Food and Public Health

Food and Public Health covers all aspects of food and public health in the form of review articles, original articles, case reports, short communications, letters to the editor, and book reviews. The International Editorial Board is dedicated to producing a high quality scientific journal of interest to researchers and practitioners from many disciplines.

Ya-Lin Lee

Editorial Board Member of Food and Public Health

Associate Professor, Taiwan Agricultural Research Institute, Taiwan

Research Areas

Enzymology, Food Science


1992-1997Ph.DNational Taiwan Ocean University
1991-1992M.S.National Taiwan Ocean University
1985-1990B.ENational Taiwan Ocean University


2009-presentTaiwan Agricultural Research Institute Associate Researcher Biotechnology Division Pathogen-resistant rice breeding
2007Fishery Research Institute Associate Researcher Seafood Technology Division Microalgae application
2003-2007Fu Jen Catholic University Assistant Professor Department of Food Science Rice bran application
2000-2003Fooyin Institute of Technology Assistant Professor Department of Biotechnology Transgenic plants
1999-2000 Taiwan Agricultural Research Institute Postdoctoral research fellowDepartment of Agronomy Medicinal herbs
1997-1999Academia Sinica Postdoctoral research fellow Institute of Botany Plant biotechnology

Publications: Conferences/Workshops/Symposiums/Journals/Books

[1]  Lee, L.C., Chou, Y.L., Chen H.H., Lee, Y.L.* and Shaw, J. F.* 2009. Functional role of a non-active site residue Trp23 on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L1. BBA-Proteins and Proteomics; 1794: 1467–1473.
[2]  Lee, L.C., Liaw, Y.C., Lee, Y.L.* and Shaw, J.F.* 2007. Enhanced preference for π-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L1. BBA-Proteins and Proteomics 1774:959-967
[3]  Lee, L.C., Lee, Y.L.*, Leu, R.J. and Shaw, J.F.* 2006. Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1. Biochem. J. 397:69-76
[4]  Huang, L.C., Lee, Y.L., Huang, B.L., Kuo, C.I., and Shaw, J.F.* 2002. High polyphenol oxidase activity and low titratable acidity as causes of browning of bamboo tissue cultures in vitro. In Vitro Cellular & Developmental Biology Plant 38:358-365.
[5]  Lee, Y.L., Sagare, A.P., Lee, Z.Y., Feng, H.T., Ko, Y.C., Shaw, J.F. and Tsay, H.S.* 2001. Formation of protoberberine-type alkaloids by the tubers of somatic embryo-derived plants of Corydalis yanhusuo. Planta Medica 67:839-842.
[6]  Sagare, A.P., Lee, Y.L., and Tsay, H.S.* 2000. Cytokinin-induced somatic embryogenesis and plant regeneration in Corydalis yanhusuo (Fumariaceae), a medicinal plant. Plant Science 160:139-147.
[7]  Lo, Y.C., Lee, Y.L., Shaw, J.F. and Liaw, Y.C.* 2000. Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli. Acta Cryst. D 56:756-757.
[8]  Lee, Y.L., Su, M.S., Huang, T.H. and Shaw J.F.* 1999. C-terminal His-tagging Results in Substrate Specificity Changes of the Thioesterase I from Escherichia coli. J. Am. Oil Chem. Soc. 76:1113-1118.
[9]  Lin, T.H., Chen, C., Huang, R.F., Lee, Y.L., Shaw, J.F. and Huang, T.H.* 1998. Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase I/protease I: a member of a new subclass of lipolytic enzymes. J. Biomol. NMR 11:363-380.
[10]  Lee, Y.L., Chang, R.C. and Shaw, J.F.* 1997. Facile purification of a C-terminal extended His-tagged Vibrio mimicus arylesterase and characterization of the purified enzyme. J. Am. Oil Chem. Soc. 74:1371-1376.
[11]  Lee, Y.L., Chen, J.C. and Shaw, J.F.* 1997. The thioesterase I of Escherichia coli is an arylesterase and shows stereospecificity for protease substrates. Biochem. Biophy. Res. Comm. 231:452-456.
[12]  Musayev, F.N., Lee, Y.L., Shaw, J.F. and Liaw, Y.C.* 1995. Crystallization and preliminary X-ray crystallographic analysis of arylesterase from Vibrio mimicus. Protein Science 4:1931-1933.