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CAS number :9001-57-4
Molecular Weight :261.940
Molecular Formula :C5H10Br2O2
Boiling Point : 370.9±42.0°C at 760 mmHg
Density :2.0±0.1 g/cm3
Flash Point:178.1±27.9 °C
EINECS :232-615-7
Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar) into fructose and glucose.
Alternative names for invertase include EC 3.2.1.26, saccharase, glucosucrase, beta-h-fructosidase, beta-fructosidase, invertin, sucrase, maxinvert L 1000, fructosylinvertase, alkaline invertase, acid invertase, and the systematic name: beta-fructofuranosidase.
The resulting mixture of fructose and glucose is called inverted sugar syrup.
Related to invertases are sucrases.
Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose.
Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond.
For industrial use, invertase is usually derived from yeast.
Invertase is also synthesized by bees, which use it to make honey from nectar.
Invertase (INV) catalyzes the hydrolysis of sucrose into glucose and fructose.
INV is produced by bees which use it to make honey from nectar.
Cell-wall Invertase is crucial for metabolism, growth and differentiation in plants.
Extracellular Invertase catalyzes the cleavage of the transport sugar sucrose released into the app-last.
Invertase is used in the food industry to produce fructose which is sweeter and does not crystallize easily.
Optimal temperature at which the rate of reaction is at invertases greatest is 60 °C and an optimum pH of 4.5.
Typically, sugar is inverted with sulfuric acid.
Invertase is expensive, so it may be preferable to make fructose from glucose using glucose isomerase, instead.
Chocolate-covered cherries,other cordials, and fondant candies include invertase, which liquefies the sugar.
Once the candy is manufactured, it needs at least a few days to a few weeks in storage so the invertase has time to break down the sucrose.
Urea acts as a non-competitive inhibitor of invertase, presumably by breaking the intramolecular hydrogen bonds contributing to the tertiary structure of the enzyme.
Recombinant invertase (b-fructofuranosidase; EC 3.2.1.26) is purified from a modified E. coli strain.
Invertase is an enzyme that catalyzes the hydrolysis of sucrose.
The enzyme is provided in 3.2 M ammonium sulphate.
Invertase is S-bD-fructo-furanosidase isolated from S. cerevisiae and other microorganisms.
Hydrolysis from sucrose to fructose and glucose is catalyzed by this enzyme.
The production of inverted sugar is one of invertase’s numerous applications.
Due to its sweetening effects, which are more than sucrose, it has great industrial significance and has good prospects for its use in biotechnology.
Invertase is more active at temperatures between 40 and 60°C and pH ranging from 3 to 5.
Microorganisms such as filamentous fungi are good producers of invertase with potential use in various industries.
Cultivated the filamentous fungus Rhizopus sp. in a wheat bran medium and obtained invertase.
Another potential invertase-producing fungus is Aspergillus casiellus.
Intervase was inoculated in a soybean meal medium and after 72 h its crude extract was isolated.
As most invertases used in the industry are produced by yeasts, the search for high yielding fungi is a requisite.
Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar).
The resulting mixture of fructose and glucose is called inverted sugar syrup.
Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose.
Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond.
Invertase (β-fructofuranosidase, EC 3.2.1.26) is easily obtainable and exhibits transferase activity so can be exploited for synthesis of fructooligosaccharides using sucrose as the donor and acceptor of the transferred glycoside.
But the transferase activity of this enzyme in aqueous media is typically low because water is the preferred acceptor .
Although Invertase is known that the transglycosylating activity of glycosyl hydrolase may be enhanced by using high substrate concentration and/or low water media, it is not always feasible to use high substrate concentration because of the problem of solubility or substrate inhibition.
With respect to invertase catalysis high substrate concentration do not correspondingly increase oligosaccharide formation.
The amount of oligosaccharide synthesized by this enzyme in aqueous medium is below 10 % (w/w) even in media containing >60 % (w/v) sucrose.
Invertase enzyme is the quick and safe tool for breaking down sucrose into glucose and fructose at very high conversion rates, without the risk of producing hydroxy-methyl-furfural (HMF) which is toxic for bees.
Conditions for optimal inversion need pH (acidity) regulation and temperature control.
Quick and safe sugar inversion for apiculture.
Invertase is one of the secret ingredients in the candy-making industry.
Invertase is an enzyme that is commonly used to make candy liquid centers, chocolate-covered cherries, fondant candies, creme eggs, and other cordials.
Invertase is usually derived from yeast, either from bread factories or beer breweries.
