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TERMAMYL
CAS NO: 9000-90-2
EC/LIST NO.: 232-565-6
Termamyl is a liquid enzyme containing outstanding heat-stable alpha amylase, expressed and produced by a genetically modified laboratory strain of Bacillus licheniformis.
Termamyl is an enzyme that hydrolyses 1,4 alpha glucosidic linkages in amylose and amylopectin.
Starch is rapidly broken down to soluble dextrins and oligosaccharide,
Termamyl is a liquid enzyme preparation containing an outstandingly heatstable alpha-amylase expressed in and produced by a genetically modified strain of Bacillus licheniformis.
The systematic name for the enzyme is 1,4- alpha-D-glucan glucano-hydrolase
Natunase TAA is exclusively used for liquefaction process in beer industry.
The optimal use of enzyme depends on processing parameters like viscosity, pH, temperature, processing time, type of raw material and dry substances.
The efficient output by this product comes through split dosing ratios are best determined and fine-tuned in actual practice.
Termamyl is widely used in cleaning products due to its effectiveness in combination with other enzymes produced by Novozymes (primarily proteases).
Allows with high efficiency to remove stains of starch nature.
Termamiil is a genetically expressed and produced liquid enzyme containing superior heat stable alpha mailase.
Termamyl is an enzyme that hydrolyzes 1,4 alpha glucosidic bonds in the modified laboratory strain of Bacilluslicheniformis.
Termamyl and amylopectin. Starch is rapidly broken down into soluble dextrins and oligosaccharides.
Termamyl , (α-amylase) is an enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose.
Termamyl is the major form of amylase found in humans and other mammals.
Termamyl is also present in seeds containing starch as a food reserve, and is secreted by many fungi.
Termamyl is a member of glycoside hydrolase family 13
Termamyl are starch hydrolases with several amino acid sequences that are highly conserved amongst family members.
Termamyl of A. hydrophila strains are about 48–49 kDa in size, although a larger Termamyl (70 kDa) is found in A. hydrophila JMP636.
The α Termamyl of A. hydrophila MCC-1 shows conservation in catalytic- and substrate-binding residues.
In addition, three of four calcium-binding residues (Asn100, Asp167, His201) present in other Termamyl are retained in MCC-1, consistent with the fact that this enzyme requires calcium for activity.
Glucose is a major source of energy in your body, but unfortunately, free glucose is relatively rare in our typical diet.
Instead, glucose is locked up in many larger forms, including lactose and sucrose, where two small sugars are connected together, and long chains of glucose like starches and glycogen.
One of the major jobs of digestion is to break these chains into their individual glucose units, which are then delivered by the blood to hungry cells throughout your body.
Termamyl s are one of the main enzymes used in industry.
Such enzymes hydrolyze the starch molecules into polymers composed of glucose units.
Termamyl s have potential application in a wide number of industrial processes such as food, fermentation and pharmaceutical industries.
Termamyl can be obtained from plants, animals and microorganisms. However, enzymes from fungal and bacterial sources have dominated applications in industrial sectors.
The production of Termamyl is essential for conversion of starches into oligosaccharides.
Starch is an important constituent of the human diet and is a major storage product of many economically important crops such as wheat, rice, maize, tapioca, and potato.
Starch-converting enzymes are used in the production of maltodextrin, modified starches, or glucose and fructose syrups.
A large number of microbial Termamyl has applications in different industrial sectors such as food, textile, paper and detergent industries.
The production of Termamyl has generally been carried out using submerged fermentation, but solid state fermentation systems appear as a promising technology.
The properties of each Termamyl such as thermostability, pH profile, pH stability, and Ca-independency are important in the development of fermentation process.
This review focuses on the production of bacterial and fungal Termamyl , their distribution, structural-functional aspects, physical and chemical parameters, and the use of these enzymes in industrial applications.
Termamyl is found in saliva and breaks starch into maltose and dextrin.
