How To Use Amylase With Moonshine?

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Description

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Alpha Amylase Enzyme for the conversion of grain starches into sugars.2oz packet. Use one level teaspoon for up to 15 lbs of grain in your recipe. Directions: After gelatinizing and sterilizing your grain mash above 180F allow mash to cool to 160F. Stir in amylase enzyme and let mash rest for one hour holding temperature at 150-160F using very low heat. Then cool before adding yeast.

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How do you add amylase to mash?

When to add amylase enzyme to the wort – The temperature of your mash is key to how effective amylase. In terms of timings, some brewers will add amylase immediately after adding strike water or about 30 minutes or so into an extended all-grain mash taking longer than 60 minutes.

If you increase the temperature immediately after adding amylase you’re working against yourself.
Amylase works best at 150-155°F.
Much higher than that and the enzyme is destroyed by the heat.
A common practice is to hold it at its activation temperature for an hour to allow full conversion of starch, then cool it rapidly to your fermentation temperature once the gelatinization of the malt/starch is complete.

This wiki advises : The ideal situation you want is to attain is one in which your mash rests at a temperature between 66° and 70° C (150°-158° F) to allow the amylase enzymes to do their work. The colder the rest, the more fermentable sugars will be available for fermenting, and therefore the higher alcohol content in the final beer.

The hotter the temperature, the more unfermentable sugars will reach fermentation, and thus the fuller the mouth-feel. This is, of course a comparison of otherwise duplicate mashes. Remember, the enzymes will work outside their optimum temperatures, so given an adequate amount of time, all starches can be converted to fermentables.

We suggest you read the whole wiki as it gives a very sound scientific description of mash temperatures and the various methods use you can use enzymes with. This page is a great read too,

How much amylase do I add to 5 gallons of mash?

Amylase Enzyme is typically used by all-grain brewers to add to a high adjunct mash that may be low in enzymes to aid in converting starches into sugar. This enzyme can also prevent starch haze in beer. Use 1 teaspoon per 5 gallon batch.

What enzymes are best for moonshine?

Glucoamylase – To form glucose, another enzyme is required: glucoamylase, also known as GA, AMG, or amyloglucosidase. As the alpha amylase breaks up the long starch chains into many smaller chains, it creates many new ends. Glucoamylase only works from the ends.

When alpha amylase has done its job, glucoamylase can form glucose in the cook.
That is what the yeast will eventually ferment.
This third, and final step, is called conversion or saccharification.
At this point, the enzymes have now turned starch into fermentable sugars.
The cook tastes much sweeter at this point.

With these two enzymes, you will be able to produce nearly 100% glucose which will make your yeast quite happy. However, in starch, there are some branch points in those long chains that alpha amylase and glucoamylase cannot break. If you want to completely break down the starch and get the highest yield of alcohol possible, you will need to break these branch points, too.

How much amylase to add to corn mash?

What is Amlase? – There are actually quite a few enzymes at play during the whiskey mashing process. The ones that get talked about the most are the amylases, both alpha (α) and beta (β). Make no mistake: These are important components of our mashing system.

Amylases are responsible for breaking apart much of our starch molecules into the simpler sugars we’re after. Alpha-amylase works better at higher temperatures (optimum activity occurs between 66–71°C ) than β-amylase. It is also what we call a “liquefaction” enzyme because it quickly gelatinizes our starches.

This liquefaction is a quick process that actually happens before your very eyes. Try mashing unmalted wheat or rye by itself and you’ll notice that the overall mixture is incredibly gummy and viscous. Add in 10% by total weight of malted barley and you’ll see the viscosity of your mash magically get thinner and easier to handle.

Alpha-amylase is an “endo-amylase,” meaning it tends to clip starch chains at points in the middle of the chain.
This is a fairly random process for a-amylase, but it goes a long way toward reducing the mash viscosity brought on by pasty starch granules.
This also means that a-amylase is not really our champion when it comes to producing fermentable sugar from starch.

Small amounts of sugars are produced at so random a pace that it just isn’t realistic to rely on a-amylase to give us every sugar we’re looking for. For that we need b-amylase. Beta-amylase works at lower temperatures than its hot-headed brother, generally 54–66°C (129–150°F), with the highest activity seen around 64°C (147°F).

Beta-amylase is an “exo-amylase,” which means it attacks starch chains from their ends and works its way along the chain in a methodical and linear fashion.
It breaks off one molecule of maltose (a two-glucose molecule) at a time.
Amylose is easily handled by both amylases working in concert with each other.