Invertase is sold either as a clear liquid or as a powder that can be dissolved in water.
When added to sucrose (table sugar) or foods that include sucrose, invertase splits the sugar into its component parts of glucose and fructose.
Invertase is commonly called "invert sugar" or "inverted sugar syrup." Inverted sugar is frequently used in commercial baking and candy recipes because it keeps baked goods moist for longer periods of time.
Chemists during the 1800s were studying the effect of yeast on sugar and realized that before the sugar began fermenting, it changed form.
After much research, the chemists isolated the enzyme that caused this: invertase.
By the year 1900, the process for deriving invertase from yeast was commonly used.
Over the course of the next 20 plus years, chemists found many uses for invertase, most importantly in candy-making.
Enzyme Activity:Sucrase/Invertase
EC Number:3.2.1.26
CAZy Family:GH32
CAS Number:9001-57-4
Synonyms:beta-fructofuranosidase; beta-D-fructofuranoside fructohydrolase,EC 3.2.1.26; saccharase; glucosucrase; beta-h-fructosidase; beta-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; beta-fructofuranosidase
Source:Yeast
Expression:Purified from Yeast
Specificity:Hydrolysis of terminal non-reducing β-D-fructofuranoside residues in β-D-fructofuranosides.
Specific Activity:~ 300 U/mg of solid (40oC, pH 4.5 on sucrose)
Unit Definition:One Unit of invertase activity is defined as the amount of enzyme required to hydrolyze one µmole of sucrose (1% w/v) per minute in sodium acetate buffer (100mM), pH 4.5 at 40oC.
Temperature Optima:60°C
pH Optima:4.5
CAS Number:9001-57-4
Enzyme Commission number: 3.2.1.26 (BRENDA, IUBMB)
EC Number: 232-615-7
MDL number:MFCD00131410
NACRES:NA.21
Information on basic physical and chemical properties:
Appearance: Physical state at 20 ºC: Liquid
Appearance: Not available
Colour: Not available
Odour: Not available
Odour threshold: Non-applicable *
Volatility:Boiling point at atmospheric pressure: 100 ºC
Vapour pressure at 20 ºC: 2350 Pa
Vapour pressure at 50 ºC: 12381,01 Pa (12,38 kPa)
Evaporation rate at 20 ºC: Non-applicable *
Density at 20 ºC: 1280,7 kg/m³
Relative density at 20 ºC: 1,281
Dynamic viscosity at 20 ºC: 2,23 cP
Kinematic viscosity at 20 ºC: 1,74 cSt
Kinematic viscosity at 40 ºC: Non-applicable *
Concentration: Non-applicable *
pH: Non-applicable *
Vapour density at 20 ºC: Non-applicable *
Partition coefficient n-octanol/water 20 ºC: Non-applicable *
Solubility in water at 20 ºC: Non-applicable *
Solubility properties: Non-applicable *
Decomposition temperature: Non-applicable *
Melting point/freezing point: Non-applicable *
Explosive properties: Non-applicable *
Oxidising properties: Non-applicable *
Flash Point: Non Flammable (>60 ºC)
Flammability (solid, gas): Non-applicable *
Autoignition temperature: 480 ºC
Lower flammability limit: Non-applicable *
Upper flammability limit: Non-applicable *
Lower explosive limit: Non-applicable *
Upper explosive limit: Non-applicable *
Surface tension at 20 ºC: Non-applicable *
Refraction index: Non-applicable
Invertase (EC 3.2.1.26; β-fructofuranosidase) catalyzes the hydrolysis of the disaccharide sucrose (table sugar) into glucose and fructose and is a major enzyme present in plants and microorganisms.
Because the yeast Saccharomyces was one of the preferred materials in early biochemical studies, yeast invertase became one of the classical model enzymes.
The existence in yeast of a substance capable of inverting dextrorotatory cane sugar into a levorotatory sugar that was identified
On the basis of sequence similarity, invertase is classified within family 32 of the glycoside hydrolases.
Invertase is encoded by the SUC2 (Saccharomyces cerevisiae S288C) gene.
In yeast invertase enzyme exist in: glycosylated (secreted) and non-glycosylated (intracellular) form.
The external invertase is composed of carbohydrate (50%) and 60,000 D subunits.
Invertase from baker′s yeast (S. cerevisiae) used in the below:
-in liquid media (YES) and is used to determine the invertase activity
supplemented to the reaction mixture in the extraction and analysis of -sugars and starch
-for sucrose hydrolysis
Invertase, also called beta-fructofuranosidase cleaving the terminal non-reducing beta-fructofuranoside residues, is a glycoprotein with an optimum pH 4.5 and stability at 50 °C.
