Scientific Program

Conference Series Ltd invites all the participants across the globe to attend 20th Global Congress on Biotechnology Park Inn by Radisson Hotel London, UK.

Day 2 :

OMICS International Biotech Congress 2018 International Conference Keynote Speaker Ibrahim Abdulhalim photo

Ibrahim Abdulhalim is a Professor at the Electro-optical Engineering Unit at Ben-Gurion University of the Negev. He worked in academic institutions and companies such
as the OCSC in University of Colorado Boulder, the ORC at Southampton University, the Thin Films Center of the University of Western Scotland, in KLA-Tencor, Nova and
GWS Photonics. He has published over 200 articles, two books, 10 chapters and has 20 patents. He is a fellow of IoP and SPIE and an Associate Editor for the Journal
of NanoPhotonics and for the Journal of Imaging.


Evanescent wave optical biosensors allow specifi c sensing by using a surface binding layer which enhances the capture
of specifi c bio-entities within the nanoscale neighborhood to the sensor surface. However, this evanescence region is
sometimes too small at the scale of few tens of nanometers which prevents obtaining monotonic signal versus concentration
when the bio-entities are larger than the optical penetration depth. Th e purpose of this study is to describe methods for
sensing both small (molecules, viruses, etc.) and large bioentities (cells, large molecules) using plasmonic sensors with
tunable penetration depth. During the last few years, we have been developing diff erent structural and system confi gurations
for improving the performance of plasmonic biosensors based on improving the reading method and enhancing the local
electromagnetic (EM) fi eld further for the purpose of improving the sensitivity and lowering the detection limit based on
SPR, SERS and SEF. Th e structural improvements include: (i) planar thin metal fi lms combined with dielectric fi lms, (ii)
periodic metallic structures on planar substrate, (iii) nanosculptured thin fi lms prepared by the glancing angle deposition
technique. (iv) long range self-referenced plasmonic confi gurations, and lately, (v) combination of nanostructures with thin
metal fi lms for coupling of extended surface plasmons (ESP) to localized surface plasmons (LSP). Th e system improvements
include: (i) diverging beam approach in the angular mode, (ii) polarimetric spectral mode, (iii) image and signal processing.
Particularly, we have shown recently that even much higher enhancement of the EM fi elds is obtained by exciting the LSPs
through extended surface plasmons generated on a semi-infi nite metallic fi lm surface. Biotechnology applications will be
presented for sensing biomolecules and cells in water and in blood. In spite of the technological advances in optics, the need
for developing molecular binding layer to improve the specifi city is still in demand from the biotechnology community.

Keynote Forum

Jennifer A Littlechild

University of Exeter, UK

Keynote: Thermophilic enzymes with applications for industrial biocatalysis

Time : 11:40-12:20

OMICS International Biotech Congress 2018 International Conference Keynote Speaker Jennifer A Littlechild photo

Jennifer A Littlechild is an Emeritus Professor of Biological Chemistry and has established the Henry Wellcome Centre for Biocatalysis at Exeter University in 2003. Her
research studies involve the structural and mechanistic characterisation of a range of enzymes from thermophilic bacteria and archaea that have industrial applications.
She has published over 200 publications in refereed high impact journals and presented her research work internationally. She has coordinated EU related project THERMOGENE
and was a partner in a consortium grant HOTZYME. In UK she is funded from BBSRC and Innovate UK. These grants involve both large industrial companies
and SME enterprises. She has supervised over 40 PhD students and acts as External Examiner for other PhD and Masters Students. She is the UK representative and
Vice Chair of the European Section of Applied Biocatalysis and a Member of EU advisory committees for Industrial Biotechnology.


There is an increasing demand for new enzymes with enhanced performance and/or novel functionalities that provide
savings in time, money and energy for industrial processes in the areas of high value chemical production and other
white biotechnology applications. Only a small proportion of nature’s catalysts have been utilised for industrial biotechnology.
Th e number of enzymes explored to date remains within the range of 1-2% of known biodiversity. A problem with using
enzymes for industrial biocatalysis reactions is oft en their stability under the harsh conditions employed. Th e use of naturally
thermostable enzymes isolated from hot environments are more stable to high temperatures, extremes of pH and exposure
to organic solvents. Th e projects HOTZYME and THERMOGENE have identifi ed hydrolase and transferase enzymes of
industrial interest isolated from high temperature environments around the world. Th ese have been isolated from thermophilic
bacterial and archaeal genomes and metagenomes. A selection of these novel thermostable enzymes including cellulases,
carboxylesterases, lactonases, epoxide hydrolases, transketolases, hydroxymethyl transferases and transaminases have been
characterized both biochemically and structurally. Transaminase enzymes have received special attention for the production
of chiral amines which are important building blocks for the pharmaceutical industries. Th ese enzymes catalyse the reversible
transfer of an amino group from a donor substrate onto a ketone/aldehyde or sugar acceptor molecule. Th ey can be subdivided
into 6 classes. Th e less studied class 4 (branched chain) (R) selective, class 5 (S) selective and class 6 (sugar) enzymes have
been identifi ed. An example of the archaeal class 4 enzyme from Archaeoglobus fulgidus; a thermostable class 5 archaeal
transaminase from Sulfolobus solfataricus and class 6 sugar transaminase from A. fulgidus. Two new enzymes with interesting
substrate specifi city and stereo-selectivity have been discovered which have already been demonstrated at industrial scale for
the production of new chiral chemical building blocks.

Keynote Forum

Kam Bo Wong

The Chinese University of Hong Kong, China

Keynote: How urease accessory proteins coupled GTP hydrolysis/binding to nickel delivery to urease?

Time : 12:20-13:00

OMICS International Biotech Congress 2018 International Conference Keynote Speaker Kam Bo Wong photo

Kam Bo Wong obtained his BSc and MPhil from the Chinese University of Hong Kong. He then pursued his PhD degree in the laboratory of Prof. Alan Fersht at the University
of Cambridge. After Postdoctoral training in the University of Washington and University of Cambridge, he joined the Chinese University of Hong Kong in 1999, where
he is now a Professor at the School of Life Sciences. His research interests are on the structure-function studies of proteins. His research group uses multi-disciplinary
techniques, including protein engineering, biophysical characterization, computational methodologies, and structure determination by NMR and X-ray crystallography, to
study how proteins function on the atomic and molecular levels.


Urease is a nickel-containing metalloenzyme that catalyzes the hydrolysis of urea into ammonia and carbon dioxide. Th is
enzymatic reaction, which produces the acid-neutralizing ammonia, is essential for the survival of Helicobacter pylori in
human stomach. In Helicobacter pylori, nickel ions delivery for urease maturation is assisted by four urease accessory proteins,
UreE, UreF, UreG and UreH. Specifi c protein-protein interactions among these urease accessory proteins are essential for the
control of binding/release of nickel along the metal delivery pathway. We have previously determined the crystal structures of
UreF/UreH and GDP-bound-UreG/UreF/UreH complexes. Upon binding of UreH, the C-terminal residues of UreF are induced
to form an extra helix and a loop structure stabilized by Arg-250. Th ese conformational changes facilitate the recruitment of
UreG to the UreG/UreF/UreH complex, which is essential to urease maturation. Recently, we have determined the crystal
structure of the nickel/GTP-bound UreG dimer, which reveals how GTP hydrolysis induces conformational changes that
induce dissociation of UreG from the UreG/UreF/UreH complex and the release of nickel to the urease.