction. This reaction, catalyzed by the enzyme glutamic acid α-decarboxylase (GAD) was studied on a gram scale. In this study, GAD was immobilized on Eupergit and in calcium alginate and its operational stability was determined in a buffer free system, using various reactor configurations. Immobilization was shown to increase the GAD stability. The conditions for the highest GABA production per gram of enzyme were determined by extrapolation of enzyme stability data. At 30 °C in a fed batch process this results in an average volumetric productivity of 35 kg m−3 hr−1. The cost of using GAD immobilized in calcium alginate was estimated as €5 per metric ton of product. Furthermore it was shown that the cofactor pyridoxal-5′-phosphate (PLP) could be regenerated by the addition of a small amount of α-ketoglutaric acid to the reactor. In conclusion the application of immobilized GAD in a fed batch reactor was shown to be a scalable process for the industrial production of GABA from glutamic acid.
Co-reporter:Carel A. G. M. Weijers, Paul M. Könst, Maurice C. R. Franssen and Ernst J. R. Sudhölter
Organic & Biomolecular Chemistry 2007 vol. 5(Issue 19) pp:3106-3114
Publication Date(Web):21 Aug 2007
DOI:10.1039/B709742E
The 1-oxaspiro[2.5]octane moiety is a common motif in many biologically active spiroepoxide compounds. Stereochemistry plays an important role in the action of these spiroepoxides, since the O-axial C3 epimers are predominantly responsible for biological activity. In view of this, the reactivity of the yeast epoxide hydrolase (YEH) from Rhodotorula glutinis towards both O-axial and O-equatorial C3 epimers of various 1-oxaspiro[2.5]octanes was investigated. O-axial C3 Epimers were hydrolyzed faster than the O-equatorial C3 epimers. The stereochemical preference was greatly dependent on the type of substitution on the cyclohexane ring. The preference of YEH for O-axial C3 epimers, found throughout this study, illustrates the effectiveness of YEH in enzymatic detoxification of spiroepoxides.
Co-reporter:Nicole W.J.T. Heinsman, Carin G.P.H. Schroën, Albert van der Padt, Maurice C.R. Franssen, Remko M. Boom, Klaas van‘t Riet
Tetrahedron: Asymmetry 2003 Volume 14(Issue 18) pp:2699-2704
Publication Date(Web):19 September 2003
DOI:10.1016/S0957-4166(03)00577-9
In the enantioselective esterification of 4-methyloctanoic acid with ethanol by immobilised Candida antarctica lipase B (Novozym 435®), the enantiomeric excesses determined during the course of the reaction deviated strongly from the theoretical values, leading to unacceptably large confidence intervals for the enantiomeric ratio (E value). This observation was in contrast to our previous findings for transesterification and hydrolysis reactions with this enzyme. Herein, the three reactions are compared; the anomalous results in the esterification reaction appear to be caused by adsorption of 4-methyloctanoic acid inside the enzyme beads. We found that on average 1.19 g of 4-methyloctanoic acid was incorporated per g of Novozym 435®. If the concentration of this substrate was adjusted accordingly in the calculations, the resulting E values showed acceptable confidence intervals. In previous research on transesterification reactions in excess apolar solvent (comparable affinity for the beads), sorption does not play an important role because only small amounts of substrate were lost. For hydrolysis reactions, sorption takes place but the acid is released from the beads upon titration and no effect on the E value is found. However, for esterification reactions, sorption should not be neglected since there is no driving force to release the acid from the beads.When immobilised Candida antarctica lipase B (Novozym 435®) is used for esterification in a solventless system, sorption of substrate disturbs the accurate determination of the enantioselectivity (E value).