Invertase is widely distributed in the biosphere especially in plants and microorganisms.
Saccharomyces cerevisiae commonly called baker's yeast is the chief strain used for the production and purification of the enzyme. Invertase in nature exists in different isoforms.
In yeasts, it is present either as extracellular Invertase or intracellular Invertase.
In plants, there are three isoforms each differing in biochemical properties and subcellular locations.
Invertase in plants is essential not only for metabolism but also help in osmoregulation, development and defence system.
In humans, the enzyme acts as an immune booster, as an anti-oxidant, an antiseptic and helpful for bone cancer or stomach cancer patients in some cases.
Invertase plays a central role as it is a sucrose hydrolyzing enzyme, named because of the inversion in the optical rotation during the hydrolysis of sucrose.
Invertase hydrolyzes sucrose into glucose and fructose yielding a colorless product, unlike acid hydrolysis which produces colored products.
One unit will hydrolyze 1.0 μmole sucrose to glucose and fructose per minute at pH 4.6 at 25 °C.
Invertase is very common in the natural world, especially in plants and various microorganisms.
Plants like Japanese pear fruit, the common garden pea, and cereal oats are good sources of invertase.
But the most common source by far is Saccharomyces cerevisiae, also known as ale yeast, bread yeast, or wine yeast.
So why do we want it?
Well, invertase is an important ingredient in the production of candies and frostings.
When added to regular sugar syrup, it breaks down (or inverts) the disaccharide sucrose into two monosaccharides, glucose and fructose.
The resulting mixture, called invert sugar or invert syrup, helps keep baked good soft and moist.
Invertase is also the magic ingredient in chocolate-covered liquid cherries.
Cherries are covered in a fondant that has been treated with a small bit of invertase and then coated with chocolate.
Slowly, in a process that spans several days, the invertase breaks down the sucrose into the transparent, sweet, syrupy confection that surrounds the cherry and fills the hard chocolate shell.
Honey bees produce their own invertase.
The other big producer of invertase is the honey bee.
To store honey in its runny liquid form, the bees use invertase to break down the sucrose portion of nectar.
Sucrose is a common ingredient of nectar, but after the bees add invertase, the nectar is inverted into its two main components.
In addition, the inverted product becomes acidic because the fructose donates a proton during the reaction, causing it to behave like an acid.
That is part of the reason honey is so acidic.
Acidity is also enhanced by other bee-produced enzymes including glucose oxidase, which forms gluconic acid (among other things).
Invertase is mainly used in the food (confectionery) industry where fructose is preferred over sucrose because it is sweeter and does not crystallize easily.
Without the aid of invertase, sucrose can be hydrolyzed relatively easily and the reaction proceeds in an acidic environment.
There are six classes of enzymes and invertase belongs to the hydrolase class of enzymes.
However, the use of invertase is rather limited because, glucose isomerase, can be used to convert glucose to fructose more inexpensively.
For health and taste reasons, its use in the food industry requires that invertase be highly purified.
Invertase occurs widely in nature and its presence has been reported in plants, certain animal tissues and microorganisms.
Invertase or β- fructofuranosidase (EC 3.2.1.26) resulting in the production of invert sugar which has a lower crystal than sucrose at high concentrations, finds numerous applications in the food industry.
Confectionary’s preference for invert sugar hovers around its ability to keep the products fresh and soft for prolonged periods.
Soluble invertase is used in the sweet industry for the production of artificial honey.
Enzyme catalyzed hydrolysis has the advantage of colorless products compared to the colored version obtained through acid hydrolysis.
A wide range of microorganisms produce invertase and can, thus utilize sucrose as a nutrient.
Commercially, invertase is biosynthesized chiefly by yeast strains of Sacharomyces cerevisiae or Sacharomyces carlsbergensis.
Even within the same yeast culture, invertase exists in more than one form.
For example, the intracellular invertase has a molecular weight of 135,000 Daltons whereas the extracellular variety has a molecular weight of 270,000 Daltons.
In contrary to most other enzymes, invertase exhibits relatively high activity over a broad range of pH (3.5-5.5), with the optimum near pH of 4.5.
The enzyme activity reaches a maximum at about 55°C. The Michaelis-Menten (Km) values of various enzymes vary widely, but for most enzymes Km is between 2 mM and 5 mM.
