Adjunct Professor Karen Robins

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Master of Applied Science (Biopharmaceuticals; University of New South Wales)

Bachelor of Science Honours (Microbiology; University of Sydney)

Karen Robins is an Adjunct Professor in the Energy and Process Engineering Discipline, at QUT and Principal at Sustain Biotechnology Pty Ltd. Karen returned five years ago from Switzerland where she spent thirty years working in the Biotechnology Research & Development Department at Lonza Ltd, Switzerland, a global leader in life sciences and industrial biotechnology. Her areas of expertise cover the use of biocatalysis and fermentation for the production of active pharmaceutical ingredients, nutraceuticals and agrochemicals. Some examples of the processes that were commercialised are:

  • production of the vitamin-like compound, L-Carnitine by fermentation
  • chemo-enzymatic production of the vitamin, nicotinamide
  • production of the dehydropeptidase inhibitor, (S)-2,2-dimethylcyclopropane carboxamide by enzymatic chiral resolution
  • chemo-enzymatic production of a herbicide

Karen also has extensive experience in technical project evaluation, project costing, innovation strategy & project management and interdisciplinary collaborations. Karen was Lonza’s representative in many external projects involving industrial consortia and academia led research centres and bilateral collaborations with universities and small start-up companies. Karen has led various scoping study projects at QUT including “Business Intelligence Reports”. The goal of these reports was to identify value-added products derived from agricultural and food industry waste and potential production methods.


  • Kimura T, Ishikawa C, Osorio-Lozada A, Robins KT, Hibi M, Ogawa J, (2014) Production of a pharmaceutical intermediate via biohydroxylation using whole cells of Rhodococcus rubropertinctus N82, Bioscience, Biotechnology and Biochemistry 78(10), 1772 – 1776
  • Bornscheuer UT, Huisman GW, Kazlauskas RJ, Lutz S, Moore JC, Robins K, (2012) Engineering the third wave of biocatalysis, Nature 485(7397), 185
  • Robins K, Osorio-Lozada A, (2012) Exploiting duality in nature: industrial examples of enzymatic oxidation and reduction reactions, Catalysis Science & Technology 2(8), 1524 – 1530
  • Schaetzle S, Steffen-Munsberg F, Thontowi A, Hoehne M, Robins, K, Bornscheuer UT, (2011) Enzymatic asymmetric synthesis of enantiomerically pure aliphatic, aromatic and arylaliphatic amines with (R)-selective amine transaminases, Advanced Synthesis and Catalysis 353(13), 2439 – 2445
  • Hoehne M, Schaetzle S, Jochens H, Robins K, Bornscheuer UT, (2010) Rational assignment of key motifs for function guides in silico enzyme identification, Nature Chemical Biology, 6(11), 807 – 813
  • Schaetzle S, Hoehne M, Robins K, Bornscheuer UT, (2010) Conductometric method for the rapid characterization of the substrate specificity of amine-transaminases, Analytical Chemistry 83(5), 2082 – 2086
  • Hoehne M, Robins K, Bornscheuer UT, (2008) A Protection strategy substantially enhances rate and enantioselectivity in ω-transaminase-catalyzed kinetic resolutions, Advanced Synthesis & Catalysis, 350(6), 807 -812
  • Hoehne M, Kuehl S, Robins K, Bornscheuer UT, (2008) Efficient asymmetric synthesis of chiral amines by combining transaminase and pyruvate decarboxylase, ChemBioChem 9(3), 363 – 365
  • Shaw NM, Robins KT, Kiener A, (2004) Biocatalytic Approaches for the large-scale production of asymmetric synthons, Asymmetric Catalysis on industrial scale: Challenges, Approaches and Solutions p105 – 115
  • Shaw NM, Robins KT, Kiener A, (2003) Lonza: 20 years of biotransformations, Advanced Synthesis & Catalysis, 345(4), 425 – 435
  • Zimmermann T, Robins K, Birch OM, Bohlen E, (1996) Genetic engineering process for the production of S-(+)-2,2-dimethylcyclopropanecarboxamide by microorganisms, Biotechnology Advances 14(3), 315


  • Robins K, Bornscheuer UT, Hohne M, (2017) Process for the preparation of optically active chiral amines, US 9551018
  • Robins K, Bornscheuer UT, Hoehne M, (2014) Process for the preparation of optically active N-protected 3-aminopyrrolidine or optically active N-protected 3-aminopiperidine and the corresponding ketones by optical resolution of the racemic amine mixtures employing a bacterial omega-transaminase, US 8728750
  • Hoehne M, Bornscheuer U, Robins K, Schaetzle S, (2013) Process for the identification and preparation of a (R)-specific omega-transaminase, US 857762
  • Robins KT, Nagasawa T, (2009) Enzymes for the preparation of amides, US 7556956
  • Zigova J, Robins K, Bartek J, (2007) Polyacrylamide beads containing encapsulated cells, US 11822928
  • Brieden W, Naughton A, Robins K, Shaw N, Tinschert A, Zimmermann T, (2004) Method of preparing (S)- or (R)-3,3,3-trifluoro-2-hydroxy-2-methylpropionic acid, US 6773910
  • Robins KT, Nagasawa T, (2002) Process for preparing amides, US 6444451
  • Zimmermann T, Robins K, Birch OM, Bohlen E, (1995) Genetic engineering process for the production of S-(+)-2,2-dimethylcyclopropanecarboxamide by microorganisms, US 5427934
  • Robins KT, Gilligan T, (1994) Bacteria capable of stereospecifically hydrolysing R-(-)-2,2-dimethylcyclopropanecarboxamide, US 5360731