Co-reporter:Arkadij Sobolev, Maurice C.R. Franssen, Janis Poikans, Gunars Duburs, Aede de Groot
Tetrahedron: Asymmetry 2002 Volume 13(Issue 21) pp:2389-2397
Publication Date(Web):31 October 2002
DOI:10.1016/S0957-4166(02)00655-9
The lipase-catalysed kinetic resolution of four derivatives of 4-[(acyloxy)methyl] and 4-ethoxycarbonylmethyl 3-methyl 5-propyl 2,6-dimethyl-1,4-dihydro-3,4,5-pyridinetricarboxylates has been investigated. Whereas the enantioselectivity of lipases towards the acyloxymethyl derivatives was rather low, the Candida antarctica lipase B (Novozym 435®, CAL-B)-catalysed hydrolysis of the ethoxycarbonylmethyl ester of 1,4-dihydroisonicotinic acid was enantioselective. In water-saturated diisopropyl ether at 45°C the enantioselectivity of CAL-B toward the ethoxycarbonylmethyl ester was rather moderate (E=13.8), but it was enhanced at rt and +4°C (E=21.5 and E=28.9, respectively). A high enantiomeric ratio (E=45.3) was reached at subzero temperatures, although at the expense of the reaction rate.Graphic(+)-3-(Methoxycarbonyl)-2,6-dimethyl-5-(propoxycarbonyl)-1,4-dihydro-4-pyridinecarboxylic acidC14H19NO6E.e.=61%[α]D20=+2.0 (c 2, MeOH)Source of chirality: enzymatic hydrolysisAbsolute configuration: not known(+)-4-[(Isobutyryloxy)methyl] 3-methyl 5-propyl 2,6-dimethyl-1,4-dihydro-3,4,5-pyridinetricarboxylateC19H27NO8E.e.=65%[α]D20=+2.8 (c 1, CHCl3)[α]D20=+4.4 (c 1, MeOH)Source of chirality: enzymatic hydrolysisAbsolute configuration: not known(+)-4-Carboxymethyl 3-methyl 5-propyl 2,6-dimethyl-1,4-dihydro-3,4,5-pyridinetricarboxylateC16H21NO8E.e.=93%[α]D20=+7.0 (c 1, MeOH)Source of chirality: enzymatic hydrolysisAbsolute configuration: not known(−)-4-Ethoxycarbonylmethyl 3-methyl 5-propyl 2,6-dimethyl-1,4-dihydro-3,4,5-pyridinetricarboxylateC18H25NO8E.e.=81%[α]D20=−5.3 (c 1, CHCl3)Source of chirality: enzymatic hydrolysisAbsolute configuration: not known
Co-reporter:T.M. Lammens, M.C.R. Franssen, E.L. Scott, J.P.M. Sanders
Biomass and Bioenergy (September 2012) Volume 44() pp:168-181
Publication Date(Web):September 2012
DOI:10.1016/j.biombioe.2012.04.021
Co-reporter:Rokus Renirie, Aliaksei Pukin, Barend van Lagen, Maurice C.R. Franssen
Journal of Molecular Catalysis B: Enzymatic (December 2010) Volume 67(Issues 3–4) pp:219-224
Publication Date(Web):1 December 2010
DOI:10.1016/j.molcatb.2010.08.009
Previously it has been shown that glycerol can be regioselectively glucosylated by sucrose phosphorylase from Leuconostoc mesenteroides to form 2-O-α-d-glucopyranosyl-glycerol (Goedl et al., Angew. Chem. Int. Ed. 47 (2008) 10086–10089). A series of compounds related to glycerol were investigated by us to determine the scope of the α-glucosylation reaction of sucrose phosphorylase. Both sucrose and glucose 1-phosphate (G1P) were applied as glucosyl donor. Mono-alcohols were not accepted as substrates but several 1,2-diols were readily glucosylated, proving that the vicinal diol unit is crucial for activity. The smallest substrate that was accepted for glucosylation appeared to be ethylene glycol, which was converted to the monoglucoside for 69%. Using high acceptor and donor concentrations (up to 2.5 M), sucrose or G1P hydrolysis (with H2O being the ‘acceptor’) can be minimised. In the study cited above, a preference for glucosylation of glycerol on the 2-position has been observed. For 1,2-propanediol however, the regiochemistry appeared to be dependent on the configuration of the substrate. The (R)-enantiomer was preferentialy glucosylated on its 1-position (ratio 2.5:1), whereas the 2-glucoside is the major product for (S)-1,2-propanediol (1:4.1). d.e.ps of 71–83% were observed with a preference for the (S)-enantiomer of the glucosides of 1,2-propanediol and 1,2-butanediol and the (R)-enantiomer of the glucoside of 3-methoxy-1,2-propanediol. This is the first example of stereoselective glucosylation of a non-natural substrate by sucrose phosphorylase. 3-Amino-1,2-propanediol, 3-chloro-1,2-propanediol, 1-thioglycerol and glyceraldehyde were not accepted as substrates. Generally, the glucoside yield is higher when sucrose is used as a donor rather than G1P, due to the fact that the released phosphate is a stronger inhibitor of the enzyme (in case of G1P) than the released fructose (in case of sucrose). Essentially the same results are obtained with sucrose phosphorylase from Bifidobacterium adolescentis.Graphical abstract.Download full-size imageResearch highlights▶ Sucrose phosphorylase only accepts compounds containing the 1,2-diol moiety. ▶ Ethylene glycol is the smallest substrate accepted by sucrose phosphorylase. ▶ Regiopreference of sucrose phosphorylase depends on configuration of the diol. ▶ Sucrose phosphorylase is a stereoselective enzyme ▶ Sucrose gives higher yields than glucose 1-phosphate in glucosylation reactions.
