Molecular Sequence Data
Amino Acid Sequence
Gene Expression Regulation, Fungal
Gram-Negative Anaerobic Straight, Curved, and Helical Rods
A cold-active glucanase from the ruminal bacterium Fibrobacter succinogenes S85. (1/1106)We previously characterized two endoglucanases, CelG and EGD, from the mesophilic ruminal anaerobe Fibrobacter succinogenes S85. Further comparative experiments have shown that CelG is a cold-active enzyme whose catalytic properties are superior to those of several other intensively studied cold-active enzymes. It has a lower temperature optimum, of 25 degrees C, and retains about 70% of its maximum activity at 0 degrees C, while EGD has a temperature optimum of 35 degrees C and retains only about 18% of its maximal activity at 0 degrees C. When assayed at 4 degrees C, CelG exhibits a 33-fold-higher kcat value and a 73-fold-higher physiological efficiency (kcat/Km) than EGD. CelG has a low thermal stability, as indicated by the effect of temperature on its activity and secondary structure. The presence of small amino acids around the putative catalytic residues may add to the flexibility of the enzyme, thereby increasing its activity at cold temperatures. Its activity is modulated by sodium chloride, with an increase of over 1.8-fold at an ionic strength of 0.03. Possible explanations for the presence of a cold-active enzyme in a mesophile are that cold-active enzymes are more broadly distributed than previously expected, that lateral transfer of the gene from a psychrophile occurred, or that F. succinogenes originated from the marine environment. (+info)
Sequence analysis of scaffolding protein CipC and ORFXp, a new cohesin-containing protein in Clostridium cellulolyticum: comparison of various cohesin domains and subcellular localization of ORFXp. (2/1106)The gene encoding the scaffolding protein of the cellulosome from Clostridium cellulolyticum, whose partial sequence was published earlier (S. Pages, A. Belaich, C. Tardif, C. Reverbel-Leroy, C. Gaudin, and J.-P. Belaich, J. Bacteriol. 178:2279-2286, 1996; C. Reverbel-Leroy, A. Belaich, A. Bernadac, C. Gaudin, J. P. Belaich, and C. Tardif, Microbiology 142:1013-1023, 1996), was completely sequenced. The corresponding protein, CipC, is composed of a cellulose binding domain at the N terminus followed by one hydrophilic domain (HD1), seven highly homologous cohesin domains (cohesin domains 1 to 7), a second hydrophilic domain, and a final cohesin domain (cohesin domain 8) which is only 57 to 60% identical to the seven other cohesin domains. In addition, a second gene located 8.89 kb downstream of cipC was found to encode a three-domain protein, called ORFXp, which includes a cohesin domain. By using antiserum raised against the latter, it was observed that ORFXp is associated with the membrane of C. cellulolyticum and is not detected in the cellulosome fraction. Western blot and BIAcore experiments indicate that cohesin domains 1 and 8 from CipC recognize the same dockerins and have similar affinity for CelA (Ka = 4.8 x 10(9) M-1) whereas the cohesin from ORFXp, although it is also able to bind all cellulosome components containing a dockerin, has a 19-fold lower Ka for CelA (2.6 x 10(8) M-1). Taken together, these data suggest that ORFXp may play a role in cellulosome assembly. (+info)
Molecular cloning and expression of the novel fungal beta-glucosidase genes from Humicola grisea and Trichoderma reesei. (3/1106)A novel fungal beta-glucosidase gene (bgl4) and its homologue (bgl2) were cloned from the cellulolytic fungi Humicola grisea and Trichoderma reesei, respectively. The deduced amino acid sequences of H. grisea BGL4 and T. reesei BGL2 comprise 476 and 466 amino acids, respectively, and share 73.1% identity. These beta-glucosidases show significant homology to plant beta-glucosidases belonging to the beta-glucosidase A (BGA) family. Both genes were expressed in Aspergillus oryzae, and the recombinant beta-glucosidases were purified. Recombinant H. grisea BGL4 is a thermostable enzyme compared with recombinant T. reesei BGL2. In addition to beta-glucosidase activity, recombinant H. grisea BGL4 showed a significant level of beta-galactosidase activity, while recombinant T. reesei BGL2 showed weak beta-galactosidase activity. Cellulose saccharification by Trichoderma cellulases was improved by the addition of recombinant H. grisea BGL4. (+info)
Cellulolytic enzymes in culture filtrates of Rhizoctonia lamellifera. (4/1106)During growth in a liquid culture containing a single soluble or an insoluble cellulosic carbon source, Rhizoctonia lamellifera released cellulolytic enzymes into the medium. These enzymes were separated by gel filtration and ion-exchange chromatography into seven components, three of high and four of low molecular weight. One of the components had the character of a C1 cellulase. When the components were combined they released more reducing sugars from cellulosic substrates than when used singly. (+info)
