All about the Amylase Enzyme
You will find the amylase enzyme in your saliva. Amylase aids in converting starch into maltose, a sugar. The moment any food enters your mouth it encounters amylase, the herald of the digestive system. This proactive enzyme is one of the first to go to work on any new culinary arrivals. Unfortunately for it, amylase doesn’t have long to get started since as soon as you swallow it and the food it has taken hold of, amylase gets “turned off.” This is because amylase has a difficult time working in the highly acidic environment of the stomach.
Amylase much prefers neutral environments. Don’t worry, however; amylase will get a second shot at your meal once it hits the small intestine. There, the pancreas manufactures more amylase and these newly created enzymes finish converting the starch into the sugar maltose. Then amylase passes the sugar on to his partner, the enzyme, maltase (the enzyme has an “a,” the sugar an “o”). Maltase finishes the job off, converting the sugar maltose into glucose, which is in due order swallowed up by the blood stream.
Why such a complicated process?
The Dietary Missing Link
Part of the reason for this complicated chain may be that the amylase enzyme is a relative new comer in evolutionary terms. Evolutionary biologists believe that Amylase’s development in humans was one of the key evolutionary steps that aided in our species’ ultimate survival and success. The theory goes that at one point our ancestors could only metabolize the sugars from fruits and the proteins from meat. However, at some point, some of our ancestors developed the amylase enzyme, which allowed us to take the first step towards digesting carbohydrates. This was important because it significantly increased the range of possible diets humans could use to survive, helping us not only in times of food scarcity, but possibly, in adapting to diverse new environments as the branches of the human family unfurled throughout the world.
The First Enzyme
The amylase enzyme also played a significant role in the development of the study of bio--chemistry. In 1831, French chemists identified the manner in which saliva broke down starches, transforming them into sugar. It was, however, only two years later that a French chemist working at a borax factory, Anselm Payen, isolated the protein he called “diastase” as compound that was doing the work in the process his colleagues had noticed. And so the first enzyme was born. Years later, it would take on the name it bears today, amylase.
(In an interesting side note, Payen was also the first scientist to use the term cellulose for fat.)
What is an enzyme?
In case it has been a while since you’ve taken a biochemistry class and need a refresher, enzymes are responsible for accelerating chemical processes in the body. If we didn’t have enzymes, we would track digestion with a calendar rather than a clock; in short, without the energy that enzymes speed to us, life as we know it would not be possible.
Technically, enzymes are catalysts, substances that speed up biological processes without themselves undergoing change. A catalyst is like a hammer that you can use over and over again without it changing in the process as well. Enzymes work like this except that they will often lose their shape and their ability to do the process the body makes them for, because of the heat of the processes they are involved in.
Enzymes are also proteins, and since high temperatures can alter proteins, they can also alter amylase. Ion metals and pH levels have a similarly strong effect on enzyme proteins. Also different from normal catalysts is that enzymes have one and only one function. They exist to accelerate only one action in one process; when they are done, they no longer have a reason for being.