The Michaelis-Menten value for the free enzyme is approximately 30 mM. Invertase is strongly inhibited by heavy metals.
Aniline also inhibits enzyme activity and is considered as a poison. Pesticides or herbicides generally derive their potency from their ability to inhibit enzymes for the growth or survival of organisms.
Cures of various diseases are also based on the discovery of enzyme inhibitors.
Substrate and product may also themselves act as enzyme inhibitors.
Invertase can be applied for any inversion of sucrose especially liquefied cherry centres, creams, mints, truffles, marshmallow, invert syrup and other fondants.
Invertase is used to improve shelf life of confections.
Invertase is available in single, double and triple strengths and is packaged in one, ten and 44 pound containers for ease of use, storage and cost efficiency.
Invertase 200,000 is powered invertase preparation, which can be applied in the confectionery industry for the production of invert syrup starting from beet or cane sugar.
When invertase 200,000 is used for this process, no browning appears and no hydroxymethylfural will form which is a normal phenomenon during hydrolysis with acid.
Invertase can be also be used to prevent sugar crystallization in confections by hydrolysis of sucrose (glucose and fructose) in fondants or chocolate coated candies with soft centres.
In addition to its main confectionery application, Invertase 200,000 can be used to produce melibiose from raffinose or D-Fructose from inulin, since it contains β - fructosidase activity.
Invertase can also be used in some specialty fruit juice products to decrease sucrose level.
Invertase, also known as Fermvertase, is a natural enzyme used to change fondant from a solid to a liquid.
Invertase is also used in commercial baking and candy making for moisture retention.
Adding invertase to candy recipes, such as fondant candy fillings, will result in liquifying the fondant over time.
Invertase is used in candies like cherry cordials and cream eggs to make the creamy liquid center.
Invertase can also be used to prevent crystallization in ganache centers.
Add invertase to moist fondant, and your chocolate covered creams will be creamy and smooth after they are dipped.
Typical application rate is 1 to .25 percent of total.
The more invertase that is used, the quicker the reaction time (twice the invertase level will enable the reaction to take place in half the time).
Alcohol and acids can negatively impact invertase.
For this reason, it is best to incorporate all ingredients to fondant creams before adding invertase.
The liquifying process takes a few days and up to a week to happen, so plan on making candies ahead of time to allow the reaction to take place.
Storing candies at room temperature will speed the process.
For maximum enzymatic activity and shelf-life, keep product refrigerated.
Recommended storage temperature is 39º - 46ºF.
Invertase (fructofuranoside fructohydrolase) (fructofuranoside fructohydrolase) specifically catalyzes the hydrolysis of β-D-fructofuranoside bonds in non-reducing sugars.
Not only can catalyze the hydrolysis of sucrose to produce glucose and fructose, but also can catalyze the hydrolysis of raffinose to produce dense disaccharide and fructose.
An intervase enzyme that catalyzes the hydrolysis of sucrose into fructose and glucose.
Intervase is widely found in animals, plants and microorganisms, and is mainly obtained from yeast.
Since Bertholet discovered invertase from Sacchacomyces Cerevisiae in 1860, it has been extensively studied.
Invertase (specifically catalyzes the hydrolysis of α-fructofuran glycoside bonds in non-reducing sugars, is relatively specific.
Intervase can not only catalyze the hydrolysis of sucrose to produce glucose and fructose, but also the hydrolysis of raffinose to produce dense disaccharides and fructose.
The intervase enzyme exists in two forms on the outside and inside of the yeast cell membrane.
Intervase is called external yeast invertase in the outer cell wall of the cell membrane, and its activity accounts for most of the activity of the sucrase, which contains 50% ~ 70 ( Mass Fraction).
The glycoprotein of the sugar component; what is called internal yeast invertase in the cytoplasm inside the cell membrane contains a small amount of sugar.
The protein part of the two enzymes is a double subunit (dimer) structure.
The amino acid composition of the two forms of enzymes is different. Each subunit of the outer enzyme has two more amino acids than the inner enzyme-serine and methionine.
The external enzyme is about 270KD (or 220KD, depending on the source of yeast) and the internal enzyme is about 135KD.
Although the two enzymes are quite different in composition, the substrate specificity and kinetic properties are still very similar, but because the internal enzyme content is very small, it is extremely difficult to extract.
Sources of Invertase:
The official name for Invertase is beta-fructofuranosidase (EC.3.2.1.26), which implies that the reaction catalyzed by the enzyme, is the hydrolysis of the terminal non-reducing beta-fructofuranoside residues in beta-fructofuranosides.