Co-reporter:Aliaksei V. Pukin, Carmen G. Boeriu, Elinor L. Scott, Johan P.M. Sanders, Maurice C.R. Franssen
Journal of Molecular Catalysis B: Enzymatic (August 2010) Volume 65(Issues 1–4) pp:58-62
Publication Date(Web):1 August 2010
DOI:10.1016/j.molcatb.2009.12.006
The title compound was prepared enzymatically from l-lysine in an excellent yield and under buffer-free conditions. l-Lysine was oxidized by the action of l-lysine α-oxidase from Trichoderma viride followed by spontaneous oxidative decarboxylation of the intermediate 6-amino-2-oxocaproic acid in the reaction medium. l-Lysine α-oxidase was immobilized on an epoxy-activated solid support (Sepabeads EC-EP) and the activity of both solution-based and immobilized enzyme in this reaction was determined.
Co-reporter:Carel A. G. M. Weijers, Paul M. Könst, Maurice C. R. Franssen and Ernst J. R. Sudhölter
Organic & Biomolecular Chemistry 2007 - vol. 5(Issue 19) pp:NaN3114-3114
Publication Date(Web):2007/08/21
DOI:10.1039/B709742E
The 1-oxaspiro[2.5]octane moiety is a common motif in many biologically active spiroepoxide compounds. Stereochemistry plays an important role in the action of these spiroepoxides, since the O-axial C3 epimers are predominantly responsible for biological activity. In view of this, the reactivity of the yeast epoxide hydrolase (YEH) from Rhodotorula glutinis towards both O-axial and O-equatorial C3 epimers of various 1-oxaspiro[2.5]octanes was investigated. O-axial C3 Epimers were hydrolyzed faster than the O-equatorial C3 epimers. The stereochemical preference was greatly dependent on the type of substitution on the cyclohexane ring. The preference of YEH for O-axial C3 epimers, found throughout this study, illustrates the effectiveness of YEH in enzymatic detoxification of spiroepoxides.
Co-reporter:Maurice C. R. Franssen, Peter Steunenberg, Elinor L. Scott, Han Zuilhof and Johan P. M. Sanders
Chemical Society Reviews 2013 - vol. 42(Issue 15) pp:NaN6533-6533
Publication Date(Web):2013/03/21
DOI:10.1039/C3CS00004D
Oils, fats, carbohydrates, lignin, and amino acids are all important raw materials for the production of biorenewables. These compounds already play an important role in everyday life in the form of wood, fabrics, starch, paper and rubber. Enzymatic reactions do, in principle, allow the transformation of these raw materials into biorenewables under mild and sustainable conditions. There are a few examples of processes using immobilised enzymes that are already applied on an industrial scale, such as the production of High-Fructose Corn Syrup, but these are still rather rare. Fortunately, there is a rapid expansion in the research efforts that try to improve this, driven by a combination of economic and ecological reasons. This review focusses on those efforts, by looking at attempts to use fatty acids, carbohydrates, proteins and lignin (and their building blocks), as substrates in the synthesis of biorenewables using immobilised enzymes. Therefore, many examples (390 references) from the recent literature are discussed, in which we look both at the specific reactions as well as to the methods of immobilisation of the enzymes, as the latter are shown to be a crucial factor with respect to stability and reuse. The applications of the renewables produced in this way range from building blocks for the pharmaceutical and polymer industry, transport fuels, to additives for the food industry. A critical evaluation of the relevant factors that need to be improved for large-scale use of these examples is presented in the outlook of this review.
