The Roles in the Cell and the Reaction Capacities of Amylase Enzyme

Study of Amylase
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Study of Amylase
Introduction
Research on the enzyme is a special study that many scientists advocate for. An enzyme is any substance that catalyzes reactions in living organisms (Miao et al., 2018). It promotes the regulation of chemical reactions without altering the body of an organism. Amylase is an enzyme that catalyzes a reaction of starch to sugars. It is majorly located in the saliva of animals or human beings. Amylase is also produced from some plants and bacteria. The reaction of starch to sugar is also noted as hydrolysis. Therefore, amylase promotes hydrolysis. The paper probes amylase, one of the common enzymes studied in chemical and biological reactions, by considering its role and reaction capacities.
Importance
Amylase plays a significant role in breaking complex carbohydrates, polysaccharides, and starch bonds. The enzyme takes this direction to produce simple sugars that the body can easily absorb. During food digestion, amylase is the first enzyme considered to initiate the reaction. Therefore, while eating, it is necessary to properly chew food to increase the surface area for salivary amylase. It is responsible for breaking down the food eaten to liberate different chemical nutrients. Amylase is produced in the mouth, pancreas, and small intestine. Therefore, it is responsible for stimulating chemical reactions during digestion.
Role in the Cell
The role of amylase in the cell is to break consumed food into starch and carbohydrate molecules. Amylase is created in two specific places, and it is generated in the salivary gland and the pancreatic cell (Dhital et al., 2015). The amylase identified in the two areas is necessary and plays a significant role in catalyzing reactions. Therefore, it is justifiable that amylase plays a substantial role in the cell, especially in mammals.
Metabolic Pathway
Metabolic pathways are significant for enzymes since they consist of chemical reactions within a given cell (Miao et al., 2018). They constitute intermediates, products, and reactants. Therefore, in the chemical reaction, amylase is an intermediate during the reaction. The reactants are the starch and other components such as polysaccharides, while the products are simple. Therefore, the identified path is one way.
Chemical Reaction
The primary chemical reaction that happens in amylase as the catalyst is hydrolysis. It involves breaking the substrate molecule by adding a water component, as shown in figure 1. The resultant elements include glucose molecules. The amylase is responsible for speeding up the reaction. Therefore, the chemical reaction cannot occur without amylase.
Figure 1: Amylase chemical reaction
Source (Miao et al., 2018).
Comparison
The type of reaction that amylase catalyzes is an enzymatic reaction. The enzymatic reaction is a type of chemical reaction that relies on enzymes for catalysis. On the other hand, non-enzymatic reactions do not require enzymes (Suckling, 2012). Therefore, enzymatic reactions take minimum time and produce more energy than non-enzymatic. Lastly, cofactors can be divided into coenzymes and inorganic ions, while the factors are specific for inorganic ions.
Methods
How the enzyme was studied
The researcher studied salivary amylase by measuring its activity. Before the study, the researcher considered different reaction elements, including product, enzyme, and substrate. The enzyme-catalyzed reaction is defined as substrate (Whitaker et al., 2002). The substrate is further converted to products in the presence of an enzyme (amylase). The study was based on the measurement of the appearance of the product. Therefore, the study involved three components, starch, enzyme, and products. The starch represented the substrate, while the enzyme was used as amylase. Besides, the product expected was maltose. To identify, the researcher measured the rate at which the starch reacted. However, the reaction is only visible whenever iodine is considered. The reaction between the starch and iodine results in purple color; thus, it was easy to determine the end of the reaction.
The study's main purpose was to justify the action of amylase on the starch. The intensity of the purple color was also considered to identify the rate of action of the enzyme. In this case, a spectrometer was used. After identifying the enzyme, it would be easy to conduct other studies such as enzyme elucidation. One of the major activities before analyzing the enzyme is effectively determining its presence and activity. Therefore, the study's experimental approach was considered the better approach to understand the enzymatic reaction. The researcher considered all the factors that correlated to the enzyme during the study. The researcher further conducted intensive literary research to understand the composition of the enzyme, the binding reactants, the mechanism, and its regulation. Therefore, due to the intense study of the identified components, the researcher successfully addressed different components of amylase.
Enzyme Elucidation
The fluorinated substrate analog achieved the elucidation of the enzyme mechanism. The process was considered a mechanical probe. The researcher used fluorine since it is necessary for understanding the mechanical growth of amylase. Fluorinated substrate probes are effective since they enable researchers to understand the catalytic reaction mechanisms (Biswanger, 2017). Therefore, it was effective to conduct and understand different approaches such as purifications.
Purification Approaches
The purification was done using the chromatographic approach. The researcher dialyzed Millipore after concentrating on it. The product was eventually exposed to anion-exchange chromatography, after which the enzyme was eluded, as shown in figure 2. The fractions containing amylase enzyme were eventually pooled using the filtration system and equilibrated to ensure the products' successful pooling. The purification was effective since it allowed the researcher to obtain alpha-amylase specifically. Purification is an essential aspect of studying an enzyme since it determines the quality and the type of an enzyme that one identifies. The process was effective since it created a better platform for understanding the mechanical nature of amylase. Therefore, the amylase purification was effective and chemically viable.
Figure 2: Amylase Purification
Crystal Structure Conditions
Specific conditions were considered during the study of the enzyme. A 250 ml conical flask is necessary for enzyme production to limit any possible pollution or effects on the crystal structure. Some of the factors include soluble starch, yeast. The main considered condition is 200 rpm. The condition is necessary since it would keep the enzyme in the crystal nature. The condition is effective for the enzymatic reactions since it prevents the enzyme from denaturing. Lastly, the researcher considered lower temperatures to prevent possible heating. Therefore, the identified conditions were necessary for crystallization.
Enzymatic Assays
Qualitative Approach
The first essay focused on the qualitative approach to understanding the enzyme activity. The essay is essential since it allows the researcher to understand the enzyme's qualitative characteristics that are likely to impact the enzymatic mechanism (Copeland, 2000). The effective approach was cut assay with specific modification. The researcher prepared agar plates with 0.01 starch and 0.15 cut assay. Solidification was considered, after which the researcher filtered the culture. After the filtration, the researcher incubated the well for 12 hours, maintaining 50 degrees Celsius. The resea...