Oligo-1,6-Glucosidase
alpha-Glucosidases
Maltose
Glucan 1,4-alpha-Glucosidase
Dextranase
Dextrans
Gammaproteobacteria
Glucosyltransferases
Sucrose
Fructose
Oligosaccharides
Substrate Specificity
Digestibility of the hydrogenated derivative of an isomaltooligosaccharide mixture by rats. (1/68)
The digestibility of the hydrogenated derivative of an isomaltooligosaccharide mixture (IMO-H) was investigated. In an in vitro experiment, the digestibility of IMO-H was examined by models of the digestive system. IMO-H was resistant to two types of alpha-amylase and to artificial gastric juice. Enzymes in the rat small intestinal mucosa hydrolyzed tri-, tetra- and higher saccharide alcohols to disaccharide alcohol, removing successive glucose units from the non-reducing ends of the chains. The hydrolysis ratio for IMO-H was intermediate between the values for maltose and maltitol. In an in vivo study, growing rats were fed on an experimental diet containing IMO-H, maltitol, or hydrogenated palatinose in the range from 5% to 20%. The growth parameters of the rats fed on the test sugar show that the availability of IMO-H was about 1.2 to 1.25 times that of maltitol or hydrogenated palatinose. (+info)Cloning and characterization of the gene cluster for palatinose metabolism from the phytopathogenic bacterium Erwinia rhapontici. (2/68)
Erwinia rhapontici is able to convert sucrose into isomaltulose (palatinose, 6-O-alpha-D-glucopyranosyl-D-fructose) and trehalulose (1-O-alpha-D-glucopyranosyl-D-fructose) by the activity of a sucrose isomerase. These sucrose isomers cannot be metabolized by plant cells and most other organisms and therefore are possibly advantageous for the pathogen. This view is supported by the observation that in vitro yeast invertase activity can be inhibited by palatinose, thus preventing sucrose consumption. Due to the lack of genetic information, the role of sucrose isomers in pathogenicity has not been evaluated. Here we describe for the first time the cloning and characterization of the palatinose (pal) genes from Erwinia rhapontici. To this end, a 15-kb chromosomal DNA fragment containing nine complete open reading frames (ORFs) was cloned. The pal gene products of Erwinia rhapontici were shown to be homologous to proteins involved in uptake and metabolism of various sugars from other microorganisms. The palE, palF, palG, palH, palK, palQ, and palZ genes were oriented divergently with respect to the palR and palI genes, and sequence analysis suggested that the first set of genes constitutes an operon. Northern blot analysis of RNA extracted from bacteria grown under various conditions implies that the expression of the palI gene and the palEFGHKQZ genes is oppositely regulated at the transcriptional level. Genes involved in palatinose uptake and metabolism are down regulated by sucrose and activated by palatinose. Palatinose activation is inhibited by sucrose. Functional expression of palI and palQ in Escherichia coli revealed sucrose isomerase and palatinase activity, respectively. (+info)Responses of the ant Lasius niger to various compounds perceived as sweet in humans: a structure-activity relationship study. (3/68)
A behavioural study on the ant Lasius niger was performed by observing its feeding responses to 85 compounds presented in a two-choice situation (tested compound versus water control or sucrose solution). Among these compounds, only 21 were phagostimulating: six monosaccharides (D-glucose, 6-deoxy-D-glucose, L-galactose, L-fucose, D-fructose, L-sorbose), four derivatives of D-glucose (methyl alpha-D-glucoside, D-gluconolactone and 6-chloro- and 6-fluoro-deoxy-D-glucose), five disaccharides (sucrose, maltose, palatinose, turanose and isomaltose), one polyol glycoside (maltitol), three trisaccharides (melezitose, raffinose and maltotriose) and two polyols (sorbitol and L-iditol). None of the 16 non-carbohydrate non-polyol compounds tested, although perceived as sweet in humans, was found to be active in ants. The molar order of effectiveness of the major naturally occuring compounds (melezitose > sucrose = raffinose > D-glucose > D-fructose = maltose = sorbitol) is basically different from the molar order of their sweetness potency in humans (sucrose > D-fructose > melezitose > maltose > D-glucose = raffinose = sorbitol). On a molar basis melezitose is in L. niger about twice as effective as sucrose or raffinose, while D-glucose and D-fructose