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Thermostability
In materials science and molecular biology, thermostability is the ability of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative temperature. Thermostable materials may be used industrially as fire retardants. A ''thermostable plastic'', an uncommon and unconventional term, is likely to refer to a thermosetting plastic that cannot be reshaped when heated, than to a thermoplastic that can be remelted and recast. Thermostability is also a property of some proteins. To be a thermostable protein means to be resistant to changes in protein structure due to applied heat. Thermostable proteins Most life-forms on Earth live at temperatures of less than 50 °C, commonly from 15 to 50 °C. Within these organisms are macromolecules (proteins and nucleic acids) which form the three-dimensional structures essential to their enzymatic activity. Above the native temperature of the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thermophile
A thermophile is a type of extremophile that thrives at relatively high temperatures, between . Many thermophiles are archaea, though some of them are bacteria and fungi. Thermophilic eubacteria are suggested to have been among the earliest bacteria. Thermophiles are found in geothermally heated regions of the Earth, such as hot springs like those in Yellowstone National Park and deep sea hydrothermal vents, as well as decaying plant matter, such as peat bogs and compost. They can survive at high temperatures, whereas other bacteria or archaea would be damaged and sometimes killed if exposed to the same temperatures. The enzymes in thermophiles function at high temperatures. Some of these enzymes are used in molecular biology, for example the ''Taq'' polymerase used in PCR. "Thermophile" is derived from the (''thermotita''), meaning heat, and (''philia''), love. Comparative surveys suggest that thermophile diversity is principally driven by pH, not temperature. Classificat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Denaturation (biochemistry)
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, radiation, or heat. If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. Protein denaturation is also a consequence of cell death. Denatured proteins can exhibit a wide range of characteristics, from conformational change and loss of solubility or dissociation of cofactors to aggregation due to the exposure of hydrophobic groups. The loss of solubility as a result of denaturation is called ''coagulation''. Denatured proteins, e.g., metalloenzymes, lose their 3D structure or metal cofactor, and therefore, cannot function. Proper protein folding is key to whether a globular or memb ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Folding
Protein folding is the physical process by which a protein, after Protein biosynthesis, synthesis by a ribosome as a linear chain of Amino acid, amino acids, changes from an unstable random coil into a more ordered protein tertiary structure, three-dimensional structure. This structure permits the protein to become biologically functional or active. The folding of many proteins begins even during the translation of the polypeptide chain. The amino acids interact with each other to produce a well-defined three-dimensional structure, known as the protein's native state. This structure is determined by the amino-acid sequence or primary structure. The correct three-dimensional structure is essential to function, although some parts of functional proteins Intrinsically unstructured proteins, may remain unfolded, indicating that protein dynamics are important. Failure to fold into a native structure generally produces inactive proteins, but in some instances, misfolded proteins have ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Egg White
Egg white is the clear liquid (also called the albumen or the glair/glaire) contained within an egg. In chickens, it is formed from the layers of secretions of the anterior section of the hen's oviduct during the passage of the egg. It forms around fertilized or unfertilized egg yolks. The primary natural purpose of egg white is to protect the yolk and provide additional nutrition for the growth of the embryo (when fertilized). Egg white consists primarily of about 90% water into which about 10% proteins (including albumins, mucoproteins, and globulins) are dissolved. Unlike the yolk, which is high in lipids (fats), egg white contains almost no fat, and carbohydrate content is less than 1%. Egg whites contain about 56% of the protein in the egg. Egg white has many uses in food (e.g. meringue, mousse) as well as many other uses (e.g. in the preparation of vaccines such as those for influenza). Composition Egg white makes up around two-thirds of a chicken egg by weight. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Purification
Protein purification is a series of processes intended to isolate one or a few proteins from a complex mixture, usually Cell biology, cells, Tissue (biology), tissues, or whole organisms. Protein purification is vital for the specification of the function, structure, and interactions of the protein of interest. The purification process may separate the protein and non-protein parts of the mixture, and finally separate the desired protein from all other proteins. Ideally, to study a protein of interest, it must be separated from other components of the cell so that contaminants will not interfere in the examination of the protein of interest's structure and function. Separation of one protein from all others is typically the most laborious aspect of protein purification. Separation steps usually exploit differences in protein size, physico-chemical properties, binding affinity, and biological activity. The pure result may be termed protein isolate. Purpose The protein manufacturin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Xylanase
Endo-1,4-β-xylanase (, systematic name 4-β-D-xylan xylanohydrolase) is any of a class of enzymes that degrade the linear polysaccharide xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls: : Endohydrolysis of (1→4)-β-D-xylosidic linkages in xylans Xylanase plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc.; mammals do not produce xylanases. However, the principal commercial source of xylanases is filamentous fungi. Commercial applications for xylanase include the chlorine-free bleaching of wood pulp prior to the papermaking process, and the increased digestibility of silage (in this aspect, it is also used for fermentative composting). Apart from its use in the pulp and paper industry, xylanases are also used as food additives to poultry ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phytase