kdgREcc negatively regulates genes for pectinases, cellulase, protease, HarpinEcc, and a global RNA regulator in Erwinia carotovora subsp. carotovora. (5/1106)Erwinia carotovora subsp. carotovora produces extracellular pectate lyase (Pel), polygalacturonase (Peh), cellulase (Cel), and protease (Prt). The concerted actions of these enzymes largely determine the virulence of this plant-pathogenic bacterium. E. carotovora subsp. carotovora also produces HarpinEcc, the elicitor of the hypersensitive reaction. We document here that KdgREcc (Kdg, 2-keto-3-deoxygluconate; KdgR, general repressor of genes involved in pectin and galacturonate catabolism), a homolog of the E. chrysanthemi repressor, KdgREch and the Escherichia coli repressor, KdgREco, negatively controls not only the pectinases, Pel and Peh, but also Cel, Prt, and HarpinEcc production in E. carotovora subsp. carotovora. The levels of pel-1, peh-1, celV, and hrpNEcc transcripts are markedly affected by KdgREcc. The KdgREcc- mutant is more virulent than the KdgREcc+ parent. Thus, our data for the first time establish a global regulatory role for KdgREcc in E. carotovora subsp. carotovora. Another novel observation is the negative effect of KdgREcc on the transcription of rsmB (previously aepH), which specifies an RNA regulator controlling exoenzyme and HarpinEcc production. The levels of rsmB RNA are higher in the KdgREcc- mutant than in the KdgREcc+ parent. Moreover, by DNase I protection assays we determined that purified KdgREcc protected three 25-bp regions within the transcriptional unit of rsmB. Alignment of the protected sequences revealed the 21-mer consensus sequence of the KdgREcc-binding site as 5'-G/AA/TA/TGAAA[N6]TTTCAG/TG/TA-3'. Two such KdgREcc-binding sites occur in rsmB DNA in a close proximity to each other within nucleotides +79 and +139 and the third KdgREcc-binding site within nucleotides +207 and +231. Analysis of lacZ transcriptional fusions shows that the KdgR-binding sites negatively affect the expression of rsmB. KdgREcc also binds the operator DNAs of pel-1 and peh-1 genes and represses expression of a pel1-lacZ and a peh1-lacZ transcriptional fusions. We conclude that KdgREcc affects extracellular enzyme production by two ways: (i) directly, by inhibiting the transcription of exoenzyme genes; and (ii) indirectly, by preventing the production of a global RNA regulator. Our findings support the idea that KdgREcc affects transcription by promoter occlusion, i.e., preventing the initiation of transcription, and by a roadblock mechanism, i.e., by affecting the elongation of transcription. (+info)
Characterization of two divergent endo-beta-1,4-glucanase cDNA clones highly expressed in the nonclimacteric strawberry fruit. (6/1106)Two cDNAs clones (Cel1 and Cel2) encoding divergent endo-beta-1, 4-glucanases (EGases) have been isolated from a cDNA library obtained from ripe strawberry (Fragaria x ananassa Duch) fruit. The analysis of the amino acid sequence suggests that Cel1 and Cel2 EGases have different secondary and tertiary structures and that they differ in the presence of potential N-glycosylation sites. By in vitro translation we show that Cel1 and Cel2 bear a functional signal peptide, the cleavage of which yields mature proteins of 52 and 60 kD, respectively. Phylogenetic analysis revealed that the Cel2 EGase diverged early in evolution from other plant EGases. Northern analysis showed that both EGases are highly expressed in fruit and that they have different temporal patterns of accumulation. The Cel2 EGase was expressed in green fruit, accumulating as the fruit turned from green to white and remaining at an elevated, constant level throughout fruit ripening. In contrast, the Cel1 transcript was not detected in green fruit and only a low level of expression was observed in white fruit. The level of Cel1 mRNA increased gradually during ripening, reaching a maximum in fully ripe fruit. The high levels of Cel1 and Cel2 mRNA in ripe fruit and their overlapping patterns of expression suggest that these EGases play an important role in softening during ripening. In addition, the early expression of Cel2 in green fruit, well before significant softening begins, suggests that the product of this gene may also be involved in processes other than fruit softening, e.g. cell wall expansion. (+info)