This form of amylase is also called "ptyalin" /ˈtaɪəlɪn/, which was named by Swedish chemist Jöns Jacob Berzelius.
The name derives from the Greek word πτυω (I spit), because the substance was obtained from saliva.
Termamyl will break large, insoluble starch molecules into soluble starches (amylodextrin, erythrodextrin, and achrodextrin) producing successively smaller starches and ultimately maltose.
Ptyalin acts on linear α(1,4) glycosidic linkages, but compound hydrolysis requires an enzyme that acts on branched products.
Salivary Termamyl is inactivated in the stomach by gastric acid.
In gastric juice adjusted to pH 3.3, ptyalin was totally inactivated in 20 minutes at 37 °C.
In contrast, 50% of Termamyl activity remained after 150 minutes of exposure to gastric juice at pH 4.3.
Both starch, the substrate for ptyalin, and the product (short chains of glucose) are able to partially protect it against inactivation by gastric acid.
Ptyalin added to buffer at pH 3.0 underwent complete inactivation in 120 minutes; however, addition of starch at a 0.1% level resulted in 10% of the activity remaining, and similar addition of starch to a 1.0% level resulted in about 40% of the activity remaining at 120 minutes.
In a starch slurry, Termamyl is satisfactorily stabilized in the presence of 50-70 ppm Ca++.
In Table 1, figures for Termamyl stability in a 30% starch slurry are shown as a function of pH and temperature for three different levels of Ca++ (ppm).
Data is considered valid for DE values in the range of 0-12.
Enzyme activity can also be expressed as an initial rate of DE (dextrose equivalent) increase for a given enzyme concentration.
The average rate of DE increase over a given time will also depend on the stability
The enzyme-catalysed degradation of starch is central to many industrial processes, including sugar manufacture and first-generation biofuels.
Classical biotechnological platforms involve steam explosion of starch followed by the action of endo-acting glycoside hydrolases termed Termamyl and then exo-acting α-glucosidases (glucoamylases) to yield glucose, which is subsequently processed.
A key enzymatic player in this pipeline is the ‘Termamyl’ class of bacterial Termamyl and designed/evolved variants thereof.
Here, the three-dimensional structure of one such Termamyl α-amylase variant based upon the parent Geobacillus stearothermophilus Termamyl is presented.
The structure has been solved at 1.9 Å resolution, revealing the classical three-domain fold stabilized by Ca2+ and a Ca2+–Na+–Ca2+ triad.
As expected, the structure is similar to the G. stearothermophilus Termamyl but with main-chain deviations of up to 3 Å in some regions, reflecting both the mutations and differing crystal-packing environments.
The starch of yam constitutes an excellent raw material to modify the texture and consistency of foods.
Its functionality depends on the molecular weight average of the amilosa and the amilopectina, as well as of the molecular organization of these glucanos within the grain, the native or natural starches are frequently not adapted for their use in some specific industrial processings.
This investigation, one carries out the modification via enzymatic of the yam starch (D.trífida) using -amilasa (Termamyl 120L, type L of Novo Nordisk) to determine their functional properties.
The established treatments for the enzymatic modification in this investigation are:
reaction temperature (50, 72 and 93ºC), concentration of starch (30, 40 and 50% p/v) and time of reaction (20, 40 and 60 minutes).
One carries out a design experimental factorial multinivel with four blocks.
The starches hydrolysated at 93ºC show dextrose equivalent (DE) highest, followed respectively by those of 72 °C and 50ºC.
The evaluated functional properties are: stability and clarity of the pasta, acidity titulable, swelling capacity, determination of the gelatinizatión point, true density, bulk density and porosity.
This investigation demonstrate the great potential of the hydrolysates of starch of D. trífida like an alternative to respond to the demands of the industrial processes in the production of foods, such as bakery products, sauces, yogurts, marmalades and frozen products.
