Human applications
Catalase is used in the dairy industry for removing hydrogen peroxide from milk prior to cheese production.[8] Another use is in food wrappers, where it prevents food from oxidizing.[9] Catalase is also used in the textile industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free.[10] A minor use is in contact lens hygiene - a few lens-cleaning products disinfect the lens using a hydrogen peroxide solution; a solution containing catalase is then used to decompose the hydrogen peroxide before the lens is used again.[11] Recently, catalase has also begun to be used in the aesthetics industry. Several mask treatments combine the enzyme with hydrogen peroxide on the face with the intent of increasing cellular oxygenation in the upper layers of the epidermis.
Hydrogen peroxide is a harmful by-product of many normal metabolic processes: To prevent damage, it must be quickly converted into other, less dangerous substances. To manage this problem, the enzyme catalase is frequently used by cells to rapidly catalyse the decomposition of hydrogen peroxide into less reactive gaseous oxygen and liquid water molecules.[8]
The true biological significance of catalase is not completely understood: mice genetically engineered to lack catalase are phenotypically normal, indicating that this enzyme is dispensable for animal life.[9]
Catalase works at an optimum temperature of 37 degrees Celsius, which is approximately the temperature of the human body. Scientific research shows that increasing the temperature by 10 degrees Celsius will double the rate of reaction between the enzyme and the hydrogen peroxide.
Catalase is located in a cellular organelle called the peroxisome.[10] Peroxisomes in plant cells are involved in photorespiration (the use of oxygen and production of carbon dioxide) and symbiotic nitrogen fixation (the breaking apart of diatomic nitrogen (N2) to reactive nitrogen atoms).
Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Pathogens that are catalase positive, such as Mycobacterium tuberculosis, Legionella pneumophila, and Campylobacter jejuni, make catalase in order to deactivate the peroxide radicals, thus allowing them to survive unharmed in the host cell.[5]
2007-03-25 12:06:02
·
answer #2
·
answered by superman 1
·
0⤊
0⤋
When the body detoxifies Zenobiotics, this can result in the generation of reactive oxygen species (ROS). One of the common compounds that is a precurser to ROS is H202 (hydrogen peroxide). Your body actually uses H202 stored in peroxisomes of macrophages to use its oxidative properties to help kill invading micro-organisms. However, H202 can be converted to the Hydroxy Radical during the Fenton Reaction. The hydroxy radical can form DNA adducts leading to mutations. Catylase is produced and used by the body (enzyme) to convert 2xH202 + 02 into 2xH20.
2007-03-25 12:50:39
·
answer #3
·
answered by jsh 1
·
0⤊
0⤋