After all, amylose is essentially a straight chain of glucose molecules, so a-amylase and b-amylase have no issues with converting it to simpler sugars. There are some other secondary enzymes at play in this process but if you get the steps right for the amylase enzymes then the others will fall into place without any other thought.

When to add the amylase enzymes.
Before we get into when you ad the enzymes I want to say that there are a lot of differing views about how this part of the process should be done.
Most of them all work just fine.
As a beginner, don’t try to find the “right” way.
This is where the art comes into play with distilling.

Find the way that works for you. I’m going to give you the basics here and if you follow this process it will work for you every time. It should be said that different manufactures of enzymes recommend slightly different optimum temperature ranges for their product so always follow those temperature ranges.

Also, different grains react differently to different temperatures optimally.
Do your own research for specific grains.
I will be giving the optimum process for a straight corn whiskey and it will work fine for most grains, but may not be optimal.
In this process, you are going to use powdered enzymes instead of malted grains.

This is a simpler process and a good way for the beginner to start learning about the use of enzymes. As you hone your art you will want to begin to experiment with the use of malted grains to get your enzymes. Use 2.5lb corn per gallon of water when starting your mash.

Bring the temperature of the mash to 160°F, the mash will become considerably more viscous and thicken greatly.
Add cold water to bring the temp down to 150° and add 1 teaspoon of amylase for every 5 gallons of mash by total volume just to thin the mash.
Bring the temperature of the mash back up to 180-190°F, this will gelatinize the remaining starches.

Now, cool the mash back down to 148-150°f and add amylase as prescribed on the package. At this point turn off the heat and allow the mash to cool naturally. When the mash reaches 90 degrees take a small portion of the mash and add water 50/50. Add yeast to create a starter.

How much amylase is needed?

What do my test results mean? – Test results may vary depending on your age, gender, health history, and other things. Your test results may be different depending on the lab used. They may not mean you have a problem. Ask your healthcare provider what your test results mean for you.

Sudden swelling of the pancreas (acute pancreatitis) Chronic pancreatitis that suddenly gets worse Cancers of the pancreas, breast, colon, ovary, or lung A sore in the pancreas A type of cyst in the pancreas (pancreatic pseudocysts) Swelling in your abdomen (ascites) Macroamylasemia. This is a noncancer (benign) condition marked by having a substance called macroamylase in your blood. Peptic ulcer that has a hole in it (perforated ulcer) Death of tissue in your intestine (intestinal infarction) Blockage in your intestines Appendicitis Sudden swelling of the gallbladder (acute cholecystitis) Ruptured ectopic pregnancy Salivary gland swelling Swelling of the lining of your abdomen (peritonitis) Burns Diabetic ketoacidosis Kidney problems Use of certain medicines such as morphine Alcohol use Mumps Tumors in the prostate Eating disorders such as bulimia or anorexia nervosa Inflammatory bowel disease Higher levels of triglycerides (hypertriglyceridemia)

Your levels may also be higher after a pancreatic procedure such as a cholangiopancreatography. They may also be higher after surgery or trauma. Your amylase levels may be lower with these conditions:

Chronic pancreatitis Liver failure Cystic fibrosis

What does amylase do to mash?

Amylase enzyme is used during the mashing process when there are not enough naturally occuring enzymes, typically due to a mash containing a high level of adjuncts. Also used to more rapidly and completely convert starches into sugars. Usage varies, but the typical dosage rate is 1/4 oz per 5 gallons.

0.25 oz – Good for 5 gallon batch 1.5 oz – Good for 30 gallon batch

Does amylase increase rate of fermentation?

Why is the flour key to the rate of fermentation? – The kind flour that you use is one of the key things you need to understand when it comes to the speed of fermentation of your dough. A flour’s enzyme levels will depend on where in the world it was grown.

British flours for example tend to have high levels of naturally occurring enzymes because they are grown in a maritime environment.
This results in high levels of enzyme activity.
The key enzyme that leads the way is called amylase, so high levels of amylase means that dough ferments more quickly and the yeasts are more active, and more carbon dioxide is produced, making the bread bouncier and more voluptuous.

