A biological catalyst is known as a?
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generally an enzyme is the catalyst, and it speeds up the rate of the reaction by lowering the activation needed to start the reaction. A single catalyst is known as the catalase
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Biotechnology, as the name implies is technology based on biology (where biology is the science of studying life). Examples include the production of alcohol by fermentation, The production of penicillin from cell cultures, the production of lysine (a protein), and many more where useful chemicals produced by biological entities are extracted as useful products. Other examples include the manufacture of cheese, yougert, wine - all involving living organisms. If you want to know more have a look at wikipedia - there is a lot of information there....
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Biochemical involves extracting quantities of something. Since extraction processes are not always that great (resulting in very little product for lots of input) you have to start out with greater quantities of unextracted material.
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Luciferase.\n\nLuciferases are enzymes that emit light. A diverse group of organisms use luciferase-mediated bioluminescence to startle predators or to attract prey or mates. The luciferase from the North American firefly releases green light during the oxidation of its chemical substrate, luciferin. Other organisms, including plants, that express the luciferase (LUC) gene will also glow faintly green when supplied with luciferin.
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active only in the presence of a catalyst
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A chemical substance that increases the rate of a reaction without being consumed; after the reaction it can potentially be recovered from the reaction mixture chemically unchanged. The catalyst lowers the activation energy required, allowing the reaction to proceed more quickly or at a lower temperature. In a fuel cell, the catalyst facilitates the reaction of oxygen and hydrogen.
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Biochemistry is the study of the chemistry of life, a bridge between biology and chemistry that studies how complex chemical reactions give rise to life. It is a hybrid branch of chemistry which specialises in the chemical processes in living organisms. This article only discusses terrestrial biochemistry (carbon- and water-based), as all the life forms we know are on Earth. Since life forms alive today are believed to have descended from the same common ancestor, they naturally have similar biochemistries, even for matters which would appear to be essentially arbitrary, such as the genetic code or handedness of various biomolecules. It is unknown whether alternate biochemistries are possible or practical.\n\nBiochemistry is the study of the structure and function of cellular components, such as proteins, carbohydrates, lipids, nucleic acids, and other biomolecules. Chemical biology aims to answer many questions arising from biochemistry by using tools developed within synthetic chemistry.\n\nAlthough there is a vast number of different biomolecules, they tend to be composed of the same repeating subunits (called monomers), in different orders. Each class of biomolecules has a different set of subunits. Recently, biochemistry has focused more specifically on the chemistry of enzyme-catalyzed reactions, and on the properties of proteins.\n\nThe biochemistry of cell metabolism and the endocrine system has been extensively described. Other areas of biochemistry include the genetic code (DNA, RNA), protein synthesis, cell membrane transport, and signal transduction.
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biological technician
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Bioluminescent organisms.
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This article has a mechanism (APPLIED AND ENVIRONMENTAL MICROBIOLOGY, Dec. 1995, p. 4374–4377), but you may not can see the link provided (try the second).
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Proteins' main fuctions are to serve as biological catalysts in living things. That means that they allow biological processes to occur faster and more efficeintly. Also proteins are used to regulate biological functions. They serve other functions also such as chemical messengers, building blocks, and transporters. Because DNA, the code of life, encode ultimately for proteins, the proteins are central to almost every biological process from respiration to reproduction. The easier question to ask is what proteins don't do.