are three and four times less effective, respectively, than sucrose or raffinose. From a structure-activity relationship study it was inferred that the active monosaccharides and polyols should interact with the ant receptor through only one type of receptor, through the same binding pocket and the same binding residues, via a six-point interaction. The high effectiveness of melezitose in L. niger mirrors the feeding habits of these ants, which attend homopterans and are heavy feeders on their honeydew, which is very rich in this carbohydrate. (+info)The sucrose analog palatinose leads to a stimulation of sucrose degradation and starch synthesis when supplied to discs of growing potato tubers. (4/68)
In the present paper we investigated the effect of the sucrose (Suc) analog palatinose on potato (Solanum tuberosum) tuber metabolism. In freshly cut discs of growing potato tubers, addition of 5 mM palatinose altered the metabolism of exogenously supplied [U-14C]Suc. There was slight inhibition of the rate of 14C-Suc uptake, a 1.5-fold increase in the rate at which 14C-Suc was subsequently metabolized, and a shift in the allocation of the metabolized label in favor of starch synthesis. The sum result of these changes was a 2-fold increase in the absolute rate of starch synthesis. The increased rate of starch synthesis was accompanied by a 3-fold increase in inorganic pyrophosphate, a 2-fold increase in UDP, decreased UTP/UDP, ATP/ADP, and ATP/AMP ratios, and decreased adenylate energy charge, whereas glycolytic and Krebs cycle intermediates were unchanged. In addition, feeding palatinose to potato discs also stimulated the metabolism of exogenous 14C-glucose in favor of starch synthesis. In vitro studies revealed that palatinose is not metabolized by Suc synthases or invertases within potato tuber extracts. Enzyme kinetics revealed different effects of palatinose on Suc synthase and invertase activities, implicating palatinose as an allosteric effector leading to an inhibition of Suc synthase and (surprisingly) to an activation of invertase in vitro. However, measurement of tissue palatinose levels revealed that these were too low to have significant effects on Suc degrading activities in vivo. These results suggest that supplying palatinose to potato tubers represents a novel way to increase starch synthesis. (+info)Effects of alpha-D-glucosylglycerol on the in vitro digestion of disaccharides by rat intestinal enzymes. (5/68)
Alpha-D-glucosylglycerol (GG) is a mixture of 2-O-alpha-D-glucosylglycerol (GG-II), (2R)-1-O-alpha-D-glucosylglycerol (R-GG-I) and (2S)-1-O-alpha-D-glucosylglycerol (S-GG-I). GG has been found to be slightly hydrolyzed in vitro only by rat intestinal enzymes, but hardly at all by other digestive juices. GG suppressed the hydrolysis of maltose, sucrose and isomaltose by rat intestinal enzymes because the amount of glucose in the digestion of a mixture of GG and disaccharide was less than the sum of that in each individual digestion. The consumption of GG was suppressed by isomaltose, but promoted by maltose, with the hydrolysis of GG being suppressed. Sucrose appeared to suppress only the consumption of S-GG-I, suggesting that S-GG-I was hydrolyzed by the active site of sucrase in a sucrase-isomaltase complex. Transglucosylation seems to have occurred more frequently in the individual digestion of maltose and isomaltose than in that of GG and sucrose. GG seemed to promote transglucosylation in the presence of maltose, to suppress it with sucrose, and to delay it with isomaltose. (+info)Novel alpha-glucosidase from Aspergillus nidulans with strong transglycosylation activity. (6/68)
Aspergillus nidulans possessed an alpha-glucosidase with strong transglycosylation activity. The enzyme, designated alpha-glucosidase B (AgdB), was purified and characterized. AgdB was a heterodimeric protein comprising 74- and 55-kDa subunits and catalyzed hydrolysis of maltose along with formation of isomaltose and panose. Approximately 50% of maltose was converted to isomaltose, panose, and other minor transglycosylation products by AgdB, even at low maltose concentrations. The agdB gene was cloned and sequenced. The gene comprised 3,055 bp, interrupted by three short introns, and encoded a polypeptide of 955 amino acids. The deduced amino acid sequence contained the chemically determined N-terminal and internal amino acid sequences of the 74- and 55-kDa subunits. This implies that AgdB is synthesized as a single polypeptide precursor. AgdB showed low but overall sequence homology to alpha-glucosidases of glycosyl hydrolase family 31. However, AgdB was phylogenetically distinct from any other alpha-glucosidases. We propose here that AgdB is a novel alpha-glucosidase with unusually strong transglycosylation activity. (+info)Metabolizable and non-metabolizable sugars activate different signal transduction pathways in tomato. (7/68)