Invertase is widely distributed among the biosphere.
Invertase is mainly characterized in plants and microorganisms.
Saccharomyces cerevisiae commonly called Baker's yeast is the chief strain used for the production of Invertase commercially.
They are found in wild growing, on the skin of grapes and other fruits.
Though plants like Japanese Pear fruit (Pyrus pyrifolia), Pea (Pisum sativum), Oat (Avena sativa) can also be used, but generally microorganisms like S.cerevisiae, Candida utilis, A.niger are considered ideal for their study.
Kinetics of Invertase enzyme
In contrary to most other enzymes, Invertase exhibits relatively high activity over a broad range of pH (3.5–4.5) with the optimum near pH of 4.5.
The Invertase enzyme activity reaches a maximum at 55 °C.
The Michaelis–Menten (Km) value for the free enzyme is typically 30 mM.
The Invertase enzyme is a glycoprotein, stable at 50 °C.
The cations Hg²+, Ag+, Ca²+ and Cu²+ exhibit a marked inhibition of the enzyme.
Competitive inhibition was observed with the fructose analogue 2, 5-anhydro-D-mannitol suggesting that the enzyme was inhibited by the furanose form of fructose.
Isoforms of Invertase in plants
Several isoforms of Invertase exist with different biochemical properties and subcellular locations in plants.
On the basis of solubility, optimum pH, isoelectric point and subcellular localization, plant Invertase can be classified into three subgroups.
Three biochemical subgroups of Invertase in plants:
vacuolar (soluble acid), cytoplasmic (soluble alkaline) and cell wall bound Invertase.
The presence of multiple isoform of Invertase in nature have functionally beneficial role to the plants.
Insoluble acid/cell wall bound Invertase:
Insoluble acid Invertase (INAC-INV) is cell wall bound, glycosylated protein with a variable molecular weight ranging between 28 and 64 KDa.
Insoluble acid Invertase has an optimum pH of 4.0, temperature optimum of 45 °C and an isoelectric point of 9.
Insoluble acid Invertases activity is inhibited by 6.2 mM Copper sulphate.
Insoluble acid Invertase is localized in the basal endosperm and pedicel tissue in maize kernels.
Using immunological techniques, it was concluded that is involved in the normal development of the endosperm cells and maternal cells in pedicel tissues in maize.
Using a bean as a plant material, in seed development, it was found in thin walls of the seed coat of the parenchyma cells.
Insoluble acid Invertase is a true member of β-fructofuranosidases which can react with sucrose and raffinose as substrates.
Soluble acid/vacuolar Invertase:
Acid invertases, CWIs and VIs, belong to the GH32 family.
CWIs play a key role in sucrose partitioning, plant development and cell differentiation while VIs are involved in cell expansion, sugar storage and regulation of cold induced sweetening .
Both are post-translationally regulated by proteinaceous inhibitors (INHs) which belong, with pectin methylesterase inhibitors (PMEIs), to the pectin methylesterase inhibitor related protein (PMEI-RP) family (Pfam 04043).
Vacuolar Invertase has an acidic pI with a pH range between 4.5 and 5.0.
Along with sucrose, Invertase also hydrolyzes raffinose or stachiose being as a true member of β-fructofuranoside family.
The Invertase enzyme loses Invertases activity when reacted by heavy metal ions like mercury or silver.
Also, glucose acts as a non-competitive inhibitor for the enzyme and fructose being a competitive inhibitor.
The mature polypeptide is N-glycosylated and has a molecular mass of approximately 70 KDa.
Soluble acid Invertase plays important biological functions related to sucrose metabolism and predominantly hydrolyzes sucrose for growth and developmental processes.
Also, sucrose hydrolysis by soluble acid Invertase helps in regulation of osmotic pressure which is controlled by cell expansion which depends on size of vacuole.
Soluble alkaline/cytoplasmic Invertase:
Soluble alkaline Invertase is a non-glycosylated polypeptide expressed at low levels.
The two isoforms are encoded by the same gene and two transcripts originate from differential splicing of a hetero nuclear mRNA.
The native polypeptides are homo tetramers with a molecular mass of 54–65 KDa.
Using cDNA expression, when the amino acid sequence of soluble alkaline Invertase was deduced, it lacks N-terminal signal peptide and has no similarity with other forms of Invertases.
Soluble alkaline Invertase is not a member of β-fructofuranosidase family as it hydrolyzes sucrose only unlike other acid Invertases.
