“Scientists are boring people doing boring work in boring labs,” I told one of my high

school friend when he wanted to become a mathematician. Little did I know that I would
become one. I initially chose to study chemistry simply because it was easy to find an
industrial job with satisfactory salary in Vietnam. Working in Professor Trinh’s lab on
my first research project as a junior, however, awoke an abiding fascination with
chemical research.

When I asked Prof. T. if I might join his group, he smiled, gave me a bottle of
wastewater from a paper mill and asked: “What can you do with it?” Curious about his
question, I spent days in the library and searching the internet to find documents relating
to this wastewater, hoping to identify a suitable solution to treat it. I discovered that one
good way was to use the wastewater as a material for composite synthesis. I opted to try
to separate lignin from this liquid and to use it as a modifier for phenol-formaldehyde
resol resins to produce PFL (Phenol Formaldehyde Lignin resin), which was then
combined with wood flour to produce adhesive composition. The idea that it was only a
simple matter of adding materials, awaiting the reaction and getting PFL seemed
disappointingly straightforward. But in the first month of this research project, I did
hundreds of reactions without generating the polymer as I had hoped. This failure made
me think more seriously about the research process. I went back to learn more about
polymers, searching for a reason. Then I continued to spend hours and days in the
laboratory, mixing materials, changing different variables [e.g., lignin concentration, ratio
of formaldehyde to phenol lignin (phenol + lignin), temperature, and polymerization
time], waiting for the reaction, failing and doing the same thing over again. Finally I
produced a PFL with promising properties; the material I made was stronger than the one
made from PF (Phenol Formaldehyde Resin). When I held the material I had made, I
knew that, although it took time and effort, doing research well worth it.

From my first biochemistry course, enzymes and their ability to catalyze reactions at a
surprising rate have fascinated me. This interest led me to produce PFL in a new way by
using H2O2/peroxidase instead of alkali to catalyze the copolymerization reaction.
However, I failed. The enzyme I used was not stable in reaction condition. This failure
raised many questions for me: What is an enzymatic reaction’s mechanism? How can an
enzyme be stabilized in reaction condition? These questions ultimately spurred me to
write my thesis about enzyme kinetics. I chose glucoseisomerase as a model for my study
of enzymes’ activity and stability, due to its commercial importance in the production of
high-fructose syrups from starch. Using new equipment (BE1, a Batch Enzyme Reactor),
I calculated the rate at which this enzyme converted glucose to fructose with different
conditions of pH, temperature as well as different concentration of substrate and metal
ion required, such as Mg2+, Co2+. From these measurements, I identified the best
conditions for the enzyme’s activity in free state and immobilized state (in various
support materials). I find it gratifying that my department will be able to use my
knowledge of the BE1 as well as my research data as lessons for future students.

Although the research ventures I describe above were only small forays, they gave me
invaluable experience in independent research/ And, through cooperating with other
members of Prof. Trinh’s research group, my appreciation for the importance of
teamwork skyrocketed. My efficiency and pleasure in solving real problems with critical
thinking were greatly enhanced, as were my laboratory skills. But, most fundamentally,
these projects roused my love for doing research in biological chemistry.

Thus I seek to deepen my knowledge in this area by earning my PhD degree. In

particular, I want to explore enzymes and their complexities far more deeply. I choose
your program not only because of its superior laboratory facilities, but also because of its
human richness: the interesting research relating to enzymes by Dr. Dale Edmondson, Dr.
MacBeth, Dr. Stefan Lutz or Dr. Conticello. For example, the focus of Dr. Edmondson’s
group involves investigations of structure-function relationships in enzymes catalyzing
oxidation-reduction reactions. Or one of Dr. MacBeth’s efforts is designing binuclear
zinc complexes as structural and functional models of co-catalytic metallohydrolases.
These synthetic catalysts could aid in screening selective binuclear enzyme inhibitors and
the development of highly active synthetic hydrolases. These projects absolutely
fascinate me.

Upon completing my doctorate, I aim to work in a university or other institutions in

Vietnam as a lecturer and a researcher. I aspire to work at Hanoi College of Science, one
of the two best science universities in Vietnam, to strengthen research in
biology/chemistry interface.