You will sometimes find flours that have had enzymes added to them – flours from the USA, for example, tend to have less naturally occurring enzymes so millers make adjustments using malt and alpha-amylase to get the liveliness and activity needed. Enzymes – there are quite a few at work as follows:

Diastase/Amylase – under the right conditions, diastase will break up some starch, liquefy it, and convert it into malt sugar. Protease – found in flour, but also in malt and yeast. Maltase. Invertase. Zymase – an enzyme complex that yeast catalyses the fermentation of sugar into ethanol and carbon dioxide.

So, amylase converts starch to dextrin’s, oligosaccharides, and the sugar maltose, and as amylases break the starch into smaller molecules, it ultimately yields maltose, which in turn is cleaved into two glucose molecules – ie sugar. Yeast do really well transforming simple sugars because they have a simple chemical structure, making them easy to break down.

So, do yeast excrete amylase? Yes, amylases are found naturally in yeast cells, however it takes time for the yeast to produce enough to break down significant quantities of starch in the bread, so the naturally occurring amylase in flour plays an important role in breaking down the starch into sugars.

Is this why some flours ferment faster than others? Yes. Essentially increasing the level of amylases in the dough, increases the quantities of sugars available for the yeast fermentation, accelerating the production of CO2. This explains why some flours ferment faster than others.

A flour that is sprouted is a good example of this. The real purpose of the enzymes is to give food to the new baby plant, but of course, we just ground this plant into flour, however it doesn’t know this. Effectively all the component parts of the seed, behave as though it landed in some soil. When you understand this then it all makes sense.

Flour is behaving like a seed that is growing and the enzymes are there to feed the plant. The yeast is very happy to find all this food and amylases love water. So, this is one of the reasons why doughs with a higher hydrations ferment faster—the amylases (and other enzymes) can literally move about and cut up the starch faster.

So, the sugar is made quicker, and the yeast get to eat up faster and produce CO2 quicker.
When yeast breaks down glucose, it transforms it into carbon dioxide and ethanol, both by-products are formed in equal parts.
So, for every glucose molecule, two molecules of carbon dioxide and two molecules of ethanol are formed.

This is aerobic respiration (funnily enough the same process we humans use). The yeast also produces ethanol as well as CO2 waste products, which in turn inflate the gluten that formed.

How much amylase is in honey?

