Search results
Results From The WOW.Com Content Network
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
Trypsin inhibitor is present in various foods such as soybeans, grains, cereals and various additional legumes. [10] The main function of trypsin inhibitors in these foods is to act as a defense mechanism. By having this harmful component wild animals learn that any food that contains trypsin inhibitor is a food to avoid.
Acidification − Browning enzymes, as other enzymes, are active at a specific range of pH. For example, PPO shows optimal activity at pH 5-7 and is inhibited below pH 3. [16] Acidifying agents and acidity regulators are widely used as food additives to maintain a desired pH in food products.
Physiologically normal intracellular pH is most commonly between 7.0 and 7.4, though there is variability between tissues (e.g., mammalian skeletal muscle tends to have a pH i of 6.8–7.1). [4] [5] There is also pH variation across different organelles, which can span from around 4.5 to 8.0. [6] [7] pH i can be measured in a number of ...
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 .
Generally, however, these guidelines agree that highly processed foods contain high amounts of total and added sugars, fats, and/or salt, low amounts of dietary fiber, use industrial ingredients ...
Despite the bactericidal effects of ethanol, acidifying effects of fermentation, and low oxygen conditions of industrial alcohol production, bacteria that undergo lactic acid fermentation can contaminate such facilities because lactic acid has a low pKa of 3.86 to avoid decoupling the pH membrane gradient that supports regulated transport.
In contrast, in site-directed enzyme immobilization, the support can be linked to a single specific amino acid (generally N- or C-termini) in a protein molecule away from the active-site. This way maximal enzyme activity is retained due to the free access of the substrate to the active-site.