Design of a pH-dependent cellulose-binding domain. (7/1106)Protein-carbohydrate interactions typically rely on aromatic stacking interactions of tyrosine, phenylalanine and tryptophan side chains with the sugar rings whereas histidine residues are rarely involved. The small cellulose-binding domain of the Cel7A cellobiohydrolase (formerly CBHI) from Trichoderma reesei binds to crystalline cellulose primarily using a planar strip of three tyrosine side chains. Binding of the wild-type Cel7A CBD is practically insensitive to pH. Here we have investigated how histidine residues mediate the binding interaction and whether the protonation of a histidine side chain makes the binding sensitive to pH. Protein engineering of the Cel7A CBD was thus used to replace the tyrosine residues in two different positions with histidine residues. All of the mutants exhibited a clear pH-dependency of the binding, in clear contrast to the wild-type. Although the binding of the mutants at optimal pH was less than for the wild-type, in one case, Y31H, this binding almost reached the wild-type level. (+info)
Characterization and cloning of celR, a transcriptional regulator of cellulase genes from Thermomonospora fusca. (8/1106)CelR, a protein that regulates transcription of cellulase genes in Thermomonospora fusca (Actinomycetaceae) was purified to homogeneity. A 6-kilobase NotI-SacI fragment of T. fusca DNA containing the celR gene was cloned into Esherichia coli and sequenced. The celR gene encodes a 340-residue polypeptide that is highly homologous to members of the GalR-LacI family of bacterial transcriptional regulators. CelR specifically binds to a 14-base pair inverted repeat, which has sequence similarity to the binding sites of other family members. This site is present in regions upstream of all six cellulase genes in T. fusca. The binding of CelR to the celE promoter is inhibited specifically by low concentrations of cellobiose (0.2-0.5 mM), the major end product of cellulases. The other sugars tested did not affect binding at equivalent or 50-fold higher concentrations. The results suggest that CelR may act as a repressor, and that the mechanism of induction involves a direct interaction of CelR with cellobiose. (+info)
Cellulase is a group of enzymes that break down cellulose, a complex carbohydrate found in plant cell walls. In the medical field, cellulase is used to treat certain digestive disorders, such as constipation and irritable bowel syndrome (IBS), by breaking down the cellulose in plant-based foods and making them easier to digest. Cellulase supplements are available over-the-counter and may be recommended by a healthcare provider for individuals who have difficulty digesting certain types of fiber. However, it is important to note that cellulase supplements should not be used as a substitute for a healthy diet or medical treatment for digestive disorders.
Cellulases are a group of enzymes that break down cellulose, a complex carbohydrate found in plant cell walls. In the medical field, cellulases are used to treat certain digestive disorders, such as constipation and inflammatory bowel disease, by breaking down cellulose into simpler sugars that can be more easily absorbed by the body. They are also used in the production of biofuels and in the textile industry for removing stains and improving the texture of fabrics.
Cellulose is a complex carbohydrate that is the primary structural component of plant cell walls. It is a long, fibrous polysaccharide made up of glucose molecules linked together by beta-1,4-glycosidic bonds. In the medical field, cellulose is used in a variety of ways. For example, it is often used as a thickening agent in medications, such as tablets and capsules, to help them maintain their shape and prevent them from dissolving too quickly in the stomach. It is also used as a binding agent in some medications to help them stick together and form a solid mass. In addition, cellulose is used in wound dressings and other medical products to help absorb excess fluid and promote healing. It is also used in some dietary supplements to help slow down the absorption of other ingredients, such as vitamins and minerals. Overall, cellulose is an important component of many medical products and plays a crucial role in their function and effectiveness.
Cellulose 1,4-beta-Cellobiosidase is an enzyme that hydrolyzes the beta-1,4-glycosidic bond in cellulose, a complex carbohydrate found in plant cell walls. This enzyme is important in the degradation of cellulose by microorganisms, such as fungi and bacteria, which play a crucial role in the decomposition of plant material and the recycling of nutrients in the environment. In the medical field, cellulose 1,4-beta-Cellobiosidase has been studied for its potential use in the treatment of certain diseases, such as diabetes and obesity, by promoting the breakdown of dietary fiber and improving glucose metabolism.