Alpha-Amylase from Persimmon Honey: Purification and Characterization The α-amylase was extracted from pure persimmon honey and purified by DEAE-Toyopearl 650M, CM-Toyopearl 650M, and Toyopearl HW-55F column chromatographies. Molecular weight of purified enzyme was estimated to be about 58 kDa by Toyopearl HW-55F gel chromatography and SDS-PAGE, respectively suggested that the purified enzyme was a monomer. Optimum pH of the enzyme was 6.0−7.0 and optimum temperature 40°C. The enzyme was extremely inactivated at pH was higher than 7.0 or lower than 5.0. Heat inactivation occurred at 40°C. This enzyme activated by Ca 2+, Mn 2+, PCMB, and DTNB, but inhibited by Ba 2+, Fe 3+, Hg 2+, Mg 2+, and iodoacetic acid. The purified enzyme was of α -type by TLC analysis. The relative rate of hydrolysis of the polymeric substance decreased with decreasing percentage of α -1,4-linkages and with increasing percentage of α -1,6-linkages in substrate similar to the results from commercially available honey. Honey market currently shows a tendency to establish geographical limits of production with the aim of protecting a production zone that has developed and marketed a particular standard of quality. Honey composition is closely associated with its botanical origin and, to some extent the geographical area in which it originated, because soil and climate characteristics determine melliferous floral. Honey is a natural complex product produced by honeybees from the nectar of blossoms or from exudates of trees and plants to produce nectar honeys or honeydews, respectively. Honey composition depends on the plants visited by the honeybees and on the climatic and environmental conditions. The strong sweetening capacity of honey is due to the presence of the monosaccharide’s fructose and glucose as majority components about 60 to 85% and phenolic compounds, minerals, proteins, free amino acids, enzymes such as amylase (diastase), and vitamins as minor components. Amino acids in honeys are attributable to the honeybees or to plant sources. It has been known the presence of enzymes in honeys for many years. In particular, α-amylase is one of most important enzyme in honey species, although it contains a very small quantity of enzymes. The origin of α-amylase in honeys is commonly attributed to the honeybee. The nectar collected is mixed with secretions from the salivary and hypopharyngeal gland of foraging honeybees. α-Amylase was estimated to account for about only 2% of the total protein in the hypopharyngeal gland. This enzyme is largely used in Europe as a measure of honey freshness, because this activity decreases in old or heated honeys. On the other hand, α-amylase is used in starch liquelaction to produce glucose, fructose, and maltose and in brewing, baking, textile, paper, detergent, and sugar industries. There are few report about α-amylase in honey species, although this enzyme is beneficial to industrial use. The primary goal of this investigation was to purify and characterize amylase from persimmon honey, and to compare with the characteristics of amylase from other species. Fresh pure honey from persimmon was obtained from Inoue Yohojo Bee Farm Inc. (Hyogo, Japan) and used in this study. DEAE-Toyopearl 650M, CM-Toyopearl 650M, and Toyopearl HW-55F were purchased from Tosoh Co. (Tokyo, Japan). Marker proteins for gel chromatography were obtained from Boehringer Mannheim Co. (Tokyo, Japan). Marker proteins for electrophoresis and starch from rice were from Sigma Chemical Co. (St. Louis, MO) and from Amersham Biosciences UK Ltd. (UK). Coomassie brilliant blue R-250 was from Fluka Fine Chemicals Co., Ltd. (Tokyo, Japan). Pure α-amylase from Bacillus subtilis (20 U/mg), pure β-amylase from barley (32 U/mg), starch (corn, wheat, potato, and sweet potato), and bovine serum albumin (BSA) were purchased from Wako Chemicals Co., Ltd. (Osaka, Japan). Soluble starch was from Nacalai tesque Inc. (Kyoto, Japan). Neo. amylase test was purchased from Daiichi pure chemicals Co., Ltd. (Tokyo, Japan). Other chemicals were of analytical grade. α-Amylase activity was measured using blue starch as substrate. A 0.02 ml of honey sample solution was mixed with 0.784 ml of substrate solution, and then incubated at 37°C for 30 min. After the reaction was stopped by the addition of 0.196 ml of 0.5 M NaOH, the suspension was centrifuged at 12,000 rpm for 5 min. The supernatants were measured by reading the absorbance at 620 nm. One enzyme unit was defined as the activity (IU/L): one unit (IU/L) = 1.85 × (Somogyi unit/dl). Distilled water was used as negative control. Protein concentration was measured as the method of Lowry et al. using BSA as standard protein. Molecular weight of the purified enzyme was estimated using Toyopearl HW-55F (1.5 × 75 cm) gel filtration. Ferritin (450 kDa), catalase (240 kDa), aldolase (158 kDa), and albumin (68 kDa) were used as the standard marker proteins for gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed by the method of Laemmli using 10% gel. Myosin (205 kDa), β-galactosidase (116 kDa), phosphorylase (97.4 kDa), bovine serum albumin (66 kDa), ovalbumin (45 kDa), and carbonic anhydrase (29 kDa) were used as standard proteins. After electrophoresis, the gel was stained with Coomassie brilliant blue R-250 and destained with 25% ethanol and 7.5% acetic acid. TLC was performed to investigate the reaction products of the purified amylase. Ten microliters of enzyme solution (pure α-amylase from Bacillus subtilis : 0.2 U/ml; pure β-amylase from barley: 0.04 U/ml; purified amylase from persimmon honey: 0.3 IU/ml) was incubated with 17 μl of 2% unmodified starch (from rice and sweet potato), 21 μl of 0.2 M sodium acetate buffer (pH 5.0), and 20 μl of 0.5 M NaCl. After at 40°C for 1 h, a 5 μl aliquot of each reaction mixture was loaded on a precoated K6F silica gel 60Å plate (size: 5 × 10 cm; layer thickness: 250 μm: Whatman