Protease is an enzyme that has the ability to break the peptide bonds of proteins into amino acids (Mitchell et al., 2007). Protease breaks down peptide bonds to engender amino acids and other more diminutive peptides. It can be isolated from a mixture of sources such as plants, animals and microbes (fungi and bacteria). It has broad application and for many years used in many fields such as in food and detergents industries (Yandri et al., 2008). Except alkaline protease all protease works best in acidic conditions which has its optimal activity shown in alkaline (basic) pH (Mitchell et al., 2007). Proteases may be acidic, neutral and alkaline in nature .Alkaline proteases have pH range in between 7.0 and 14.0, but between pH 9.0 and 11.0 …show more content…
They are active at neutral to alkaline pH. Alkaline protease holds a monstrous par take in world catalyst market. They represent around 2/3rd offer of the of overall cleanser catalyst sales (fig1). Market analysis reports indicate a steady growth for these enzymes. Alkaline proteases have either a serine amino acid serine or a metal ion at the catalytic centre. These enzymes have been reported to operate under brutal physiological state of temperature of (20 to 70oC), pH (up to 11) and in presence of organic solvents, cleansers and so on. Although alkaline proteases are primarily used as detergent additives, they have extensive variety of uses in the fields of research and commercial venture such as food, leather, textile, photography …show more content…
They are produced by an extensive variety of microorganisms including microscopic organisms, molds, and yeasts further more mammalian tissues. The vast majority of the commercial alkaline proteases were separated from Bacillus species (Maurer, 2004). An impressive number of fungal species are known to produce extracellular basic proteases, for example, Conidioboluscoronatus (Phadatare et al., 1993), Arthrobotrysolgospora (Tunlid et al.,1994), Trichodermaharzianum (Dunaevsky et al., 2000), Cephalosporium sp. KM388 (Tsuchiya et al.,1987) and Aspergillus Fumigatus (Wang et al.,2005). Alkaline proteases of microbial origins have significant mechanical potential because of their biochemical differences and wide applications in tannery and food industries, medicinal formulations, cleansers and procedures like waste treatment, silver recuperation and determination of amino corrosive blends (Rao et al., 1998; Agarwal et al., 2004). The alkaline proteases locate their biggest use in house hold clothing with an overall yearly production of cleansers of more or less 13 billion tons (Nehra et al.,
Serratia marcescens, a Gram-negative bacillus, was originally and solely considered a biological marker in the medicinal industry, due to its highly natural red pigment: Prodigiosin (Hejazi and Falkiner, 1997). The pigment has numerous roles within bacteria, which can be further translated into the pharmaceutical and medical domain. This bacterium naturally occurs in water, soil, on plants as well as in humans and animals (Khanafari et al, 2006), where it is deemed an opportunistic pathogen.
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
Because of its undeniable and scientifically-proven powerful antioxidant properties, catalase enzyme has a wide commercial application. Primarily in combination with the enzyme glucose oxidase, catalase is used as a preserving system in mayonnaise and egg products such as whole eggs or dried egg white, in the preparation of milk and cheese, in the manufacture of baked goods, beverages, textile industry, cosmetic industry (as face mask), and in cleaning agents for contact lenses, for the elimination of the hydrogen peroxide that is present in some products, (Worthington Biochemical Corporation,
Alkaline Phosphatase (APase) is an important enzyme in pre-diagnostic treatments making it an intensely studied enzyme. In order to fully understand the biochemical properties of enzymes, a kinetic explanation is essential. The kinetic assessment allows for a mechanism on how the enzyme functions. The experiment performed outlines the kinetic assessment for the purification of APase, which was purified in latter experiments through the lysis of E.coli’s bacterial cell wall. This kinetic experiment exploits the catalytic process of APase; APase catalyzes a hydrolysis reaction to produce an inorganic phosphate and alcohol via an intermediate complex.1 Using the Michaelis-Menton model for kinetic characteristics, the kinetic values of APase were found by evaluating the enzymatic rate using a paranitrophenyl phosphate (PNPP) substrate. This model uses an equation to describe enzymatic rates, by relating the
As Ph levels get closer to 8 enzyme activity will increase, because this is the optimum Ph level for this enzyme.