To gain insight into the regulatory mechanisms of sugar signaling in plants, the effect of derivatives of the transport sugar sucrose (Suc), the Suc isomers palatinose and turanose, and the Suc analog fluoro-Suc were tested. Photo-autotrophic suspension culture cells of tomato (Lycopersicon peruvianum) were used to study their effect on the regulation of marker genes of source and sink metabolism, photosynthesis, and the activation of mitogen-activated protein kinases (MAPKs). Suc and glucose (Glc) resulted in reverse regulation of source and sink metabolism. Whereas the mRNA level of extracellular invertase (Lin6) was induced, the transcript level of small subunit of ribulose bisphosphate carboxylase (RbcS) was repressed. In contrast, turanose, palatinose, and fluoro-Suc only rapidly induced Lin6 mRNA level, whereas the transcript level of RbcS was not affected. The differential effect of the metabolizable and non-metabolizable sugars on RbcS mRNA regulation was reflected by the fact that only Suc and Glc inhibited photosynthesis and chlorophyll fluorescence. The activation of different signal transduction pathways by sugars was further supported by the analysis of the activation of MAPKs. MAPK activity was found to be strongly activated by turanose, palatinose, and fluoro-Suc, but not by Suc and Glc. To analyze the role of sugars in relation to pathogen perception, an elicitor preparation of Fusarium oxysporum lycopersici was used. The strong activation of MAPKs and the fast and transient induction of Lin6 expresssion by the fungal elicitor resembles the effect of turanose, palatinose, and fluoro-Suc and indicates that non-metabolizable sugars are sensed as stress-related stimuli. (+info)Isomaltulose synthase from Klebsiella sp. strain LX3: gene cloning and characterization and engineering of thermostability. (8/68)
The gene (palI) encoding isomaltulose synthase (PalI) from a soil bacterial isolate, Klebsiella sp. strain LX3, was cloned and characterized. PalI converts sucrose into isomaltulose, trehalulose, and trace amounts of glucose and fructose. Sequence domain analysis showed that PalI contains an alpha-amylase domain and (beta/alpha)(8)-barrel structures, suggesting that it belongs to the alpha-amylase family. Sequence alignment indicated that the five amino acid residues of catalytic importance in alpha-amylases and glucosyltransferases (Asp(241), Glu(295), Asp(369), His(145), and His(368)) are conserved in PalI. Purified recombinant PalI displayed high catalytic efficiency, with a Km of 54.6 +/- 1.7 mM for sucrose, and maximum activity (approximately 328.0 +/- 2.5 U/mg) at pH 6.0 and 35 degrees C. PalI activity was strongly inhibited by Fe3+ and Hg2+ and was enhanced by Mn2+ and Mg2+. The half-life of PalI was 1.8 min at 50 degrees C. Replacement of selected amino acid residues by proline significantly increased the thermostability of PalI. Simultaneous replacement of Glu(498) and Arg(310) with proline resulted in an 11-fold increase in the half-life of PalI at 50 degrees C. (+info)Isomaltose is a type of disaccharide, which is a complex sugar consisting of two monosaccharides. It is specifically composed of two glucose molecules linked together in a way that forms a straight chain. Isomaltose can be found naturally in some foods such as honey and fermented products, and it can also be produced industrially as a sweetener.
In the medical field, isomaltose may be relevant in the context of carbohydrate metabolism disorders or in relation to certain types of diagnostic tests that measure the ability to digest and absorb specific sugars. However, it is not a commonly used term in most areas of medical practice.
Oligo-1,6-glucosidase is an enzyme that breaks down complex carbohydrates by hydrolyzing the α-1,6 glycosidic bonds in oligosaccharides, producing simpler sugars such as glucose. This enzyme plays a crucial role in the digestion of certain types of carbohydrates, particularly those found in plants.
