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]
Many proteins are extremely temperature-sensitive, and in many cases can start to denature at temperatures of only 4 degrees Celsius. Within the microchannels, temperatures exceed 4 degrees Celsius, but the machine is designed to cool quickly so that the time the cells are exposed to elevated temperatures is extremely short ( residence time 25 ...
Soil fertility and plant production: Use of enzyme activity as indicator of soil quality [71] [72] Composting. Impacts of composting municipal solid waste on soil microbial activity [10] Soil organic matter stability: Impact of temperature and soil respiration on enzymatic activity and its effect on soil fertility [73] Climate change indicators
It is regulated by moisture, temperature, and bacteria. [5] This process does not occur at a uniform rate and thus some proteins are degraded during early decomposition, while others are degraded during later stages of decomposition. During the early stages of decomposition, soft tissue proteins are broken down. These include proteins that:
Ascorbate is a known cofactor of myrosinase, serving as a base catalyst in glucosinolate hydrolysis. [1] [7] For example, myrosinase isolated from daikon (Raphanus sativus) demonstrated an increase in V max from 2.06 μmol/min per mg of protein to 280 μmol/min per mg of protein on the substrate, allyl glucosinolate (sinigrin) when in the presence of 500 μM ascorbate. [4]
Thermus aquaticus is a species of bacteria that can tolerate high temperatures, one of several thermophilic bacteria that belong to the Deinococcota phylum. It is the source of the heat-resistant enzyme Taq DNA polymerase, one of the most important enzymes in molecular biology because of its use in the polymerase chain reaction (PCR) DNA amplification technique.
These enzymes convert skatole to a reactive intermediate, 3-methyleneindolenine, which damages cells by forming protein adducts (see fog fever). [16] With the testicular steroid androstenone, skatole is regarded as a principal determinant of boar taint. [17] High amounts of skatole stored in the fat tissue of pigs corresponds with boar taint.
Alliinases are part of the plant's defense against herbivores. Alliinase is normally sequestered within a plant cell, but, when the plant is damaged by a feeding animal, the alliinase is released to catalyze the production of the pungent chemicals. This tends to have a deterrent effect on the animal.