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.
Pepsin assists in the breaking down of proteins into small peptides in the use of amino acids, and pepsin is released in the stomach. This explains that the environment must be acidic in order to function properly and with the detergent being in an alkaline state, it would be lucky if there was any activity which resulted from the detergent. This all assists in understanding the effect that pH has on enzyme activity, by showing various levels of pH in affecting the activity of pepsin. Limitations in this experiment may have been an access to materials which were at a quality state, due to it being very difficult to find pure 100 % pepsin and other Materials. Improvements could be made in this experiment by including more materials, to show different levels of pH, which can increase the understanding of why different levels of pH lead to different results in relative activity of pepsin.
When eaten, protein is broken down into amino acids. Proteins and amino acids are used for almost every metabolic process in the body, and are the building blocks for every tissue in your body.
The Effect of pH on Enzyme Activity. pH is a measure of the concentration of hydrogen ions in a solution. The higher the hydrogen ion concentration, the lower the pH. Most enzymes function efficiently over a narrow pH range. A change in pH above or below this range reduces the rate of enzyme reaction. considerably.
Proteolysis is a very complex and the most important of all the primary biochemical reactions occurring in the cheese during ripening. Proteolysis in hard Italian cheeses is no different from the other hard or semi hard cheeses. The high salt and low moisture concentration, temperature and persistence of gradients of NaCl are some of the factors which affect proteolysis in cheese during ripening. Due to its importance, the enzymes influencing proteolysis have been reviewed on a large scale from the past two decades. Proteolysis contributes in forming the soft texture of the cheese by the hydrolysis of casein matrix and the reduction in the water activity (aw) due to the changes taking place in water binding by new carboxylic acid and the formation of amino groups during hydrolysis. The production of amino acids and shorta peptides have a direct effect on flavour during proteolysis, by generating sapid compounds from the cheese, and mainly by supplying free amino acids that are substrates for a series of catabolic reactions which release important flavour compounds. The peptidases and proteinases which catalyse proteolysis during ripening come
The effect of a change in PH on enzymes is the alteration in the ionic
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
The exocrine function of the pancreas is that it produces enzymes that aids in the digestion of food. There are three important enzymes that are crucial in helping with digestion. The first digestive enzyme is amylase. Amylase function is to break down carbohydrates. The amylase enzyme is made in two places: the cells in the digestive tract that produces saliva and the main one specifically found in the pancreas that are called the pancreatic amylase (Marie, Joanne; Media Demand, “What Are the Functions of Amylase, Protease and Lipase Digestive Enzymes”). The amylase in the pancreas passes through the pancreatic duct to the small intestines. This amylase in the pancreas completes the process of digestion of carbohydrates. Consequently, this leads to the production of glucose that gets absorbed into the bloodstream and gets carried throughout the body. The next enzyme that aids in digestion of food is protease. While amylase breaks down carbohydrates, protease breaks down protein. Protease breaks down protein into the building block form of amino acids. The three main proteases that it produces are: pepsin, trypsin and chymotrypsin (Marie, Joanne; Media Demand, “What Are the Functions of Amylase, Protease and Lipase Digestive Enzymes”). Pepsin does not occur in the pancreas but it is the catalysis in starting the digestion of proteins. Trypsin and chymotrypsin are the two proteases that occur in
Protein is in the form of zwitterion in aqueous solution which means it has both negative and positive charge at each end in which the negative charge allocated at the -COOH group while positive charge at the -NH2 group. Ionic interactions occur between both charged amino and carboxyl groups in the side chains of some amino acids in the folded protein. This both group take up the ions produce by the acid and base which then causes them to lose their charge. This disrupts some or perhaps many of the ionic interactions in the protein structure. Therefore, protein is denatured. However, the degree of denaturation by using lemon juice is not obvious compared to other test tube since there is no or only a small amount of white precipitate formed. This may due to the losing of ascorbic acid which is also known as vitamin C as a result of occurring oxidation reaction when it had been exposed to the environment for a long time. Therefore, the acidity of lemon juice is greatly reduced and almost reaches