Teramyl® is used in the following industries:
Starch industry -
the enzyme is used for continuous liquefaction of starch in steam jet cookers or similar equipment operating at temperatures up to 110ºC and thereby taking advantage of the extreme heat stability of this enzyme.
Alcohol industry -
the enzyme is used for thinning of starch in distilling mashes.
The heat stable of the enzyme is important advantage in the thinning of mashes .
Brewing industry -
Termamyl® is used for adjunct liquidification (unmalted grains such as corn, rice, rye, oats, barley, and wheat used in brewing beer which supplement the main mash ingredient - malted barley).
Due to the heat stability of the enzyme, the cooking programme can be simplified, it also means more of the adjunct can be used.
Sugar industry -
Termamyl® is used to break down starch present in cane sugar.
The starch content in the raw sugar is reduced which improves refinery filtering
Starch
Alcohol
Brewing
Sugar
The enzyme is an endoamylase which hydrolyzes 1,4-alpha-glucosidic linkages in amylose and amylopectin.
Starch is therefore rapidly broken down to soluble dextrins and oligosaccharides.
In the starch industry, Termamyl is used for continuous liquefaction of starch in steam jet-cookers or similar equipment operating at temperatures up to 105- 110°C (221-230°F), thereby taking advantage of the extreme heat stability of this enzyme.
In the alcohol industry, Termamyl is used for the thinning of starch in distilling mashes.
Here too, advantage is taken of the heat stability of the enzyme.
Furthermore, it is possible to work without pH adjustment and Ca addition, despite conditions not being optimal.
This is due to the relatively broad pH tolerance and low Ca requirements of the enzyme.
This simplifies the process and minimizes the risk of Ca scaling in the distillation column.
In the brewing industry, Termamyl is used for adjunct liquefaction.
Due to the extreme heat stability of the enzyme, the cooking programme can be simplified; an increase in proportion of adjuncts is also a possibility.
In the sugar industry, Termamyl is used to break down the starch present in cane juice.
Thereby the starch content in the raw sugar is reduced and filtration at the refinery facilitated.
Our more detailed recommendations with respect to operating conditions are provided in separate papers for each industry and are available on request.
Termamyl s are one of the main enzymes used in industry.
Such enzymes hydrolyze the starch molecules into polymers composed of glucose units.
Termamyl s have potential application in a wide number of industrial processes such as food, fermentation and pharmaceutical industries.
Termamyl s can be obtained from plants, animals and microorganisms. However, enzymes from fungal and bacterial sources have dominated applications in industrial sectors.
The production of Termamyl is essential for conversion of starches into oligosaccharides.
Starch is an important constituent of the human diet and is a major storage product of many economically important crops such as wheat, rice, maize, tapioca, and potato.
Starch-converting enzymes are used in the production of maltodextrin, modified starches, or glucose and fructose syrups.
A large number of microbial Termamyl has applications in different industrial sectors such as food, textile, paper and detergent industries.
The production of Termamyl has generally been carried out using submerged fermentation, but solid state fermentation systems appear as a promising technology.
The properties of each Termamyl such as thermostability, pH profile, pH stability, and Ca-independency are important in the development of fermentation process.
This review focuses on the production of bacterial and fungal Termamyl s, their distribution, structural-functional aspects, physical and chemical parameters, and the use of these enzymes in industrial applications.
IUPAC NAME:
1,4-α-D-Glucan-glucanohydrolase
1,4-α-D-Glucan-glucanohydrolase
4-alpha-D-glucan glucanohydrolase
a-Amylase
Alpha Amylase
Alpha amylase
ALPHA-AMYLASE
Alpha-Amylase
Alpha-amylase
alpha-Amylase
alpha-amylase
Alpha-amylase
alpha-Amylase
alpha-amylase
alpha-Amylase diluted with Starch, from Bacillus subtilis
SYNONYMS:
AMYLASE
ALPHA
ANIMAL DISTASE
AMY(a-Amylase)
Amylase(bacterial)