Cellobiose is a disaccharide sugar composed of two glucose molecules linked together by a beta-1,4-glycosidic bond. It is commonly found in plant cell walls and is a major component of cellulose, a complex carbohydrate that provides structural support to plant cells. In the medical field, cellobiose is not typically used as a therapeutic agent, but it can be used as a dietary supplement for individuals with certain medical conditions, such as diabetes, who require additional sources of carbohydrates. It is also used as a substrate in the production of certain enzymes and antibiotics. Cellobiose is not absorbed by the human body and is instead fermented by gut bacteria, producing short-chain fatty acids and gases. In some cases, excessive consumption of cellobiose can lead to digestive symptoms such as bloating, gas, and diarrhea.
Carboxymethylcellulose sodium (CMC sodium) is a water-soluble polymer that is commonly used in the medical field as a thickening agent, emulsifier, and stabilizer. It is derived from cellulose, which is a natural polymer found in plant cell walls. CMC sodium is often used in pharmaceuticals to improve the texture and consistency of various products, such as tablets, capsules, and ointments. It can also be used as a binder to help hold ingredients together in a cohesive mixture. In addition to its use in pharmaceuticals, CMC sodium is also used in medical devices, such as wound dressings and catheters, to improve their handling and performance. It is also used in food and beverage products as a thickener and stabilizer. CMC sodium is generally considered safe for use in humans and is listed as a food additive by the Food and Drug Administration (FDA). However, it may cause allergic reactions in some people, and its use in certain medical products may be contraindicated in individuals with certain medical conditions.
Glycoside hydrolases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds in carbohydrates. These enzymes are involved in a wide range of biological processes, including digestion, metabolism, and signaling. In the medical field, glycoside hydrolases are often used as diagnostic tools to study carbohydrate metabolism and to develop new treatments for diseases related to carbohydrate metabolism, such as diabetes and obesity. They are also used in the production of biofuels and other industrial products.
Beta-glucosidase is an enzyme that catalyzes the hydrolysis of beta-1,4-glycosidic bonds in carbohydrates, specifically those that contain glucose. It is found in a variety of organisms, including bacteria, fungi, and plants, and plays an important role in the metabolism of carbohydrates. In the medical field, beta-glucosidase is used in the treatment of certain digestive disorders, such as lactose intolerance and galactosemia. It is also used in the production of certain foods and beverages, such as beer and certain types of cheese, where it helps to break down complex carbohydrates into simpler sugars that can be more easily digested and absorbed by the body. In addition, beta-glucosidase has been studied for its potential use in the treatment of certain types of cancer, as it has been shown to have anti-tumor effects in some laboratory studies. However, more research is needed to fully understand its potential therapeutic applications in this area.
Dextrins are a type of polysaccharide that are formed by partial hydrolysis of starch. They are composed of glucose molecules linked together by alpha-1,4-glycosidic bonds, with some alpha-1,6-glycosidic bonds present as well. Dextrins are often used as thickening agents in food and pharmaceutical products, and they have also been studied for their potential health benefits, including their ability to lower blood sugar levels and improve cholesterol levels. In the medical field, dextrins are sometimes used as a source of glucose for patients who are unable to produce enough glucose on their own, such as those with diabetes or liver disease. They may also be used as a thickening agent in medications or as a filler in certain medical devices.
Endo-1,4-beta xylanases are a class of enzymes that break down xylan, a complex carbohydrate found in the cell walls of plants and some microorganisms. In the medical field, endo-1,4-beta xylanases have been studied for their potential therapeutic applications, particularly in the treatment of digestive disorders. One potential use of endo-1,4-beta xylanases is in the management of irritable bowel syndrome (IBS), a chronic digestive disorder characterized by abdominal pain, bloating, and changes in bowel habits. Some studies have suggested that xylanase supplementation may help to improve symptoms of IBS by breaking down xylan in the gut, which can help to reduce the viscosity of the gut contents and improve gut motility. Endo-1,4-beta xylanases have also been studied for their potential use in the treatment of other digestive disorders, such as inflammatory bowel disease (IBD) and celiac disease. In these conditions, the gut lining is damaged, which can lead to increased permeability and the passage of undigested food particles into the bloodstream. Some research has suggested that xylanase supplementation may help to reduce the permeability of the gut lining and improve symptoms of these conditions. Overall, while more research is needed to fully understand the potential therapeutic applications of endo-1,4-beta xylanases in the medical field, they have shown promise as a potential treatment for a range of digestive disorders.
