Invertase

Key takeaways

Invertase belongs to mathematics; place it in that map before memorising details.
Learn the definition first, then one example that makes the definition concrete.
Connect Invertase to a quantity you can measure, compute or draw — that is where exam questions come from.
Reproduce the core statement of Invertase from memory before moving on to harder problems.

Reference excerpt

β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. Sucrose is a fructoside. Alternative names for β-fructofuranosidase EC 3.2.1.26 include invertase, saccharase, glucosucrase, β-fructosidase, invertin, fructosylinvertase, alkaline invertase, and acid invertase. 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. Invertase is a glycoprotein that hydrolyses (cleaves) the non-reducing terminal β-fructofuranoside residues. Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond. Invertase cleaves the α-1,2-glycosidic bond of sucrose. For industrial use, invertase is usually derived from yeast. It is also synthesized by bees, which use it to make honey from nectar. The temperature optimum is 60 °C and a pH optimum is 4.5. Sugar can be inverted by sulfuric acid but this is not suitable for food-grade products and enzymic hydrolysis is preferred. Invertase is produced by various organisms such as yeast, fungi, bacteria, higher plants, and animals. For example: Saccharomyces cerevisiae, Saccharomyces carlsbergensis, S. pombe, Aspergillus spp, Penicillium chrysogenum, Azotobacter spp, Lactobacillus spp, Pseudomonas spp etc.

Applications and examples Invertase is used to produce inverted sugar syrup. Invertase is expensive, so it may be preferable to make fructose from glucose using glucose isomerase, instead. Chocolate-covered candies, other cordials, and fondant candies include invertase, which liquefies the sugar.

Inhibition Urea acts as a pure non-competitive inhibitor of invertase, presumably by breaking the intramolecular hydrogen bonds contributing to the tertiary structure of the enzyme.

Structure and function

Reaction pathway Invertase works to catalyze the cleavage of sucrose into its two monosaccharides, glucose and fructose. This specific invertase (β-fructofuranosidase) cleaves the molecule from its fructose end resulting in the two monosaccharides. It does this by adding a hydrogen ion to the glycosidic atom by an imidazolium cation. From there, an unstable intermediate carbonium ion will be left behind by the leaving of an alcohol group. Finally, the nucleophilic oxygen atom from alcohol or water will attack the C-2 cation which will leave behind a fructose molecule. The active-site carboxylate anion will take action to help keep the unequal balance of electrons stabilized throughout this process.

Purpose of invertase in yeast As mentioned previously, invertase is commonly found in bakers' yeast. One of the main reasons that bakers use this yeast is to help bread rise, but another reason is to help influence the increase of sugar in bread. This function is able to happen due to the presence of invertase since glucose and fructose is sweeter than sucrose is. When looking at invertase across different species of yeasts, it has been known to be more active in some than others. The yeast that invertase is more active in is the yeast bakers use due to its higher sweetness levels.

Known crystal structures Continuing to look at invertase through Saccharomyces, it can be seen that it has a unique structure; that structure being an octameric quaternary structure. Within the octameric quaternary structure, two dimerization types can be seen that in turn, form the octamer structure. Dimerization is an important aspect of protein folding due to it increasing the affinity of substrate binding. The crystal structure shows that the invertase is made up of eight subunits. The octamer shape is made up of two different types of dimers, a “‘closed’ arrangement” and an “‘open’ assembly” dimer. Each of these types has two subunits located opposite from each other in the structure. The “‘closed’ arrangement” dimers have fourteen out of the 32 hydrogen bonds made between the catalytic domain which creates a tighter pocket for the ligand; in turn, this makes it more stable. In contrast, the “‘open’ assembly” dimers only have a few hydrogen bonds in the catalytic domain, and the interactions that strengthen the pocket come from the salt bridges between Asp-45 and Lys-385. With the weaker interactions being in the “‘open’ assembly", it causes more instability that results in a lower denaturing temperature and lower durability at high-speed centrifugation. The way that the two dimers assemble, creates an antiparallel β sheet composed of β sandwiches made from two β sheets.

Known active sites While the focus has been on invertase in Saccharomyces, one of the known active sites is in the invertase in Bifidobacterium longum and is located within the β-propeller domain. The β-propeller domain is the inside the funnel created by five blades. Some amino acids to note are, Asp-54 and Glu-235, which are on the first strand of blades 1 and 4, along with Asn-53, Gln-70, Trp-78, Ser-114, Arg-180 and Asp-181 in the fructofuranoside ring.

Worked examples

Example 1 — a first encounter with Invertase

Start with the simplest possible case. Write down what Invertase claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In mathematics, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to Invertase before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about Invertase ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of Invertase

In research: Invertase appears in mathematics research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry: Engineering practice reuses Invertase in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom: Invertase is common in secondary-school and first-year university syllabi. It links to neighbouring topics E-number additives, EC 3.2.1, Food additives, so understanding it makes those chapters shorter.
In everyday life: Look for Invertase outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.

How to study Invertase in 20 minutes

Read the reference excerpt below once, without taking notes.
Close the page and write down what Invertase means in your own words.
Compare your version with the excerpt and mark what you missed.
Work through the three examples above with pen and paper.
Explain Invertase out loud to somebody else — or to Teacher Smith in the lgStudy chat.

Frequently asked questions

What is Invertase in simple terms?

β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. Sucrose is a fructoside.

Why does Invertase matter?

Because it connects several mathematics ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study Invertase?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on Invertase.