For biocatalysis-based processes to be scalable, one has to fulfill at least three requirements: (1) industrially acceptable throughput (volume efficiency); (2) prevention of product inhibition; (3) product separation by partition without recourse to chromatography; and in the case of kinetic resolution, the off-enantiomer needs to be recycled. In the chemoenzymatic synthesis of (R)-3-tert-butoxycarbonyl-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid (BocDMTA) 1 featuring a Klebsiella oxytoca hydrolase, the thermal stability of the enzyme helps to attain an industrially feasible concentration of the substrate, methyl (+/-)-5,5-dimethyl-1,3-thiazoline-4-carboxylate 6b, at 60 degreesC: [(+/-)-6b] = 3.0 M (575 g/L). In the (S)-selective hydrolysis of (+/-)-3-butyryloxyquinuclidinium butyrate 12 with an Aspergillus melleus protease, Ca(OH)(2) serves as so effective a scavenger of butyric acid as to prevent it from impeding the catalytic activity of the protease. This allows the enzymatic hydrolysis to proceed at [(+/-)-12] = 2.0M (571 g/L); on extractive separation from the left-over (R)-3-quinuclidinyl butyrate 11a, which is converted to (R)-3-quinuclidinol 2 via methanolysis, the digested (S)-2 can be racemized over Raney Co under hydrogen for another round of the enzymatic resolution. In the synthesis of traps-1-(1,3-dihydroxypropan-2-yl)-4-propylcyclohexane 3, cis-4-propylcyclohexanol 14 is prepared by Galactomyces geotrichum-mediated equatorial hydride delivery to 4-propylcyclohexanone 15; while the microbial reduction fails to go to completion, the unconsumed ketone 15 can be removed via bisulfite adduct formation or by simple distillation after malonate homologation. (C) 2004 Elsevier B.V. All rights reserved.