@article { , title = {Development of a high throughput screening tool for biotransformations utilising a thermophilic L-aminoacylase enzyme}, abstract = {Micro-reactors containing a monolith-immobilised thermophilic l-aminoacylase, from Thermococcus litoralis, have been developed for use in biotransformation reactions and a study has been carried out to investigate the stereospecificity and stability of the immobilised enzyme. The potential to use the developed micro-reactors as a tool for rapid screening of enzyme specificity was demonstrated, confirming that the l-aminoacylase showed a similar substrate specificity to that previously reported of the free enzyme. From this baseline, the technique was employed as a tool to evaluate potential unreported substrates with N-benzoyl- (l-threonine, l-leucine and l-arginine) and N-acetyl- (d,l-serine, d,l-leucine, l-tyrosine and l-lysine) protecting groups. The order of preferred substrates was found to be Phe > Thr > Leu > Arg for N-benzoyl substrates and Phe ≫ Ser > Leu > Met > Tyr > Trp for N-acetyl substrates. It was found that by using the micro-reactor a significantly smaller quantity of enzyme and substrates was required. It was shown that the micro-reactors were still operational in the presence of selected organic solvents, such as ethanol, methanol, acetone, dimethylformamide (DMF) and dimethylsulfoxide (DMSO). The results indicated that a combination of a small amount of an appropriate solvent (5\% DMSO) and a higher reaction temperature could be employed in biotransformations where substrate solubility was an issue. © 2009 Elsevier B.V. All rights reserved.}, doi = {10.1016/j.molcatb.2009.12.013}, issn = {1381-1177}, issue = {1-2}, journal = {JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC}, note = {Output ID 22972.}, pages = {81-86}, publicationstatus = {Published}, publisher = {Elsevier}, url = {https://hull-repository.worktribe.com/output/391490}, volume = {63}, keyword = {Specialist Research - Other, Process Chemistry and Technology, Biochemistry, Bioengineering, Catalysis}, year = {2010}, author = {Ngamsom, B. and Hickey, A. M. and Greenway, G. M. and Littlechild, J. A. and Watts, P. and Wiles, C.} }