Deficiency or absence of this enzyme can lead to a rare genetic disorder called Glycogen Storage Disease Type IV (GSD IV), also known as Andersen's disease. This condition is characterized by the accumulation of abnormal glycogen molecules in various organs, leading to progressive damage and failure.
It's important to note that oligo-1,6-glucosidase should not be confused with other similar enzymes such as α-glucosidase or lactase, which have different functions and substrate specificities.
Alpha-glucosidases are a group of enzymes that break down complex carbohydrates into simpler sugars, such as glucose, by hydrolyzing the alpha-1,4 and alpha-1,6 glycosidic bonds in oligosaccharides, disaccharides, and polysaccharides. These enzymes are located on the brush border of the small intestine and play a crucial role in carbohydrate digestion and absorption.
Inhibitors of alpha-glucosidases, such as acarbose and miglitol, are used in the treatment of type 2 diabetes to slow down the digestion and absorption of carbohydrates, which helps to reduce postprandial glucose levels and improve glycemic control.
Maltose is a disaccharide made up of two glucose molecules joined by an alpha-1,4 glycosidic bond. It is commonly found in malted barley and is created during the germination process when amylase breaks down starches into simpler sugars. Maltose is less sweet than sucrose (table sugar) and is broken down into glucose by the enzyme maltase during digestion.
Glucan 1,4-alpha-glucosidase, also known as amyloglucosidase or glucoamylase, is an enzyme that catalyzes the hydrolysis of 1,4-glycosidic bonds in starch and other oligo- and polysaccharides, breaking them down into individual glucose molecules. This enzyme specifically acts on the alpha (1->4) linkages found in amylose and amylopectin, two major components of starch. It is widely used in various industrial applications, including the production of high fructose corn syrup, alcoholic beverages, and as a digestive aid in some medical supplements.
Disaccharides are a type of carbohydrate that is made up of two monosaccharide units bonded together. Monosaccharides are simple sugars, such as glucose, fructose, or galactose. When two monosaccharides are joined together through a condensation reaction, they form a disaccharide.
The most common disaccharides include:
* Sucrose (table sugar), which is composed of one glucose molecule and one fructose molecule.
* Lactose (milk sugar), which is composed of one glucose molecule and one galactose molecule.
* Maltose (malt sugar), which is composed of two glucose molecules.
Disaccharides are broken down into their component monosaccharides during digestion by enzymes called disaccharidases, which are located in the brush border of the small intestine. These enzymes catalyze the hydrolysis of the glycosidic bond that links the two monosaccharides together, releasing them to be absorbed into the bloodstream and used for energy.
Disorders of disaccharide digestion and absorption can lead to various symptoms, such as bloating, diarrhea, and abdominal pain. For example, lactose intolerance is a common condition in which individuals lack sufficient levels of the enzyme lactase, leading to an inability to properly digest lactose and resulting in gastrointestinal symptoms.
Dextranase is an enzyme that breaks down dextran, a type of complex sugar (polysaccharide) consisting of many glucose molecules linked together in a chain. Dextran is produced by certain bacteria and can be found in some foods, as well as in the body during infections or after surgery. Dextranase is used medically to help prevent or treat complications associated with dextran, such as blockages in blood vessels caused by the accumulation of dextran molecules. It may also be used in research and industry for various purposes, including the production of clarified fruit juices and wine.
Glucosidases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds, specifically at the non-reducing end of an oligo- or poly saccharide, releasing a single sugar molecule, such as glucose. They play important roles in various biological processes, including digestion of carbohydrates and the breakdown of complex glycans in glycoproteins and glycolipids.
In the context of digestion, glucosidases are produced by the pancreas and intestinal brush border cells to help break down dietary polysaccharides (e.g., starch) into monosaccharides (glucose), which can then be absorbed by the body for energy production or storage.
There are several types of glucosidases, including:
1. α-Glucosidase: This enzyme is responsible for cleaving α-(1→4) and α-(1→6) glycosidic bonds in oligosaccharides and disaccharides, such as maltose, maltotriose, and isomaltose.
