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Alkaline phosphatase is commonly used in the dairy industry as an indicator of successful pasteurization. This is because the most heat stable bacterium found in milk, Mycobacterium paratuberculosis, is destroyed by temperatures lower than those required to denature the enzyme. Therefore, its presence is ideal for indicating failed pasteurization.
Pasteurized milk in Japan A 1912 Chicago Department of Health poster explains household pasteurization to mothers.. In food processing, pasteurization (also pasteurisation) is a process of food preservation in which packaged foods (e.g., milk and fruit juices) are treated with mild heat, usually to less than 100 °C (212 °F), to eliminate pathogens and extend shelf life.
Pasteurization is widely used to prevent infected milk from entering the food supply. The pasteurization process was developed in 1864 by French scientist Louis Pasteur, who discovered that heating beer and wine was enough to kill most of the bacteria that caused spoilage, preventing these beverages from turning sour. The process achieves this ...
In biochemistry, a phosphatase is an enzyme that uses water to cleave a phosphoric acid monoester into a phosphate ion and an alcohol. Because a phosphatase enzyme catalyzes the hydrolysis of its substrate , it is a subcategory of hydrolases . [ 1 ]
A simple qualitative method to determine the presence of phosphate ions in a sample is as follows. A small amount of the sample is acidified with concentrated nitric acid, to which a little ammonium molybdate is added.
Fluorimetry is widely used by the dairy industry to verify whether pasteurization has been successful. This is done using a reagent which is hydrolysed to a fluorophore and phosphoric acid by alkaline phosphatase in milk. [2] If pasteurization has been successful then alkaline phosphatase will be entirely denatured and the sample will not ...
Acid phosphatase (EC 3.1.3.2, systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase .
The enzyme phosphoserine phosphatase (EC 3.1.3.3) catalyzes the reaction O-phospho-L(or D)-serine + H 2 O L(or D)-serine + phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is O-phosphoserine phosphohydrolase.