technology opportunity

Trehalose phosphorylases phosphorylases of trehalose-analoguesof a asyd n bfe a 6° uig -1-pho from enzyme th of using specificity 60°C acceptor The at acceptors. buffer different a in assayed was syn The purified. and coli E. in expressed been has bacterium the of phosphorylase trehalose The developmentof Status • • Advantages sev produce to methods temperatures. elevated at analogues recombinant and/or Enzymatic Applications mutations. of introduction the D-g enz and/or this of variants and enzyme this of L-fucose specificity L-, D-, glucose, t activity high a displays bacterium and 70°C at thermostable marine the t a identified have University Ghent at Researchers Technology sca industrial meth enzymatic an acceptable and yields low in results at produced yet not are analogues treha of inhibitor competitive a i as functions it as it met as the lower to preparations able is it food addition, In intestine. of content caloric the to treha to compared -when example for Lactotrehalose, physicochemical beneficial have analogues Trehalose Introduction rdcin f rhls-nlge uig thermostabl using trehalose-analogues specificity an acceptor broad having phosphorylases of i the in production interested l partners research seeking of is University, consortium a Valley, Bio-Energy Ghent 75% at 60°C. 60°C. 75%at been developed with the wild-type from from wild-type the with developed been pr production A regions. coding amino-acid specific

en al t poue rhls-nlge a hg t high contamination microbial at trehalose-analogues produce to able being analogues production enzymatic high-yield and Cost-effective Thermoanaerobacter brockii Thermoanaerobacter adneoatr subterraneus Caldanaerobacter

useful was optimized by mutagenesis within within mutagenesis by wasoptimized . subterraneusC. Caldanaerobacter subterraneus subterraneus Caldanaerobacter for the production production the for lase. Unfortunately, trehalose- Unfortunately, lase. abolic conversion of trehalose trehalose of conversion abolic yme was further optimized by by optimized further was yme rehalose phosphorylase from from phosphorylase rehalose owards acceptors such as D- as such acceptors owards thetic activity of the enzyme enzyme the of activity thetic s nye n o a variant a of and enzyme is ods are not yet available. yet not are ods ocess for lactotrehalose has has lactotrehalose for ocess d high activity. activity. high d and biological properties. properties. biological and lose-, does not contribute contribute not does lose-, ndustrial and enzymatic enzymatic and ndustrial s not hydrolysed in the the in hydrolysed not s le as chemical synthesis synthesis chemical as le alactose. The acceptor acceptor The alactose. aboratories of Ghent Ghent of aboratories sphate as donor and and donor as sphate f eea trehalose- several of obtaining a yield of of yield a obtaining emperatures avoids avoids emperatures that is highly highly is that rl trehalose- eral e trehalose trehalose e

technology opportunity Chaen et al. (2001) (2001) al. et Chaen www.techtransfer.ugent.be www.gbev.org +32-9-264.61.34 Phone: - +32-497-94.26.69 Mobile: Belgium Gent, 9000 - 653 links Coupure Universi -Ghent Engineering Bioscience of Faculty Biotechnology -Industrial Expertise of Centre p/a -GBEV Economy Biobased UGent IOF Developer Business Eycken der Van Walter ir. Dr. Contact phosphorylase analogues, trehalose Biocatalysis, Keywords References Universit -Ghent Engineering Bioscience of Faculty and Biotechnology -Industrial Expertise of Centre Borght der Jef Van and Desmet Tom Soetaert, Wim Inventors The TPfrom of activity Relative Figure phospho trehalose a covering application European A property Intellectual methodology. a validation further for partner a seeking is UGent Partnership Kim et al. (2007) (2007) al. Kimet 1263-1269 Chem.74: Appl. Pure T(2002) Higashiyama subterraneus plcto camn pirt fo ti Erpa ap European this 2011. 12, December from priority claiming Dece on application filed was thereof, uses and phosphorylases, D- < 5 <5 <5 <5 109 115 136 109 D-Glucosamine D-Fructose D- (%) activity Relative L-Fucose D- L-Arabinose D-Xylose D-Glucose mM) (500 Acceptor mttd om o ti ezm ad ain trehalos variant and enzyme this of forms mutated ,

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