Glucan 1,4-beta-glucosidase is an enzyme that hydrolyzes beta-1,4-glycosidic bonds in glucans, which are polysaccharides composed of glucose molecules linked by beta-1,4-glycosidic bonds. This enzyme is found in various organisms, including fungi, bacteria, and plants, and plays a crucial role in the degradation and metabolism of glucans. In the medical field, glucan 1,4-beta-glucosidase has been studied for its potential therapeutic applications. For example, it has been shown to have anti-inflammatory and immunomodulatory effects, making it a potential candidate for the treatment of inflammatory diseases such as rheumatoid arthritis and inflammatory bowel disease. Additionally, it has been studied for its potential use in the treatment of cancer, as it has been shown to inhibit the growth of certain cancer cells and enhance the efficacy of chemotherapy.
Glucosidases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds in carbohydrates. In the medical field, glucosidases are important in the metabolism of carbohydrates, particularly in the breakdown of complex carbohydrates into simpler sugars that can be absorbed and used by the body. There are several types of glucosidases, including alpha-glucosidases, beta-glucosidases, and glucoamylases. Alpha-glucosidases are found in the small intestine and are responsible for breaking down complex carbohydrates, such as starches, into simpler sugars like glucose. Beta-glucosidases are found in the liver and are involved in the metabolism of certain drugs and toxins. Glucoamylases are found in the saliva and are responsible for breaking down starches into maltose, which can then be further broken down by enzymes in the small intestine. In the medical field, glucosidases are used in the treatment of certain conditions, such as diabetes, where the body is unable to produce enough insulin to properly regulate blood sugar levels. Alpha-glucosidase inhibitors are a type of medication that work by slowing down the breakdown of carbohydrates in the small intestine, which can help to lower blood sugar levels in people with type 2 diabetes. Beta-glucosidases are also used in the treatment of certain liver diseases, such as Wilson's disease, where the liver is unable to properly metabolize certain toxins.
Xylans are a type of polysaccharide (complex carbohydrate) that are commonly found in plants, particularly in the cell walls of plants. In the medical field, xylans are often used as dietary supplements or as ingredients in various medical products. Xylans are known for their prebiotic properties, meaning they can promote the growth of beneficial bacteria in the gut. This can help improve digestive health and reduce the risk of certain diseases, such as inflammatory bowel disease and colorectal cancer. Xylans are also used in medical products such as wound dressings, dental products, and pharmaceuticals. They can help improve the texture and stability of these products, as well as enhance their absorption and bioavailability. Overall, xylans have a number of potential health benefits and are an important component of many medical and dietary products.
Lignin is a complex organic polymer that is found in the cell walls of plants. It is a major component of wood and other plant fibers, and it plays an important role in the structure and strength of these materials. In the medical field, lignin has been studied for its potential use in a variety of applications, including as a source of bioactive compounds, as a dietary fiber, and as a material for the development of new medical devices and implants. However, lignin is not typically used in medical treatments or therapies.
Glucan 1,3-beta-glucosidase is an enzyme that hydrolyzes beta-1,3-glycosidic linkages in beta-glucans, a type of polysaccharide found in various plant and fungal cell walls. This enzyme is also known as beta-glucanase or 1,3-beta-D-glucan glucohydrolase. In the medical field, glucan 1,3-beta-glucosidase has been studied for its potential therapeutic applications. For example, it has been shown to have anti-inflammatory and immunomodulatory effects, making it a potential treatment for various inflammatory diseases such as rheumatoid arthritis and inflammatory bowel disease. Additionally, it has been studied for its potential use in cancer therapy, as it has been shown to enhance the immune response against cancer cells. In the food industry, glucan 1,3-beta-glucosidase is used as a food additive to improve the texture and nutritional value of various food products, such as bakery products, breakfast cereals, and dairy products. It is also used in the production of biofuels and in the bioremediation of contaminated soils.
In the medical field, glucans refer to a group of polysaccharides that are composed of glucose molecules linked together by glycosidic bonds. Glucans are found in various organisms, including plants, fungi, and bacteria, and they play important roles in their biology and physiology. In humans, glucans have been studied for their potential health benefits, particularly in the context of immune function. Some types of glucans, such as beta-glucans, have been shown to stimulate the immune system and enhance the body's ability to fight off infections and diseases. Glucans have also been used in the development of dietary supplements and functional foods, as well as in the treatment of certain medical conditions, such as cancer and HIV/AIDS. Overall, glucans are an important class of biomolecules that have a wide range of biological and medical applications.