2. β-Glucosidase: This enzyme hydrolyzes β-(1→4) glycosidic bonds in cellobiose and other oligosaccharides derived from plant cell walls.
3. Lactase (β-Galactosidase): Although not a glucosidase itself, lactase is often included in this group because it hydrolyzes the β-(1→4) glycosidic bond between glucose and galactose in lactose, yielding free glucose and galactose.
Deficiencies or inhibition of these enzymes can lead to various medical conditions, such as congenital sucrase-isomaltase deficiency (an α-glucosidase deficiency), lactose intolerance (a lactase deficiency), and Gaucher's disease (a β-glucocerebrosidase deficiency).
Dextrans are a type of complex glucose polymers that are formed by the action of certain bacteria on sucrose. They are branched polysaccharides consisting of linear chains of α-1,6 linked D-glucopyranosyl units with occasional α-1,3 branches.
Dextrans have a wide range of applications in medicine and industry. In medicine, dextrans are used as plasma substitutes, volume expanders, and anticoagulants. They are also used as carriers for drugs and diagnostic agents, and in the manufacture of immunoadsorbents for the removal of toxins and pathogens from blood.
Dextrans can be derived from various bacterial sources, but the most common commercial source is Leuconostoc mesenteroides B-512(F) or L. dextranicum. The molecular weight of dextrans can vary widely, ranging from a few thousand to several million Daltons, depending on the method of preparation and purification.
Dextrans are generally biocompatible and non-toxic, but they can cause allergic reactions in some individuals. Therefore, their use as medical products requires careful monitoring and testing for safety and efficacy.
Gammaproteobacteria is a class of proteobacteria, a group of Gram-negative bacteria. This class includes several important pathogens that can cause various diseases in humans, animals, and plants. Some examples of Gammaproteobacteria include Escherichia coli (a common cause of food poisoning), Pseudomonas aeruginosa (a leading cause of hospital-acquired infections), Vibrio cholerae (the causative agent of cholera), and Yersinia pestis (the bacterium that causes plague).
Gammaproteobacteria are characterized by their single flagellum, which is used for motility, and their outer membrane, which contains lipopolysaccharides that can elicit an immune response in host organisms. They are found in a wide range of environments, including soil, water, and the guts of animals. Some species are capable of fixing nitrogen, making them important contributors to nutrient cycling in ecosystems.
It's worth noting that while Gammaproteobacteria includes many pathogenic species, the majority of proteobacteria are not harmful and play important roles in various ecological systems.
Glucosyltransferases (GTs) are a group of enzymes that catalyze the transfer of a glucose molecule from an activated donor to an acceptor molecule, resulting in the formation of a glycosidic bond. These enzymes play crucial roles in various biological processes, including the biosynthesis of complex carbohydrates, cell wall synthesis, and protein glycosylation. In some cases, GTs can also contribute to bacterial pathogenesis by facilitating the attachment of bacteria to host tissues through the formation of glucans, which are polymers of glucose molecules.
GTs can be classified into several families based on their sequence similarities and catalytic mechanisms. The donor substrates for GTs are typically activated sugars such as UDP-glucose, TDP-glucose, or GDP-glucose, which serve as the source of the glucose moiety that is transferred to the acceptor molecule. The acceptor can be a wide range of molecules, including other sugars, proteins, lipids, or small molecules.
In the context of human health and disease, GTs have been implicated in various pathological conditions, such as cancer, inflammation, and microbial infections. For example, some GTs can modify proteins on the surface of cancer cells, leading to increased cell proliferation, migration, and invasion. Additionally, GTs can contribute to bacterial resistance to antibiotics by modifying the structure of bacterial cell walls or by producing biofilms that protect bacteria from host immune responses and antimicrobial agents.
Overall, Glucosyltransferases are essential enzymes involved in various biological processes, and their dysregulation has been associated with several human diseases. Therefore, understanding the structure, function, and regulation of GTs is crucial for developing novel therapeutic strategies to target these enzymes and treat related pathological conditions.
Sucrose is a type of simple sugar, also known as a carbohydrate. It is a disaccharide, which means that it is made up of two monosaccharides: glucose and fructose. Sucrose occurs naturally in many fruits and vegetables and is often extracted and refined for use as a sweetener in food and beverages.