International Ltd Maidstone England, UK). At the same time, 2% maltose and 1% unmodified starch (from rice and sweet potato) were included as controls. The hydrolysates were developed with butanol, ethanol, and water (5:3:2). The plates were sprayed with sulfuric acid-methanol (1:3) solution and then heated it in an oven at 100°C for 30 min to detect the distribution of sugars. Pure honey from persimmon was dialyzed to remove a large amount of free sugars against distilled water at 4°C for 3 days by changing the water once a day. The dialysate was centrifuged at 50,000 × g for 1 h, and the supernatants were pooled and then freeze-dried. The dried sample (400 mg) was dissolved in 40 ml of 10 mM sodium phosphate buffer (pH 7.0). The enzyme solution was applied to a DEAE-Toyopearl 650M column (1.0 × 5.0 cm) previously equilibrated with the same buffer. The enzyme was not absorbed in the column. Next, the active fractions were collected, and were applied to a CM-Toyopearl 650M column (1.0 × 5.0 cm) previously equilibrated with the same buffer. Unfortunately, the enzyme was also not absorbed in this column. The active fractions were collected and concentrated to 0.5 ml using ultrafree-MC (10,000 NMWL Filter Unit: Millipore Co., USA). The concentrated enzyme solution was loaded on a Toyopearl HW-55F column (1.5 × 70 cm) which has been equilibrated with the same buffer, and the enzyme was eluted with the same buffer. Fractions of 3 ml were collected at a flow rate of 0.3 ml/min. This solution was separated into two protein fractions. The purified enzyme was stored at −85°C until used in the following experiments. The purification procedures are summarized in, Finally, α-amylase was purified up to 5.4-fold with a recovery rate of 46.8% as compared with crude extract. The molecular weight of the purified enzyme was estimated about 58 kDa by Toyopearl HW-55F (1.5 × 75 cm) gel filtration (data not shown). According to SDS-PAGE, the purified enzyme gave a single protein band of molecular weight about 58 kDa (). Babacan and Rand purified amylase from commercially available honey using ultrafiltration with a Hollow Fiber Cartridge Adapter System Model DH4 (Amicon Co., USA), ultracentrifugation, gel filtration, and ion-exchange chromatography. As a result, the amylase was purified up to 531.3-fold with a recovery rate of 3.9% in comparison to crude enzyme. The partial purified enzyme showed three protein bands by SDS-PAGE using 10% gel: the major band with 57 kDa and faint traces of two smaller component bands. Noman and others purified α-amylase from post-harvest Pachyrhizus erosus L. tuber by DEAE- and CM-Cellulose chromatographies. This enzyme was not absorbed in DEAE-Cellulose column, but was absorbed in CM-Cellulose column. These purification procedures yielded a pure amylase with 22.8% and the purity of the enzyme was 110-fold to crude enzyme. The molecular weight of the enzyme was estimated to 40 kDa. Tsvetkov and Emanuilova reported the purification and characterization of heat stable extracellular α-amylase from Bacillus brevis, Purification achieved was 8.1-fold from the crude extract with a yield of 30%. This had a molecular weight of about 58 kDa. Moreover, Ivanova and others were purified extracellular α-amylase having the molecular weight of 58 kDa produced by the Bacillus licheniformis, These values about molecular weight were similar to that from persimmon honey. On the other hand, Paquet and others purified the extracellular α-amylase from Clostridium acetobutylicum ATCC 824 using Mono Q ion-exchange chromatography and Superose 12 gel chromatography. Purification was 22.2-fold from crude extract with a yield of 23.2%. The purified enzyme showed the molecular weight about 84 kDa using SDS-PAGE. This value was similar to that of the extracellular enzyme from Streptococcus bovis JB1. The influence of pH on enzymatic activity and stability is shown in A. The α-amylase from persimmon honey showed optimal activity from 6.0 to 7.0. This value was generally similar to those of B. brevis (pH 5.0 to 9.0), C. acetobutylicum ATCC 824 (pH 5.6), S. bovis JB1 (pH 5.0 to 6.0), and B. licheniformis (pH 6.0 to 6.5). The enzyme was most stable at pH 5.0 to 6.0, however it suddenly unstable when the pH was lower than 5.0 or higher than 7.0. This tendency was similar to that of S. bovis JB1 (pH 5.5 to 8.5), but was fairly different from those of C. acetobutylicum ATCC 824 (pH 3.0 to 5.5) and B. licheniformis (pH 6.5 to 8.0). The effect of temperature on enzymatic activity and stability is shown in B. The enzyme had a temperature optimum at 40°C and a stability below 40°C. Babacan and Rand reported that amylase from commercially available honey was optimal at pH 4.6 to 5.3 and at 55°C. The pH stability of this enzyme ranged from 7.0–8.0. These results indicate that optimal pH of amylase from persimmon honey was similar to that from commercially available honey, but optimal temperature was fairly different. Noman and others reported that α-amylase from P. erosus L. tuber exhibited optimum activity at pH 7.3 and at 37°C. This enzyme was stable between pH 6.0 and 8.0 for 24 h incubation at 4°C. The enzymatic activity decreased gradually at acidic pH or alkaline pH. Effects of metal ions and chemicals such as SH-blocking reagents at a final concentration of 1.0 mM each on the purified enzyme were determined under the standard assay and the results were indicated as relative activity. As a result, Mn 2+ and PCMB and DTNB one of the sulfhydryl reagents strongly activated the enzymatic activity (). The enzyme was slightly activated by Na+, Ca 2+, and Co 2+, On the other hand, Ba 2+, Cu 2+, Zn 2+, and glutathione had a slight inhibitory effects (about 10-57%) on the enzymatic activity. In particular, the enzyme strongly inhibited by Fe 3+, Hg 2+, CH 2 ICOOH. Among these chemicals Mg 2+ completely inhibited the enzyme activity at a final concentration of 