Biofuels are not typically used in the medical field. Biofuels are typically derived from organic matter, such as crops or waste, and are used as a source of energy, often as a substitute for fossil fuels. They are commonly used as a fuel for vehicles, power plants, and other industrial applications. In the medical field, energy sources are typically used to power medical equipment and facilities, but they are not typically referred to as biofuels.
Fungal proteins are proteins that are produced by fungi. They can be found in various forms, including extracellular proteins, secreted proteins, and intracellular proteins. Fungal proteins have a wide range of functions, including roles in metabolism, cell wall synthesis, and virulence. In the medical field, fungal proteins are of interest because some of them have potential therapeutic applications, such as in the treatment of fungal infections or as vaccines against fungal diseases. Additionally, some fungal proteins have been shown to have anti-cancer properties, making them potential targets for the development of new cancer treatments.
Beta-mannosidase is an enzyme that is involved in the breakdown of complex carbohydrates, specifically those that contain the sugar mannose. It is a lysosomal enzyme, meaning that it is found in the lysosomes of cells, which are organelles responsible for breaking down and recycling cellular waste. In the medical field, beta-mannosidase deficiency is a rare genetic disorder that affects the breakdown of certain complex carbohydrates. This can lead to the accumulation of these carbohydrates in the body, which can cause a variety of symptoms, including intellectual disability, developmental delays, and skeletal abnormalities. There are several forms of beta-mannosidosis, which are distinguished by the specific type of carbohydrate that is affected and the severity of the symptoms. Treatment for beta-mannosidosis typically involves enzyme replacement therapy, which involves administering the missing enzyme to help break down the accumulated carbohydrates and alleviate symptoms.
Polygalacturonase is an enzyme that breaks down the bonds between galacturonic acid residues in the cell wall of plants. It is commonly found in fruits, vegetables, and other plant tissues, and plays a role in the ripening and softening of these foods. In the medical field, polygalacturonase has been studied for its potential use in treating certain medical conditions. For example, it has been shown to have anti-inflammatory properties and may be useful in treating conditions such as arthritis and inflammatory bowel disease. It has also been studied for its potential use in treating cancer, as it may be able to help break down the protective cell walls of cancer cells, making them more susceptible to treatment. However, more research is needed to fully understand the potential therapeutic applications of polygalacturonase in medicine.
Lactose is a disaccharide sugar found in milk and other dairy products. It is composed of two molecules of glucose and one molecule of galactose, which are linked together by a glycosidic bond. In the medical field, lactose intolerance is a common condition in which the body is unable to digest lactose properly. This can lead to symptoms such as bloating, gas, diarrhea, and abdominal pain. Lactose intolerance is often caused by a deficiency in the enzyme lactase, which is responsible for breaking down lactose in the small intestine. In some cases, lactose intolerance may be treated with lactase supplements or by avoiding foods that contain lactose. However, for individuals with severe lactose intolerance, it may be necessary to follow a lactose-free diet.
Bacterial proteins are proteins that are synthesized by bacteria. They are essential for the survival and function of bacteria, and play a variety of roles in bacterial metabolism, growth, and pathogenicity. Bacterial proteins can be classified into several categories based on their function, including structural proteins, metabolic enzymes, regulatory proteins, and toxins. Structural proteins provide support and shape to the bacterial cell, while metabolic enzymes are involved in the breakdown of nutrients and the synthesis of new molecules. Regulatory proteins control the expression of other genes, and toxins can cause damage to host cells and tissues. Bacterial proteins are of interest in the medical field because they can be used as targets for the development of antibiotics and other antimicrobial agents. They can also be used as diagnostic markers for bacterial infections, and as vaccines to prevent bacterial diseases. Additionally, some bacterial proteins have been shown to have therapeutic potential, such as enzymes that can break down harmful substances in the body or proteins that can stimulate the immune system.
