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conferenceseries.com
Volume 7, Issue 1 (Suppl) J Biotechnol Biomater
ISSN: 2155-952X JBTBM, an open access journal
March 20-21, 2017 Rome, Italy
&
15th World Congress on
2nd International Conference on
Biotechnology And Biotech Industries Meet
Enzymology and Molecular Biology
Enzymology & Mol. Biology 2017
Biotechnology Congress 2017
March 20-21, 2017
J Biotechnol Biomater 2017, 7:1(Suppl)
Biotransformation of inexpensive natural platform chemicals to higher value flavor compounds
Hayley W S Tsang1, Serena Gargiulo2, Charlotte Catignani2, Gary W Black1 and Georgios Koutsidis1
1Northumbria University, UK
2Treatt Plc, UK
The project focuses on biotranformations of relative inexpensive natural platform chemicals derived from distillation of essential
oils and non-volatile compounds to higher value flavour compounds through biocatalysis. Experimental processes using a range
of enzymes (cytochrome P450s, aldo-keto reductases/alcohol dehydrogenases and carotenoid cleavage oxygenases) from various
sources have been previously described and a number of high value flavour components produced from inexpensive starting
materials. In this project similar processes will be used to transform platform molecules using an array of enzymes focussed around
those previously described.
Different structure-oriented design of selective butyrylcholinesterase probe and its application in drug
discovery
Wen-Chao Yang, Shu-Hou Yang, Qi Sun and Guang-Fu Yang
Central China Normal University, China
The two major human cholinesterases are acetylcholinesterase (AChE; EC 3.1.1.7) and butyrylcholinesterase (BChE; EC 3.1.1.8),
and are very important enzymes in multiple areas such as pharmacology, neurobiology and toxicology due to their significant
roles in human body and health. Although the biological function is uncertain, the BChE levels have been implicated in lipid
metabolism and various human diseases such as liver damage, cirrhosis, Alzheimer’s disease (AD) and liver metastasis. BChE is also
responsible for detoxifying xenobiotics like organophosphates and cocaine and is a well-known biomarker for clinical diagnosis.
Thus, the quantification of BChE activity and its inhibition is not only important in diseases diagnosis, but also indispensable for drug
discovery. We report on the different structure-oriented design and application of a selective fluorogenic molecular probe (BChE-
FP) for human butyrylcholinesterase (BChE). This probe, rationally designed by mimicking the native substrate and manipulating
the steric feature of the recognition group of designed probes targeting the structural difference of the active sites for BChE and
acetylcholinesterase (AChE), exhibits near-zero background fluorescence but produce remarkable fluorescence enhancement upon
the catalysis by BChE in a fast biochemical reaction. To the best of our knowledge, BChE-FP is the first probe that can discriminate
BChE from AChE, which is successfully applied for BChE inhibitor screening and characterization under physiological conditions,
and BChE detection in human serum. These results demonstrate that this molecular probe can function as a useful molecular tool for
high-throughput drug discovery against BChE-related diseases, as well as the biosensing for neuromuscular blocking agents.