1.0 mM. Babacan and Rand investigated the effects of various metal ions on amylase from commercially available honey. The enzyme was inhibited by Cu+, Mg 2+, and Hg 2+, while Ca 2+, Mn 2+, and Zn 2+ did not affect in this enzymatic activity. Noman and others measured enzymatic activity of amylase from P. erosus L. tuber against inhibition by different concentration of metal ions and chelating reagent. Most of ions, except for Na+, Ca 2+, Fe 2+, and Mn 2+, strongly inhibited the enzymatic activity. The enzymatic activity was completely inhibited by addition of 100 mM EDTA. It was suggested that this amylase required metal ions for revelation of the activity. On the other hand, Ca 2+ at a final concentration of 100 mM drastically enhanced the activity, suggesting the requirement of calcium for appearance of the activity and stability of the enzyme. From these results indicated that the inhibitory effects of other divalent cations might be due to the competition for calcium binding site while monovalent cations and Mg 2+ might be poor competitors for calcium binding. Savchenko and others reported that calcium is required for α-amylase secretion and synthesis in Pyrococcus furiosus, Ranwala and Miller reported that Hg 2+ and Ag+ at 2.0 mM completely inhibited the enzyme. Shaw and Ou-Lee reported α-amylase strongly inhibited by Cu 2+ and moderately by Li+. It was reported that α-amylase from B. brevis was inhibited by Mg 2+, Co 2+, Cu 2+, Ag+, and PMSF. Paquet and others reported that α-amylase from C. acetobutylicum ATCC 824 exhibited a slightly inhibition by Fe 3+, Fe 2+, Co 2+, Mn 2+, Zn 2+, and Pb 2+ at a final concentration of 1 mM (less than 35%) and totally inhibited by sulfhydryl oxidant metals such as Cu 2+, Ag+, and Hg 2+, Freer reported that α-amylase from S. bovis JB1 inhibited by Mn 2+ (final concentration of 1.0 mM) and EDTA (10 mM) about 19 and 11%, respectively. This enzyme also moderately inhibited by Hg 2+ about 19% and by PCMB about 88% at a final concentration of 1.0 mM each. In the same year, Ivanova and others reported that α-amylase from B. licheniformis was strongly inhibited by N-bromosuccinimide and EDTA, and the stability against temperature depended on the existence of Ca 2+, Kinetic parameters of purified amylase from persimmon honey for starch as substrate were measured at optimal conditions (pH 6.0 and 40°C). This enzyme showed Michaelis-type kinetics when hydrolyzing starch. As calculated from Lineweaver-Burk plots, apparent K m and Vmax values were 2.81 mg and 0.532 (IU/L), respectively. There are many literatures about K m values of α-amylase as follows: 0.72 mg/ml (commercially available honey), 0.8 mg/ml (yeast Lipomyces kononenkoae ), 0.9 mg/ml ( B. licheniformis ), 0.88 mg/ml ( S. bovis ), 3.6 mg/ml ( C. acetobutylicum ATCC 824), 0.8 mg/ml ( B. brevis 174), respectively. Noman and others reported K m and Vmax values were 0.29% and 0.37 μM/min/mg protein, respectively, for starch as substrate. Moreover, Abe and others also reported the same value in two allozymes from S. oryzae, however, Baker reported about double one in amylase extract from Rhyzopertha dominica, Using several raw starches such as potato, sweet potato, wheat, and rice, soluble starch, polysaccharides such as amylose and amylopectin, substrate specificity of persimmon honey were investigated. As a result, amylose, high molecular weight substrate containing a large amount of α-1,4-linkage, was good substrate for this enzyme in comparison to soluble starch (). With increasing percentage of α-1,6-linkages and decreasing percentage of α-1,4-linkages in the substrate, the rate of hydrolysis of polymeric substrate decreased. Among these starches tested, starches from potato and sweet potato were good substrates, however the rate of hydrolysis did not reach to that of soluble starch. The relative activities of starches were as follows in the order: potato > sweet potato > wheat > rice. These tendencies of hydrolytic rate were similar to those of α-amylase from P. erosus L. tuber. Paquet and others studied the substrate specificity of α-amylase from C. acetobutylicum ATCC 824. As a result, amylose and amylopectin were the best substrates. The enzymatic activity increased from maltotriose to maltoheptaose, suggesting that the activity was higher in high molecular weight substrates than in low molecular weight. Freer investigated the substrate specificities of α-amylase from S. bovis JB1 using starches from potato and corn and polysaccharides such as amylose and amylopectin. The relative activities of this enzyme were higher in the following order: soluble corn starch > soluble potato starch = potato amylose (type III) > potato amylopectin > corn amylopectin. TLC analysis was performed to easily detect the enzymatic reaction products of purified amylase from persimmon honey and to identify type α- or β-amylase. α-Amylase from B. subtilis and α-amylase from Barley were used for comparison. As a result, α-amylase from Barley produced only maltose from rice starch (D). On the other hand, α-amylase from B. subtilis produced a large number of intermediate products (C). Purified amylase from persimmon honey not only produced maltose, but other intermediate products: this result also bore a striking resemblance to that from α-amylase from B. subtilis, In other words, purified enzyme from persimmon honey was an type α-amylase. On the other hand, corn starch was also degradated in the same manner. The results were shown in that was similar to those in rice starch. It suggests purified amylase from persimmon honey split the interior α-1,4-glycosidic bonds in a random manner. The α-amylase from pure persimmon honey was purified by some chromatographies and then was characterized. This enzyme was an type α-amylase that split the interior α-1,4-glycosidic bonds in a random manner. Table 1 Summary of purification of α-amylase from persimmon honey


