Bacillus Litoralis
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Bacillus Litoralis
''Bacillus'' (Latin "stick") is a genus of Gram-positive, rod-shaped bacteria, a member of the phylum ''Bacillota'', with 266 named species. The term is also used to describe the shape (rod) of other so-shaped bacteria; and the plural ''Bacilli'' is the name of the class of bacteria to which this genus belongs. ''Bacillus'' species can be either obligate aerobes which are dependent on oxygen, or facultative anaerobes which can survive in the absence of oxygen. Cultured ''Bacillus'' species test positive for the enzyme catalase if oxygen has been used or is present. ''Bacillus'' can reduce themselves to oval endospores and can remain in this dormant state for years. The endospore of one species from Morocco is reported to have survived being heated to 420 °C. Endospore formation is usually triggered by a lack of nutrients: the bacterium divides within its cell wall, and one side then engulfs the other. They are not true spores (i.e., not an offspring). Endospore format ...
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Bacillus Subtilis
''Bacillus subtilis'', known also as the hay bacillus or grass bacillus, is a Gram-positive, catalase-positive bacterium, found in soil and the gastrointestinal tract of ruminants, humans and marine sponges. As a member of the genus ''Bacillus'', ''B. subtilis'' is rod-shaped, and can form a tough, protective endospore, allowing it to tolerate extreme environmental conditions. ''B. subtilis'' has historically been classified as an obligate aerobe, though evidence exists that it is a facultative anaerobe. ''B. subtilis'' is considered the best studied Gram-positive bacterium and a model organism to study bacterial chromosome replication and cell differentiation. It is one of the bacterial champions in secreted enzyme production and used on an industrial scale by biotechnology companies. Description ''Bacillus subtilis'' is a Gram-positive bacterium, rod-shaped and catalase-positive. It was originally named ''Vibrio subtilis'' by Christian Gottfried Ehrenberg, and renamed ''B ...
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Symbiosis
Symbiosis (from Greek , , "living together", from , , "together", and , bíōsis, "living") is any type of a close and long-term biological interaction between two different biological organisms, be it mutualistic, commensalistic, or parasitic. The organisms, each termed a symbiont, must be of different species. In 1879, Heinrich Anton de Bary defined it as "the living together of unlike organisms". The term was subject to a century-long debate about whether it should specifically denote mutualism, as in lichens. Biologists have now abandoned that restriction. Symbiosis can be obligatory, which means that one or more of the symbionts depend on each other for survival, or facultative (optional), when they can generally live independently. Symbiosis is also classified by physical attachment. When symbionts form a single body it is called conjunctive symbiosis, while all other arrangements are called disjunctive symbiosis."symbiosis." Dorland's Illustrated Medical Dictionary. ...
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Surfactin
Surfactin is a very powerful surfactant commonly used as an antibiotic. It is a bacterial cyclic lipopeptide, largely prominent for its exceptional surfactant power. Its amphiphilic properties help this substance to survive in both hydrophilic and hydrophobic environments. It is an antibiotic produced by the Gram-positive endospore-forming bacteria ''Bacillus subtilis''. In the course of various studies of its properties, surfactin was found to exhibit effective characteristics like antibacterial, antiviral, antifungal, anti-mycoplasma and hemolytic activities. Structure and Synthesis The structure of the main congener consists of a peptide loop of seven amino acids ( L-glutamic acid, L-leucine, D-leucine, L-valine, L-aspartic acid, D-leucine and L-leucine) and a β-hydroxy fatty acid of variable length, thirteen to fifteen carbon atoms long. The glutamic acid and aspartic acid residues at positions 1 and 5 respectively, give the ring its hydrophilic character, as well as its ne ...
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Lipopeptide
A lipopeptide is a molecule consisting of a lipid connected to a peptide. They are able to self-assemble into different structures. Many bacteria produced these molecules as a part of their metabolism, especially those of the genus ''Bacillus'', ''Pseudomonas'' and ''Streptomyces''. Certain lipopeptides are used as antibiotics. Other lipopeptides are toll-like receptor agonists. Certain lipopeptides can have strong antifungal and hemolytic activities. It has been demonstrated that their activity is generally linked to interactions with the plasma membrane, and sterol components of the plasma membrane could play a major role in this interaction. It is a general trend that adding a lipid group of a certain length (typically C10–C12) to a lipopeptide will increase its bactericidal activity. Lipopeptides with a higher amount of carbon atoms, for example 14 or 16, in its lipid tail will typically have antibacterial activity as well as anti-fungal activity. Lipopeptide detergents (LPDs ...
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Detergent
A detergent is a surfactant or a mixture of surfactants with cleansing properties when in dilute solutions. There are a large variety of detergents, a common family being the alkylbenzene sulfonates, which are soap-like compounds that are more soluble in hard water, because the polar sulfonate (of detergents) is less likely than the polar carboxylate (of soap) to bind to calcium and other ions found in hard water. Definitions The word ''detergent'' is derived from the Latin adjective ''detergens'', from the verb ''detergere'', meaning to wipe or polish off. Detergent is a surfactant or a mixture of surfactants with cleansing properties when in dilute solutions. However, conventionally, detergent is used to mean synthetic cleaning compounds as opposed to ''soap'' (a salt of the natural fatty acid), even though soap is also a detergent in the true sense. In domestic contexts, the term ''detergent'' refers to household cleaning products such as ''laundry detergent'' or '' dish ...
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Subtilisin
Subtilisin is a protease (a protein-digesting enzyme) initially obtained from ''Bacillus subtilis''. Subtilisins belong to subtilases, a group of serine proteases that – like all serine proteases – initiate the nucleophilic attack on the peptide (amide) bond through a serine residue at the active site. Subtilisins typically have molecular weights 27kDa. They can be obtained from certain types of soil bacteria, for example, ''Bacillus amyloliquefaciens'' from which they are secreted in large amounts. Nomenclature Subtilisin is also commercially known as ''Alcalase®'', ''Endocut-02L'', ''ALK-enzyme'', ''bacillopeptidase'', ''Bacillus subtilis alkaline proteinase bioprase'', ''bioprase AL'', ''colistinase'', ''genenase I'', ''Esperase®'', ''maxatase'', ''protease XXVII'', ''thermoase'', ''superase'', ''subtilisin DY'', ''subtilopeptidase'', ''SP 266'', ''Savinase®'', ''kazusase'', ''protease VIII'', ''protin A 3L'', ''Savinase®'', ''orientase 10B'', ''protease S.'' It ...
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Protease
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes (increases reaction rate or "speeds up") proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in many biological functions, including digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling. In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Hierarchy of proteases Based on catalytic residue Proteases can be classified into seven broad groups: * Serine protease ...
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Alpha Amylase
α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolysis, hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose: :Endohydrolysis of (1→4)-α-D-glucosidic linkages in polysaccharides containing three or more (1→4)-α-linked D-glucose units It is the major form of amylase found in humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. It is a member of glycoside hydrolase family 13. In human biology Although found in many tissues, amylase is most prominent in pancreas, pancreatic juice and saliva, each of which has its own isoform of human α-amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibody, monoclonal antibodies. In humans, all amylase isoforms link to chromosome 1p21 (see AMY1A). Salivary a ...
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