The chemical formula for sucrose is C12H22O11, and it has a molecular weight of 342.3 g/mol. In its pure form, sucrose is a white, odorless, crystalline solid that is highly soluble in water. It is commonly used as a reference compound for determining the sweetness of other substances, with a standard sucrose solution having a sweetness value of 1.0.
Sucrose is absorbed by the body through the small intestine and metabolized into glucose and fructose, which are then used for energy or stored as glycogen in the liver and muscles. While moderate consumption of sucrose is generally considered safe, excessive intake can contribute to weight gain, tooth decay, and other health problems.
Fructose is a simple monosaccharide, also known as "fruit sugar." It is a naturally occurring carbohydrate that is found in fruits, vegetables, and honey. Fructose has the chemical formula C6H12O6 and is a hexose, or six-carbon sugar.
Fructose is absorbed directly into the bloodstream during digestion and is metabolized primarily in the liver. It is sweeter than other sugars such as glucose and sucrose (table sugar), which makes it a popular sweetener in many processed foods and beverages. However, consuming large amounts of fructose can have negative health effects, including increasing the risk of obesity, diabetes, and heart disease.
Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.
There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:
1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.
Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.
Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).
Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.
Substrate specificity can be categorized as:
1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.
Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.
Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.
Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.
Isomaltose
Glucan 1,6-α-isomaltosidase
Maltose
Isomaltooligosaccharide
Sucrose intolerance
Sucrase-isomaltase
Enzyme promiscuity
Icodextrin
Maltase
Trefoil knot fold
List of diseases (C)
List of MeSH codes (D09)
C12H22O11
List of EC numbers (EC 3)
Glycogen storage disease type II
Isomaltose - Wikipedia
Isomaltose, TMS
Isomaltose (definition)
High Quality Isomaltose 499-40-1
Other Native Semisynthetic Glycans | Product Tags A - Z
Cells | Free Full-Text | Enhancing Salt Tolerance of Plants: From Metabolic Reprogramming to Exogenous Chemical Treatments and...
MedlinePlus: Genetic Conditions: C
KEGG REACTION: R01718
Fermentation | Free Full-Text | Heterologous Expression of Thermotolerant α-Glucosidase in Bacillus subtilis 168 and...
Is Truvia Healthy? | Food Renegade
Frontiers | Essentiality of the Maltase AmlE in Maltose Utilization and Its Transcriptional Regulation by the Repressor AmlR in...
Effects of pH and sugar supplements on bacteriocin-like inhibitory substance production by Pediococcus pentosaceus |...
Pediatric Malabsorption Syndromes: Background, Pathophysiology, Epidemiology
International Classification of Diseases - Endocrine, Nutritional and Metabolic Diseases, and Immunity Disorders
Australia New Zealand Food Standards Code - Schedule 3 - Identity and purity
Mars patent for multi-texture caramel process
Classification, Structure and Properties of Carbohydrates - agriinfo.in
Bioscience, Biotechnology, and Biochemistry
江蘇先卓食品科技股份有限公
GH19 2 Eukaryota Acacia koa AFY08283.1 ncbi
ID 3.2.1.48
Hypothesis
SCD Diet: Can a Specific Carbohydrate Diet Help You? - Dr. Axe
Baklava with olives, pistachio & ice cream + Cretanthos ''Bio Early Harvest Bon Bon'' | Cretanthos
TYPES OF CARBOHYDRATES(SUGARS AND NON SUGARS) - Saga of Life
Research Reagents Supplier - NAGASE Europe
FComEx: Listing Compounds in the FoodComEx Library
Metabolite High Resolution MS/MS Spectral Library
D -(+)-Cellobiose analytical standard 528-50-7
Lactose2
- Module-II Disaccharides:Establishment of structures of sucrose and lactose, biological importance and structure of isomaltose, trehalose and maltose. (cutm.ac.in)
- 2. Double Sugars (disaccharides) - lactose, sucrose, maltose and isomaltose. (oilchangeandfilter.com)
Sucrose1
- Patients with rare hereditary problems of fructose intolerance, glucose-galactose malabsorption or sucrose-isomaltose insufficiency should not take this product. (sohaticare.com)