Fraction	Volume	Total protein	Total activity	Specific activity	Yield	Purification
Crude extract	40.0	26.5	384.7	14.5	100	1.0
DEAE-Toyopearl 650M	64.0	18.1	301.9	16.7	78.5	1.2
CM-Toyopearl 650M	74.0	17.5	294.5	16.8	76.6	1.2
Toyopearl HW-55F	8.7	2.3	180.1	78.3	46.8	5.4

Table 2 Effects of metal ions and chemicals on persimmon honey α-amylase activity


Reagents	Relative activity
None	100
NaCl	109.7
KCl	102.8
BaCl 2	43.1
CaCl 2	111.1
CoCl 2	108.3
CuSO 4	90.3
HgCl 2	5.6
MgCl 2	0.0
MnCl 2	141.7
ZnCl 2	90.3
FeCl 3	4.2
EDTA-2Na	100
CH 2 ICOOH	4.2
PCMB	123.6
DTNB	213.9
Glutathione	79.2
PCMB: p -chloromercuribenzoic acid; DTNB: 5,5′-dithiobis(2-nitrobenzoic acid).

Table 3 Substrate specificity of α-amylase from persimmon honey


Substrate	Relative activity
Starch, soluble	100
Amylose	97.2
Amylopectin	70.5
Starch, potato	94.6
Starch, sweet potato	92.7
Starch, wheat	80.4
Starch, rice	75.9