Soluble alkaline Invertase is found in all plant organs at different developmental stages, especially in the developing tissues implying it has growth related functions
Plant osmoregulation and metabolism:
To provide cell, fuel for respiration, carbon and energy for the synthesis of different compounds,
Invertase cleave sucrose into corresponding monosaccharide. By generating the necessary sucrose concentration gradient between sites of phloem loading and unloading, Invertase also help in long-distance transport of sucrose.
Hydrolysis of sucrose into glucose and fructose influences the osmotic pressure of cells and thus helps in cell elongation and plant growth.
Developing roots of carrot or elongating stems of bean are some of the organs of the plant which contain high activity of acid Invertase especially in rapidly growing tissues.
High acid Invertase activity can also be correlated with the accumulation of hexoses in sugar storing sink organs such as fruit.
Thus, indicating that a soluble acid Invertase also function as a regulator of sugar composition in the post harvest processes.
Invertase isoenzymes are potentially to be found in all compartments which may contain sucrose as a metabolite whether as a transient or a stored molecule.
In the cytosol, sucrose synthase provides an important alternative to invertase action and sometimes even becomes the dominant obligatory route of sucrose cleavage.
The degree of expression of each of the invertase isoenzymes can show large variation according to the physiological and developmental stage of the particular organ examined and may vary in different species of plants.
The molecular basis for the regulatory patterns of invertase activity is little understood.
An evaluation of the role of invertase in leaves concluded that high activity of vacuolar invertase in such species as soybean and tobacco prevents sucrose accumulation within the vacuole.
Role of Invertase in plant development:
In the early stages, by controlling sugar composition and metabolic fluxes, Invertase appears to play key role in plant development.
Both isoenzymes i.e. cell wall Invertase and vacuolar Invertase performs functions in sucrose partitioning, when their activities have shifted development in favour of leaves.
The higher levels of Invertase activity can be observed in oat internodes reflecting the increased energy and carbon requirements to sustain the biochemical reactions during growth period.
Thus, suggesting that a close relationship exists between growth rate and level of Invertase activity.
The degradation of carbohydrate in the tissue is also observed proportional to the enhancements in respiration, and protein and cell-wall biosynthesis during the growth period.
Invertase in defence mechanism
Invertase results in a link reaction between carbohydrate degradation and pathogen responses.
This includes the phenomenon of high sugar resistance in which key pathogenesis related genes which are sugar inducible get over expressed in the plant apoplast.
This results in an increased expression of Pathogen Related (PR) proteins and thus increased resistance against viral infections.
The regulation of extracellular Invertase by phytohormones could also contribute to plant pathogen responses involving in expression of various defences related genes.
In this process the extracellular Invertase induced by sugars provides a mechanism in which the sink strength will elevate increasing the sugar concentration.
This induces PR genes and represses photosynthetic genes in addition to signals derived from the pathogen.
Applications of Invertase enzyme
An equimolar mixture of fructose and glucose (invert syrup) obtained by sucrose hydrolysis is sweeter than sucrose due to high degree of sweetness of fructose, as a result the sugar content can be increased without crystallization of the material.
The production of non-crystallizable sugar syrup from sucrose is one of the major applications of Invertase enzyme.
Invert syrup has hygroscopic properties which makes it useful in the manufacturing of soft- centred candies and fondants as ahumectants.
Alcoholic beverages, lactic acid, glycerol etc. produced by fermentation of sucrose containing substrates requires the use of Invertase.
Invertase enzyme is also associated with insulinase for the hydrolysis of inulin (poly-fructose) to fructose.
Other application of the Invertase enzyme is seen in drug and pharmaceutical industries.
Also Invertase enzyme is used in the manufacture of artificial honey and plasticizing agents which are used in cosmetics.
Invertase enzyme electrodes are used for the detection of sucrose.
Formation of undesirable flavouring agents as well as coloured impurities do not take place on enzymatic hydrolysis of sucrose instead of acid hydrolysis.
Immobilized Invertase is used for continuous hydrolysis of sucrose as the resulting shifts in the pH can be used to prevent the formation of oligosaccharides by the transferase activity associated with the soluble enzyme.
Invertase being a powerful anti-microbial agent and an anti-oxidant aids in the prevention of bacterial infestations and gut fermentation due to oxidation.
Raw honey was used in ancient India in killing bacteria, reducing intestinal ailments and was given to patients having a weak heart.
