Peter C K Lau
Principal Research Officer
National Research Council Canada
Dr. Lau holds a Ph.D. in Biochemistry (steroid metabolism) from the University of Ottawa, Ontario. He is a Principal Research Officer of the National Research Council of Canada, Montreal, 6100 Royalmount Avenue research facilities (previously known as the Biotechnology Research Institute). Presently, he is in the Bio-derived Products Program of the Aquatic and Crop Resource Development Portfolio of the Life Sciences Division. Dr. Lau’s laboratory (Bioconversion and Sustainable Development Group) and research interests are focused on the discovery, improvement and deployment of enzyme (biocatalyst) technology and associated microbial processes to meet industrial needs and environmental sustainability. Since 1999, Dr. Lau has served as a member of the Organization for Economic Co-operation and Development (OECD) Task Force on Biotechnology for Sustainable Industrial Development. He was a theme leader on platform chemicals of the Canadian Triticale Biorefinery Initiative, funded by Agriculture and Agri-Food Canada through the Agricultural Bioproducts Innovation Program.
- Member of the FQRNT Centre of Green Chemistry and Catalysis
- Distinguished Research Fellow (2015- ) at Tianjin Institute of Industrial Biotechnology, China
- Editorial boards of Applied and Environmental Microbiology and Journal of Microbiological Methods
- Visiting Professorship for Senior International Scientists of the Chinese Academy of Sciences in 2011
Chemicals, Bioproducts and Value Creation Through Enzyme Technology and Innovation
Quality Living Through Chemurgy and Green Chemistry
There are two kinds of biomass in this world - an infinite microbial biomass and a renewable plant-based biomass. Microbes, through the use of diverse enzymes or whole cells, can be harnessed to provide a sustainable supply of goods (e.g., chemicals, polymers) and services (bioconversion, biocatalysis, biotransformation, etc.) from a variety of biological raw materials and feedstock for the benefit of humankind.
Green chemistry via biocatalysis and bioprocesses is a fundamental tool used to address environmental protection and sustainability. It has been viewed as a new environmental priority. Through the use of isolated enzymes or whole cell systems, biocatalysis has become an increasingly important technology for producing compounds of high value for the chemical and pharmaceutical industries and environmental applications as well.
Chemurgy (root word: chemistry [chemi] and work [ergon];urgy – Greek word for work) is the development of new industrial chemical products from organic raw materials, especially those from agricultural biomass.
Journal Covers Collection
- Li, G., Ren J, Yao, P., Duan Y., Zhang, H., Wu, Q., Feng, J., Lau, PCK, Zhu, D. (2014) Deracemization of 2-methyl-1, 2, 3, 4-tetrahydroquinoline using mutant cyclohexylamine oxidase obtained by iterative saturation mutagenesis. ACS Catalysis. 4: 903-908.
- Morley, K., Grosse, S., Leisch, H. and Lau, PCK. (2013) Antioxidant canolol production from a renewable feedstock via an engineered decarboxylase. Green Chemistry, 15: 3312-3317.
- Xu, Y., Grosse, S., Iwaki H., Hasegawa, Y., Lau PCK (2013). Characterization of CpdC, a large-ring lactone hydrolyzing enzyme from Pseudomonas sp. strain HI-70, and its use as a fusion tag facilitating overproduction of proteins in Escherichia coli. Appl. Environ. Microbiol. 79: 7091-7100.
- Leisch, H., Shi, R., Grosse, S., Morley, K., Bergeron, H., Cygler, M., Iwaki, H., Hasegawa,Y. and Lau P.C.K. (2012) Cloning, Baeyer-Villiger biooxidations, and structures of camphor pathway 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase of Pseudomonas putida ATCC 17453. Appl. Environ. Microbiol. 78:2200-2212.
- Xiao, Z., Wu, M., Beauchemin, M., Groleau, D. and Lau, P.C.K. (2011) Direct fermentation of triticale starch to lactic acid by Rhizopus oryzae. Ind. Biotechnol. 7: 129-134.
- Leisch, H., Morley, K., and Lau, P.C.K. (2011) Baeyer-Villiger monooxygenases: More than just green chemistry. Chemical Reviews: Enzymes in Catalysis Thematic issue; 111 (7):4165-4222.
- Grosse, S., Bergeron, H., Imura, A., Boyd, J., Wang, S., Kubota, K., Miyadera, A., Sulea, T., and Lau, P. C. K. (2010) Nature versus nurture in two highly enantioselective esterases from Bacillus cereus and Thermoanaerobacter tengcongensis, Microb. Biotech. 3: 65-73.
- Mirza, A., Yachnin, B.J., Wang, S., Grosse, S., Bergeron, H., Imura, A., Iwaki, H., Hasegawa,Y., Lau, P.C.K. and Berghuis., A.M. (2009) Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor. JACS 131(25): 8848-8854.