Fungal extracellular enzyme activity
Glycoside hydrolase family 10
Glycoside hydrolase family 8
Glycoside hydrolase family 5
Harry J. Gilbert
Devendra Prasad Gupta
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- Cellulase is a hydrolytic enzyme produced by fermentation of a selected strain of Trichoderma reesei. (vitaactives.com)
- Cellulase (from trichoderma longibrachatum) 2.5 C.U. (veganessentials.com)
- 23. Domingues FC, Queiroz JA, Cabral JM, Fonseca LP. The influence of culture conditions on mycelial structure and cellulase production by Trichoderma reesei Rut C-30. (bvsalud.org)
- Look for supplements that contain protease, amylase, lipase and cellulase. (vetinfo.com)
- Biomolecular engineers at Vanderbilt University have obtained the most detailed measurements ever made of the behavior of an individual cellulase enzyme as it decomposes cellulose, the most plentiful polymer on the planet. (vanderbilt.edu)
- As a kind of multi-component compound china enzyme, cellulase contains several kinds of enzyme with synergistic effect which can catalyze the hydrolysis of cellulose and generate oligosaccharide and cellose which finally decomposed into glucose. (kitairu.net)
- The total activity of cellulase is defined as the ability of the enzyme to produce glucose, which is the final product of cellulose hydrolysis, and is expressed in cellulase units. (springeropen.com)
- In the present study deals with the isolation and screening of freshly isolated potent fungal strain as Aspergillus flavus for the production of cellulase enzyme consisting of the endoglucanase. (journalcra.com)
- Assessment of Decortication and degumming also recorded in cellulase enzyme production by Aspergillus flavus. (journalcra.com)
- Aspergillus flavus showed the production of higher activity of cellulase enzyme consisting of endoglucanase yielded higher cellulase enzyme activity. (journalcra.com)
- Cellulases are a group of enzymes, which catalyse different steps of cellulose hydrolysis, and are broadly used in industry as unpurified mixtures of several enzymes. (springeropen.com)
- However, common strategies for the determination of the cellulolytic activity of industrial cellulase preparations are based on the assessment of different steps of cellulose hydrolysis, and the results obtained with different methods are not similar. (springeropen.com)
- The aim of the present study was to develop an assay for the determination of cellulase activity that relies on the amperometric determination of the final product of cellulose hydrolysis glucose. (springeropen.com)
- The name "cellulase" is commonly used for a natural mixture of enzymes that in general includes three major glycosylases: endoglucanase (EC 18.104.22.168), exoglucanase (cellulase 1,4-beta-cellobiosidase (non-reducing end), EC 22.214.171.124), and cellobiase or β- d -glucosidase (EC 126.96.36.199) (Anoop Kumar et al. (springeropen.com)
- Cellulase breaks the 1, 4-beta-D-glycosidic linkages and converts native cellulose as well as derived celluloses to glucose which is easily digested, and this assists in digesting cellulosic products. (vitaactives.com)
- 2020 ). Another application of cellulases is the valorisation of food waste and by-products via the conversion of cellulose fibres into soluble sugars to be converted by fermentation to bio-energy, mainly bio-ethanol (Zou et al. (springeropen.com)
- Cellulose is readily biodegraded by organisms that utilize cellulase enzymes, but due to the additional acetyl groups cellulose acetate requires the presence of esterases for the first step in biodegradation. (springer.com)
Days of incubation1
- Maximum cellulase production was recorded with 9 days of incubation time, optimum pH 7.0 and 350 C temperature. (journalcra.com)
- The culture medium that provided the best mycelial growth of the strains was used for semi-quantitative tests of ligninase and cellulase activity. (microbiologyjournal.org)
- The performance of the strains with respect to the production of cellulase and ligninase was different. (microbiologyjournal.org)
- One unit (U) of cellulase activity is defined as the amount of feed enzymewhich liberates 1 μmol reducing sugar per minute from 4mg/mL substrate (carboxymethylcellulose) sodium at 37℃ and pH 5.5. (kitairu.net)
- The standard technique for the assessment of total cellulase activity, which was first proposed by Mandels and acknowledged by the International Union of Pure and Applied Chemistry (IUPAC), is the filter paper activity (FPA) method, measuring the decomposition degree of filter paper (Mandels et al. (springeropen.com)
- Ligninase and Cellulase Activity of Lentinula edodes (Berk. (microbiologyjournal.org)