Invertase enzyme can also be used in subsiding bacterial infections because of its ability to extract moisture from the body of the patient. Honey has been proved effective in treating respiratory tract infection such as bronchitis, asthma and allergies.
Invertase along with other enzymes has also been shown to help cure colds, flu and other respiratory problems.
Invertase (E.C 3.2.1.26) also known as β-fructofuranosidase
is an enzyme which catalyzes the breakdown of sucrose which is a non-reducing disaccharide to fructose and glucose which are reducing monosaccharides.
The mixture of glucose and fructose produced is called inverted sugar syrup.
Invertases exist in different isoforms in nature and these isoforms are differentiated by their locations, in yeasts cell for example, it is present in two forms as either extracellular or intracellular invertase, while in plants, as three isoforms, each different in their biochemical properties and subcellular locations.
Invert sugar consists of an equimolar mixture of fructose and glucose which has been reported to be sweeter and to have lower crystallinity than sucrose.
Invertases are known to be used in various industrial food applications especially in the preparation of jams and candies, these enzymes are also essential in the production of non- crystallizing creams, artificial honey, lactic acid,ethanol, confectionary (food), in digestive aid tablets, powder milk for infants and other infant foods.
Despite the wide range of application of invertase in various industries, the commercially available invertase is rather expensive, thus limiting the applicability of the enzyme.
Micro-organism are mainly employed in the production of invertase in a process that needs very strict regulation of production conditions and requires high level of purificationfor taste and health reasons, thereby making the enzyme expensive.
Plant enzymes have been reported to be have higher thermal stability than microbial enzymes.
Thermostability is a very important prerequisite for industrial applicability of enzymes.
Invertase Uses
When invertase is added to sugar candy recipes, like fondant candy fillings, it gradually liquefies the fondant.
This is one way of producing the liquid center in candies like cherry cordials.
The reaction takes a few days to occur, so there is a waiting period when making liquid centers with invertase.
This Intervase enzyme also makes fondant appear smoother.
Although Intervase enzyme sounds like something made in a lab, invertase is a part of many different natural processes.
Besides bees, we actually have our own supply of invertase as part of our saliva.
The Health Benefits of Invertase:
1. Natural Immune Booster
Enzymes found in honey, such as invertase have been studied for their metabolic activity.
Studies done on asparagus found that high invertase activity found in the top portion of asparagus spears might be related to the high metabolism occurring in this portion.
2. Antioxidant Support
Invertase has many antioxidant properties, and it is a powerful agent against harmful organisms.
These two aspects allow it to aid in the defense against of bacterial infestations and gut fermentation due to oxidation.
In Ancient India, raw honey was often used in patients with a weak heart.
Invertase was known to kill off bacteria and reduce intestinal ailments.
Invertase was also used for its hygroscopic (moisture-retaining) properties, and its ability to pull moisture out of the body, causing bacterial infestations to subside.
Invertase is one of these key elements of the enzymatic support found in honey.
3. Ulcers
Because invertase creates pre-digested simple sugars, it helps reduce stomach toxicity, in that sugars do not remain in the stomach long enough to create toxic fermentation.
Fermentation is what causes bacteria and disease to build up in the digestive tract.
In this way, invertase helps protect the body from ulcers, as well as many other digestive diseases.
4. Naturally Toxic to Harmful Organisms
Again, in honey, enzymes such as invertase show the ability to turn glucose into natural hydrogen peroxide.
5. Natural Respiratory Support
Enzymes including invertase have been shown to help reduce colds, flu and other respiratory infections.
One European study on 18,000 patients found that honey drastically helped upper respiratory tract infections such as bronchitis, asthma and allergies.
6. Cancer Support
Some medicinal studies also show that the invertase enzyme may exhibit some chemotherapeutic properties.
Research done in Australia and Japan have found that the enzymes in honey helped support patients with advanced cases of both bone and stomach cancer.
In some cases, the cancers even went into regression.
Currently, enzyme therapy is being used as a vital component of many natural cancer therapies.
European researchers reported, "Studies showed that enzyme therapy can reduce the adverse effects caused by radiotherapy and chemotherapy.
There is also evidence that, in some types of tumours, survival may be prolonged and that the beneficial effect of systemic enzyme therapy seems to be based on its potential to reduce redness and swelling."
Storage of Intervase:
The invertase itself should be stored in the refrigerator for longevity.
Cold temperatures slow the invertase reaction.
Candies with invertase should be stored at room temperature instead of in the refrigerator for the best and fastest results.