- Xiao, Z., Bergeron, H., Grosse, S., Beauchemin, M., Garron, M.-L., Shaya, D., Sulea, T., Cygler, M., and Lau, P. C. K. (2008) Improving the thermostability and activity of a pectate lyase by single amino acid substitutions using a strategy based on TM - guided sequence alignment, Appl. Environ. Microbiol. 74:1183-1189.
- Iwaki, H., Muraki, T., S. Ishihara, Y. Hasegawa, K. Rankin, T. Sulea, J. Boyd, and P.C.K. Lau (2007). Characterization of 2-nitrobenzoate catabolic genes nbaAB encoding a novel 2-nitrobenzoate nitroreductase and a 2-hydroxylaminobenzoate mutase, and their adjacent chemotactic gene nbaY in Pseudomonas fluorescens strain KU-7. J. Bacteriol. 189: 3502-3514.
Other Recent Publications
- Yachnin, BJ, McEvoy, MB, MacCuish, RJD, Morley, KL, Lau, PCK, Berghuis, AM. (2014) Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis. ACS Chem. Biol. 9: 2843-2851.
- Xiao, X., Wu, M., Grosse, S., Beauchemin, M., Lévesque, M., and Lau, PCK. (2014) Genome mining for new α-amylase and glucoamylase encoding sequences and high level expression of a glucoamylase from Talaromyces stipitatus for potential raw starch hydrolysis. Appl. Biochem. Biotechnol., 172:73-86.
- Xiao, Z., Grosse, S., Bergeron, H., Lau, PCK. (2014) Cloning and characterization of the first GH10 and GH11 xylanases from Rhizopus oryzae. Appl. Microbiol. Biotechnol. 98: 8211-8222.
- Lau, P.C.K. and Grosse, S. (2013) The fundamentals and fun of biocatalysis. In Marine enzymes for biocatalysis: sources, biocatalytic characteristics and bioprocesses of marine enzymes. A. Trinconi (Ed.) Woodhead Publishing Ltd (doi: 10.1533/9781908818355.1.17). pp17-69.
- Bocedi A., Fabrini, R., Farrotti, A., Stella, L., Ketterman, AJ., Pedersen, JZ., Allocati, N., Lau, PCK., Grosse, S., Eltis, LD., Ruzzini, A., Edwards, TE., Morici, L., Grosso, ED., Guidoni, L., Bovi, D., Bello, ML., Federici, G., Parker, MW., Board, PG., Ricci, G. (2013) The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: A proposal for an evolutionary driving force. J. Biol.Chem, 288:24936-47.
- Li, G., Ren, J., Iwaki, H., Zhang, D., Hasegawa, Y., Wu, Q., Feng, J., Lau, PCK., and Zhu, D. (2013). Substrate specificity profiling of cyclohexylamine oxidase and its mutants reveals new biocatalytic potential in deracemization of racemic amines. Appl. Microbiol. Biotechnol. 98:1681-1689.
- Xu, Y., Salmi, Y., Kloser, E., Perrin, F., Grosse, S., Denault, J. and Lau, PCK. (2013) Feasibility of nanocrystalline cellulose production by endoglucanase treatment of natural bast fibres. Ind. Crops Products, 51: 381-384.
- Kim, Y.H., Song, W.S.,Go, H., Cha,C., Lee,C.,Yu, M., Lau, P.C.K., and Lee, K. (2013) 2-Nitrobenzoate 2-nitroreductase (NbaA) switches its substrate specificity from 2-nitrobenzoic acid to 2,4-dinitrobenzoic acid under oxidizing conditions. J. Bacteriol. 195:180-192.
- Leisch, H., S. Grosse, K. Morley, K. Abokitse, F. Perrin, J. Denault, and P.C.K. Lau. (2013) Chemicals from agricultural biomass: Chemoenzymatic approach for production of vinyl phenols and polyvinylphenols from phenolic acids. Green Processing and Synthesis 2:7-17.
- Mirza, I. A., D.L. Burk, B. Xiong, H. Iwaki, Y. Hasegawa, S. Grosse, P.C.K. Lau and A. M. Berghuis. (2013). Structural analysis of a novel cyclohexylamine oxidase from Brevibacterium oxydans IH-35A. PLosOne 8(3) e60072.
- Iwaki H., S. Grosse, H. Bergeron,H. Leisch, K. Morley, Y. Hasegawa, and P.C.K. Lau. (2013) Camphor pathway redux: Functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl. Environ. Microbiol. 79(10) 3282-3293.
- Kohler, G.A, and P.C.K. Lau (2013) Genomics, microbiomes, single cell analysis and next generation sequencing (editorial) J. Microbiol. Methods. 95:400.