Maltose and isomaltose2
- Glucoamylase enzyme also helps in catalyzing the reverse reaction in which the dextrose molecules get combined to form maltose and isomaltose. (infinitabiotech.com)
- Maltose and isomaltose are found in corn syrup and candies and dietary starches. (oilchangeandfilter.com)
Similar to maltose2
- Isomaltose is a disaccharide similar to maltose, but with a α-(1-6)-linkage instead of the α-(1-4)-linkage. (wikipedia.org)
- Isomaltose is an isomer of maltose, which is similar to maltose. (turito.com)
Sugars1
- Open in a new window), FSA Blog *In the case of D-tagatose and isomaltose this should read other sugars. (westved.eu)
Glucose1
- Isomaltose is a product of the caramelization of glucose. (richest-group.com)
Sugar3
- Isomaltose is a reducing sugar. (wikipedia.org)
- Isomaltose has low fat ,low sugar and high fiber, high protein content, for those who love sweets and worry about get fatting, also suitable for people who have high blood pressure, high blood fat, high blood sugar, coronary heart disease, constipation, dental caries and olderly food. (richest-group.com)
- ISOMALTOSE Sugar substitute. (com.gr)
High1
- Isomaltose is produced when high maltose syrup is treated with the enzyme transglucosidase (TG) and is one of the major components in the mixture isomaltooligosaccharide. (wikipedia.org)
Maltose5
- Isomaltose is a disaccharide similar to maltose, but with a α-(1-6)-linkage instead of the α-(1-4)-linkage. (wikipedia.org)
- Isomaltose is produced when high maltose syrup is treated with the enzyme transglucosidase (TG) and is one of the major components in the mixture isomaltooligosaccharide. (wikipedia.org)
- Therapy for this disorder is aimed at sucrose, isomaltose, and maltose restriction. (medscape.com)
- The aim of this research was to develop a method that would allow simple and accurate measurement of available carbohydrates, defined as non-resistant starch, maltodextrins, maltose, isomaltose, sucrose, lactose, glucose, fructose and galactose. (megazyme.com)
- Sucrose, lactose, maltose and isomaltose are completely hydrolyzed by specific enzymes to their constituent monosaccharides, which are then measured using pure enzymes in a single reaction cuvette. (megazyme.com)
Sucrose-isomaltose malabsorption1
- Other names for CSID include genetic sucrase-isomaltase deficiency (GSID), congenital sucrose intolerance, congenital sucrose-isomaltose malabsorption, disaccharide intolerance I, SI deficiency, or sucrase-isomaltase deficiency. (iffgd.org)
Disaccharide3
- A second crystal structure of the ROK repressor in complex with isomaltose (its disaccharide activator) reveals the mechanism of transcriptional activation. (nih.gov)
- B) Structure of ROK repressor bound to the disaccharide inducer isomaltose. (nih.gov)
- We attempted to develop an efficient method for producing isomaltose, a disaccharide consisting of an α-(1â 6)-linkage, from starch by combining enzymes of known activity. (bvsalud.org)
Corn1
- In the case of the patient presented here, the sucrose was first introduced as a component of the antibiotic cefdinir and then upon transition to other formulas that contained corn syrup solids, thus containing isomaltose and sucrose, and so the diarrhea continued. (medscape.com)
Deficiency1
- BACKGROUND & AIMS: The sucrase-isomaltase (SI) c.273_274delAG loss-of-function variant is common in Arctic populations and causes congenital sucrase-isomaltase deficiency, an inability to breakdown and absorb sucrose and isomaltose. (ku.dk)
Product1
- PRE SPORT is a brand new product using 30% isomaltose. (thefeed.com)
Complex1
- Key Highlights: Iron polymaltose is a water soluble, macro-molecular complex of iron (III) hydroxide and isomaltose. (ailaaj.com)
Method1
- We discovered a novel enzyme in our pursuit of an improved method for the production of isomaltose. (bvsalud.org)
Activity2
- ntSI and ctSI show additional activity toward α-1,6 (isomaltose substrates) and α-1,2 (sucrose) glycosidic linkages, respectively. (nih.gov)
- Isomaltose E953, E102, E133 (may impair activity and attention in children) Note for allergy sufferers: Can be slightly laxative in large amounts. (sweetsworld.com.au)