If the candies are kept cool, the invertase cannot break down the sucrose and the liquification process will not occur (or will take much longer).
Conditions for safe storage, including any incompatibilities:
Technical measures for storage
-Store in a cool, dry, well-ventilated location
General conditions for storage:
-Avoid sources of heat, radiation, static electricity and contact with food.
Best storage conditions are 0 ‐ 10 °C.
Higher temperatures will cause shortage of product shelf life.
Avoid temperature above 25 °C.
Reseal open packages and use completely on short term.
History Of Invertase Enzyme
Invertase actually goes back several years.
Chemists in the 1800s were studying the effect of yeast on sugar and realised that before the sugar began fermenting it changed form.
After much research, the chemists isolated the enzyme that caused this: invertase.
By the year 1900, the process for deriving invertase from yeast was commonly used.
Over the course of the next 20 plus years, chemists found many uses for invertase, most importantly in candy-making.
Production Of Invertase Enzyme
Common sugar can be inverted quickly by mixing sugar and citric acid or cream of tartar at a ratio of about 1000:1 by weight and adding water.
If lemon juice which is about five percent citric acid by weight is used instead then the ratio becomes 50:1.
Such a mixture, heated to 114 °C (237 °F) and added to another food, prevents crystallization without tasting sour.
Inverted sugar syrup can be made without acids or enzymes by heating it up alone: two parts granulated sugar and one-part water, simmered for five to seven minutes, will be partly inverted.
Commercially prepared enzyme-catalysed solutions are inverted at 60 °C (140 °F).
The optimum pH for inversion is 5.0. Invertase is added at a rate of about 0.15% of the syrup’s weight, and inversion time will be about 8 hours.
When completed the syrup temperature is raised to inactivate the invertase, but the syrup is concentrated in a vacuum evaporator to preserve colour.
Commercially prepared hydrochloric-acid catalysed solutions may be inverted at the relatively low temperature of 50 °C (122 °F).
The optimum pH for acid-catalysed inversion is 2.15.
As the inversion temperature is increased, the inversion time decreases.
They are neutralised when the desired level of inversion is reached.
In confectionery and candy making, cream of tartar is commonly used as the acidulant, with typical amounts in the range of 0.15-0.25% of the sugar’s weight.
The use of cream of tartar imparts a honey-like flavour to the syrup. After the inversion is completed, it may be neutralised with baking soda using a weight of 45% of the cream of tartar’s weight.
The amount of water can be increased to increase the time it takes to reach the desired final temperature and increasing the time increases the amount of inversion that occurs.
In general, higher final temperatures result in thicker syrups, and lower final temperatures, in thinner ones.
All constituent sugars (sucrose, glucose, and fructose) support fermentation, so invert sugar solutions of any composition can be fermented.
Purification of invertase
The crude enzyme solution was purified by O-Sepharose FF anion exchange column chromatography.
The crude enzyme solution with high sucrase activity extracted by the SDS extraction method was precipitated with 50% ethanol by mass, dissolved and dialyzed, and then passed through a Q-Sepharose FF anion exchange column (with pH 7.0, 0.05 mol/L Tris-HCl buffer is fully equilibrated).
Intervase was eluted with a NaCI solution with a linear gradient of 0 to 1 mol/L and 60 min (containing pH values of 7.0 and 0.05 mol / L% s-HCI buffer).
The volume flow rate is 0.5 mL/min, and each mL is collected.
Measure the invertase activity and protein content of each tube eluate, and combine several tube effluents with high invertase activity.
The effluent is desalted by dialysis and dried in vacuum to be purified yeast invertase.
How to Read the Units of Measurement for Invertase
Carbohydrases such as invertase measure the hydrolysis of carbohydrates.
One SU (Sumner Unit Invertase/Sucrase) is the FCC assay of measurement, whereby one Sumner Unit is the quantity of enzyme that will convert 1 mg of sucrose to glucose and fructose in 5 minutes.
The FCC notation stands for Foods Chemical Codex, and is a division of USP (United States Pharmacopeia).
Invertase sets standards for ingredients.
In the case of enzymes, FCC is a standard assay used to accurately determine the activity of enzymes.
The current compendium is FCC VI
Synonyms:
beta-fructofuranosidase
beta-D-fructofuranoside fructohydrolase
saccharose
glucosucrase
beta-h-fructosidase
beta-fructosidase
your invert
sucrase
maxinvert L 1000
fructosilinvertase
alkaline invertase
acid invertase
beta-fructofuranosida