- M.A. Carvalho, L.M.A.S. Costa, D.M. da Silveira E. Santos, D.R. Dias, D.C. Zied and E.S. Dias, Ligninase and Cellulase Activity of Lentinula edodes (Berk. (microbiologyjournal.org)
- After cellulase activity was stopped by washing with physiologic water and 5 minutes of centrifugation at 3,000 g, the pellet was incorporated into 4',6-diamidino-2-phenylindole-FISH staining. (cdc.gov)
- Species of this genus, Thermomonospora fusca and Thermomonospora curvata, are known for their roles in the industrial production of enzymes including CELLULASE. (bvsalud.org)
- Dos especies de este género, Thermomonospora fusca y Thermomonospora curvata, son conocidas por su papel en la producción industrial de enzimas, entre otras CELULASA. (bvsalud.org)
- As a cellulase supplierand cellulase manufacturer, we can offer kinds of related products for sale, if you have needs, please contact us. (kitairu.net)
- Each small capsule contains enzymes like amylase, lipase, cellulase and protease to break down macronutrients (carbohydrates, fats and protein, plus fiber) along with those hard-to-digest foods. (enzymedica.com)
- High activities of filter-paper cellulase and xylanase were also obtained in plastic bags and some results are reported. (scielo.br)
- 16. Comprehensive studies on optimization of cellulase and xylanase production by a local indigenous fungus strain via solid state fermentation using oil palm frond as substrate. (nih.gov)
- A synergistic of pectinase, cellulase, and glucoamylase on anthocyanin content and extraction yield of roselle petals (Hibiscus sabdariffa L. (unida.ac.id)
- Mardiah, M and Novidahlia, Noli and Khoerunnisa, Ma'rifat and Hanafi, H and Aminullah, A A synergistic of pectinase, cellulase, and glucoamylase on anthocyanin content and extraction yield of roselle petals (Hibiscus sabdariffa L.). Jurnal Teknologi dan Industri Hasil Pertanian. (unida.ac.id)
- The objective of this research was to study the effect of three enzymes: pectinase, cellulase, and glucoamylase, on the quality of the extract of the Roselle petals. (unida.ac.id)
- The research revealed that different preparation methods (water, ethanol, cellulase, pectinase, and a combination of cellulase and pectinase) resulted in biosorbents with varying bioactive ingredients and antioxidant activity. (ncl.edu.tw)
- In terms of degradation, cellulose may be considered nonbiodegradable in vivo or, at best, slowly degradable, due to the lack of cellulase enzymes in animals. (medscape.com)
- Analysis of cellulase production with sugarcane bagasse and Eicchornia crassipes biomass showed that high pressure steaming followed by alkali treatment of the sugarcane bagasse and Eicchornia crassipes biomass led to significant increase in the cellulase production as compared to the untreated substrates. (iitr.ac.in)
- The mutant UNSC-442 resulted into CMCase (7.18 IU ml'1), FPase (6.0 IU ml'1) and p-glucosidase (2.55 IU ml'1) activities with treated sugarcane bagasse as the substrate and the activities respectively were 89%, 130% and 54.5% higher as compared to the cellulase production with wild type Aspergillus niger RK-3 strain under similar conditions. (iitr.ac.in)
- 5. Temperature dependent cellulase adsorption on lignin from sugarcane bagasse. (nih.gov)
- A similar level increase in cellulases was also observed with Eicchornia crassipes biomass. (iitr.ac.in)
- To further ascertain its bioconversion capability, the levels of cellulases produced were evaluated using the commercially available synthetic cellulosic substrates under submerged state fermentation. (iitr.ac.in)
- In an attempt to isolate a strain with potential bioconversion ability, twenty two (fungal and bacterial) strains were isolated from decomposing substrates, among themAspergillus nigerRK-3 was found to have maximum cellulase producing ability. (iitr.ac.in)
- A high yielding and end product resistant mutant UNSC-442 was finally selected having substantially higher cellulase production abilities. (iitr.ac.in)
- The temporal profile of GH 1 gene abundance and the shift in GH 1 cellulase-producing microbial communities during vermicomposting of corn stover and cow dung. (bvsalud.org)
- This study was conducted with different earthworm densities to quantify the GH1 gene abundance and investigate the evolution of GH1 cellulase -producing microbial communities using qPCR and pyrosequencing . (bvsalud.org)
- cellulase-producing microbial communities during vermicomposting of corn stover and cow dung. (bvsalud.org)
- Conzyme®V999 is high concentrated neutral cellulase preparation, which is designed specially for denim abrasion process. (enzymes.bio)
- After cellulase activity was stopped by washing with physiologic water and 5 minutes of centrifugation at 3,000 g, the pellet was incorporated into 4',6-diamidino-2-phenylindole-FISH staining. (cdc.gov)