A phytase (''myo''-inositol hexakisphosphate phosphohydrolase) is any type of phosphatase enzyme that catalyzes the hydrolysis of phytic acid (myo-inositol hexakisphosphate) – an indigestible, organic form of phosphorus that is found in many plant tissues, especially in grains and oil seeds – and releases a usable form of inorganic phosphorus. While phytases have been found to occur in animals, plants, fungi and bacteria, phytases have been most commonly detected and characterized from fungi. History The first plant phytase was found in 1907 from rice bran and in 1908 from an animal ( calf's liver and blood). In 1962 began the first attempt at commercializing phytases for animal feed nutrition enhancing purposes when International Minerals & Chemicals (IMC) studied over 2000 microorganisms to find the most suitable ones for phytase production. This project was launched in part due to concerns about mineable sources for inorganic phosphorus eventually running out (see peak ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Salmonella
''Salmonella'' is a genus of bacillus (shape), rod-shaped, (bacillus) Gram-negative bacteria of the family Enterobacteriaceae. The two known species of ''Salmonella'' are ''Salmonella enterica'' and ''Salmonella bongori''. ''S. enterica'' is the type species and is further divided into six subspecies that include over 2,650 serotypes. ''Salmonella'' was named after Daniel Elmer Salmon (1850–1914), an American veterinary surgeon. ''Salmonella'' species are non-Endospore, spore-forming, predominantly motility, motile enterobacteriaceae, enterobacteria with cell diameters between about 0.7 and 1.5 micrometre, μm, lengths from 2 to 5 μm, and peritrichous flagella (all around the cell body, allowing them to move). They are chemotrophs, obtaining their energy from Redox, oxidation and reduction reactions, using organic sources. They are also facultative aerobic organism, facultative anaerobes, capable of generating adenosine triphosphate with oxygen ("aerobically") ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polymerase Chain Reaction
The polymerase chain reaction (PCR) is a method widely used to make millions to billions of copies of a specific DNA sample rapidly, allowing scientists to amplify a very small sample of DNA (or a part of it) sufficiently to enable detailed study. PCR was invented in 1983 by American biochemist Kary Mullis at Cetus Corporation. Mullis and biochemist Michael Smith (chemist), Michael Smith, who had developed other essential ways of manipulating DNA, were jointly awarded the Nobel Prize in Chemistry in 1993. PCR is fundamental to many of the procedures used in genetic testing and research, including analysis of Ancient DNA, ancient samples of DNA and identification of infectious agents. Using PCR, copies of very small amounts of DNA sequences are exponentially amplified in a series of cycles of temperature changes. PCR is now a common and often indispensable technique used in medical laboratory research for a broad variety of applications including biomedical research and forensic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pfu DNA Polymerase
''Pfu'' DNA polymerase is an enzyme found in the hyperthermophilic archaeon '' Pyrococcus furiosus'', where it functions to copy the organism's DNA during cell division (thermostable DNA polymerase). In the laboratory setting, ''Pfu'' is used to amplify DNA in the polymerase chain reaction (PCR), where the enzyme serves the central function of copying a new strand of DNA during each extension step. It is a family B DNA polymerase. It has an RNase H-like 3'-5' exonuclease domain, typical of B-family polymerase such as DNA polymerase II. Proofreading ability of ''Pfu'' polymerase ''Pfu'' DNA polymerase has superior thermostability and proofreading properties compared with ''Taq'' DNA polymerase. Unlike ''Taq'' DNA polymerase, ''Pfu'' DNA polymerase possesses 3' to 5' exonuclease proofreading activity, meaning that as the DNA is assembled from the 5' end to 3' end, the exonuclease activity immediately removes nucleotides misincorporated at the 3' end of the growing DNA strand. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Taq Polymerase
''Taq'' polymerase is a thermostable DNA polymerase I named after the thermophilic eubacterial microorganism ''Thermus aquaticus,'' from which it was originally isolated by master's student Alice Chien et al. in 1976. Its name is often abbreviated to ''Taq'' or ''Taq'' pol. It is frequently used in the polymerase chain reaction (PCR), a method for greatly amplifying the quantity of short segments of DNA. ''T. aquaticus'' is a bacterium that lives in hot springs and hydrothermal vents, and ''Taq'' polymerase was identified as an enzyme able to withstand the protein-denaturing conditions (high temperature) required during PCR. Therefore, it replaced the DNA polymerase from '' E. coli'' originally used in PCR. Enzymatic properties ''Taqs optimum temperature for activity is 75–80 °C, with a half-life of greater than 2 hours at 92.5 °C, 40 minutes at 95 °C and 9 minutes at 97.5 °C, and can replicate a 1000 base pair strand of DNA in less than 10 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thermostable DNA Polymerase
Thermostable DNA polymerases are DNA polymerases that originate from thermophiles, usually bacterial or archaeal species, and are therefore thermostable. They are used for the polymerase chain reaction and related methods for the amplification and modification of DNA. Properties Several DNA polymerases have been described with distinct properties that define their specific utilisation in a PCR, in real-time PCR or in an isothermal amplification. Being DNA polymerases, the thermostable DNA polymerases all have a 5'→3' polymerase activity, and either a 5'→3' or a 3'→5' exonuclease activity. Structure DNA polymerases are roughly shaped like a hand with a thumb, palm and fingers.T. A. Steitz''DNA polymerases: structural diversity and common mechanisms.''In: '' Journal of Biological Chemistry.'' Volume 274, issue 25, June 1999, p. 17395–17398, , .P. J. Rothwell, G. Waksman: ''Structure and mechanism of DNA polymerases.'' In: ''Advances in protein chemistry.'' Volu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