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If the Catalyst is inorganic the higher the temp the quicker it works, if the catalyst is organic(enzyme),it will reach a peak of activity,then further temp will destroy the catalyst
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An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. The word comes from the Greek ένζυμο, énsymo, which comes from én ("at" or "in") and simo ("leaven" or "yeast"). Certain RNAs also have catalytic activity, but to differentiate them from protein enzymes, they are referred to as RNA enzymes or ribozymes.\n\nEnzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products without enzymes. A malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a severe disease. For example, the most common type of phenylketonuria is caused by a single amino acid mutation in the enzyme phenylalanine hydroxylase, which catalyzes the first step in the degradation of phenylalanine. The resulting build-up of phenylalanine and related products can lead to mental retardation if the disease is untreated.\n\nLike all catalysts, enzymes work by providing an alternate pathway of lower activation energy of a reaction, thus allowing the reaction to proceed much faster. Enzymes may speed up reactions by a factor of many millions. An enzyme, like any catalyst, remains unaltered by the completed reaction and can therefore continue to function. Because enzymes do not affect the relative energy between the products and reagents, they do not affect equilibrium of a reaction. However, the advantage of enzymes compared to most other catalysts is their sterio-, regio- and chemoselectivity and specificity.\n\nEnzyme activity can be affected by other molecules. Inhibitors are naturally occurring or synthetic molecules that decrease or abolish enzyme activity; activators are molecules that increase activity. Some irreversible inhibitors bind enzymes very tightly, effectively inactivating them. Many drugs and poisons act by inhibiting enzymes. Aspirin inhibits the COX-1 and COX-2 enzymes that produce the inflammation messenger prostaglandin, thus suppressing pain and inflammation. The poison cyanide inhibits cytochrome c oxidase, which effectively blocks cellular respiration.\n\nWhile all enzymes have a biological role, some enzymes are used commercially for other purposes. Many household cleaners use enzymes to speed up chemical reactions ( e.g., breaking down protein or starch stains in clothes).\n\nMore than 5,000 enzymes are known. Typically the suffix -ase is added to the name of the substrate (e.g., lactase is the enzyme that catalyzes the cleavage of lactose) or the type of reaction (e.g., DNA polymerase catalyzes the formation of DNA polymers). However, this is not always the case, especially when enzymes modify multiple substrates. For this reason Enzyme Commission or EC numbers are used to classify enzymes based on the reactions they catalyze. Even this is not a perfect solution, as enzymes from different species or even very similar enzymes in the same species may have identical EC numbers.\nIn enzymes, as with other proteins, function is determined by structure. An enzyme can be:\n\n    * A monomeric protein, i.e., containing only one polypeptide chain, typically one hundred or more amino acids; or\n    * an oligomeric protein consisting of several polypeptide chains, different or identical, that act together as a unit.\n\nAs with any protein, each monomer is actually produced as a long, linear chain of amino acids, which folds in a particular fashion to produce a three-dimensional product. Individual monomers may then combine via non-covalent interactions to form a multimeric protein. Many enzymes can be unfolded or inactivated by heating, which destroys the three-dimensional structure of the protein.\n\nhttp://en.wikipedia.org/wiki/Enzyme#3D_Structure
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To trigger a biological response.
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it speeds up the rate of a biological reaction without itself being used up. it acts by binding with the substrate involved in the reaction and converting it into another substance. it is relatively specific on the reaction it catalyses. this is produced within living cells and may act either within the cell or outside it
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I'll assume you mean a trophic cascade in terms of cell biology.  A ligand-mediated event, such as any binding of a hormone, cytokine, or trophic factor, causes a "cascade' of intracellular reactions that serves to amplify the signal.  So, if only one molecule of, say, TNF binds to it's receptor, that may activate an enzyme that alters 100 other proteins.  Each of those 100 other proteins may in turn be enzymes (and often are), and each may then alter 100 proteins-thus from a single binding event at the cell surface, we very rapidly (within seconds) have 10's or 100's of thousands of proteins effected, which in turn effects the function of those proteins.  This is a typical cascade of any ligand-receptor interaction. Now trophic means that it aids in growth or survival of the cell, so a trophic cascade would be one in which a trophic factor, such as nerve growth factor, binds to the receptor on the cell and induces changes in that cell which aid it in surviving and functioning.
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A + B -> C + D  . In between the arrow (in upper side f the arrow), put the catalyst name, fr example nicel