ul> González Paramás, A.M., Gómez Báres, J.A., Garcia-Villanova, R.J., Rivas Palá, T., Ardunuy Albajar, R. and Sánchez, Sánchez, J.2000, Geographical discrimination of honeys by using mineral composition and common chemical quality parameters,J. Sci. Food Agric., 80: 157 – 165,,, Ortiz Valbuena, A. and Fernandez Maeso, M.C.1996, ” Subra Muñoz dela Torre, E. Principales características de la miel de La Alcarria “. In Investigación Agraria en Castilla la Mancha; Consejería de Agricultura y Medio Ambiente de Castilla la Mancha, 94 Spain : Castilla la Mancha, Conforti, P.A., Lupano, C.E., Malacalza, N.H., Arias, V. and Castells, C.B.2006, Crystallization of honey at –20°C, Inter.J. Food Prop., 9: 99 – 107,,, Ohashi, K., Natori, S. and Kubo, T.1999, Expression of amylase and glucose oxidase in the hypopharyngeal gland with an age-dependent role change of the worker honeybee ( Apis mellifera L.), Eur.J. Biochem., 265: 127 – 133,,, Crueger, W. and Crueger, A.1990, Biotechnology: a textbook of industrial microbiology, Edited by: Brock, T.D.191 – 199, Sunderland, IL,, USA : Sinauer Associate Inc, Babacan, S. and Rand, A.G.2005, Purification of amylase from honey,J. Food Sci., 70: C413 – 418,,, Babacan, S. and Rand, A.G.2007, Characterization of honey amylase,J. Food Sci., 72: C50 – 55,,, Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J.1951, Protein measurement with the Folin phenol reagent,J. Biol. Chem., 193: 265 – 275,,,, Laemmli, U.K.1970, Cleavage of structural protein during the assembly of the head of bacteriophage T4, Nature, 227: 680 – 685,,,, Noman, A.S.M., Hoque, M.A., Sen, P.K. and Karim, M.R.2006, Purification some properties of α-amylase from post-harvest Pachyrhizus erosus L. tuber, Food Chemistry, 99, 444–449.,, Tsvetkov, V.T. and Emanuilova, E.I.1989, Purification and properties of heat stable α-amylase from Bacillus brevis, Appl. Microbiol. Biotechnol., 31: 246 – 248,,, Ivanova, V.N., Dobreva, E.P. and Emanuilova, E.I.1993, Purification and characterization of a thermostable alpha-amylase from Bacillus licheniformis,J. Biotechnol, 28: 277 – 289,,, Paquet, V., Croux, C., Goma, G. and Soucaille, P.1991, Purification and characterization of the extracellular α-amylase from Clostridium acetobutylicum ATCC 824, Appl. Environ. Microbiol., 57: 212 – 218,,,, Freer, S.N.1993, Purification and characterization of the extracellular α-amylase from Streptococcus bovis JB1, Appl. Environ. Microbiol., 59: 1398 – 1402,,,, Savchenko, A., Vielle, C., Kang, S. and Zeikus, G.2002, Pyrococcus furiosus α-amylase is stabilized by calcium and zinc, Biochemistry, 41: 6193 – 6201,,,, Ranwala, A.P. and Miller, W.B.2000, Purification and characterization of an endoamylase from tulip ( Tulipa gesneriana ) bulbs, Physiologia Plantarum, 109: 388,, Shaw, J.F. and Ou-Lee, T.M.1984, Simultaneous purification of α-amylase β-amylase from germinated rice seeds and some factors affecting activities of the purified enzyme, Bot. Bull. Acad. Sin., 25: 197 – 204, Prieto, J.A., Bort, B.R., Martinez, J., Randez-Gil, F., Buesa, C. and Sanz, P.1995, Purification and characterization of new α-amylase of intermediate thermal stability from the yeast Lipomyces kononenkoae, Biochem. Cell. Biol., 73: 41 – 49,,,, Abe, R., Chib, A.Y. and Nakajima, T.2002, Characterization of the functional module responsible for the low temperature optimum of rice α-amylase(Amy 3E), Biologia Bratislava, 57(Suppl.11): 197 – 202, Baker, J.E.1991, Purification and partial characterization of α-amylase allozymes from the lesser grain borer Rhyzopertha dominica, Insect Biochem., 21: 303 – 311,,

: Alpha-Amylase from Persimmon Honey: Purification and Characterization

What is the dilution of amylase?

Prepare amylase solution by adding 0.1 g of amylase to 100 mL of water.

What makes the strongest moonshine?

Buffalo Trace White Dog Mash – This moonshine is considered a #1 mash. It is corn, rye, and malted barley moonshine with a proof of 125 or an ABV of 62.5%. Dark Corner Distillery Moonshine This moonshine is brewed in partnership with the legendary NASCAR driver Billy Elliot. It is a corn whiskey with a proof of 100 or an ABV of 50%. This moonshine is branded as the ‘World’s Best Moonshine’.

What makes moonshine taste better?

How Commercial Brewers Flavor Spirits – Commercially produced spirits are usually stored in wooden casks or to enhance the taste of the spirits. Some commercial brewers allow their products to sit for a minimum of one year where others may choose to age their products for many years which increase both the taste and price of the product.

The type of wood you use for aging your spirits can also affect its taste. For instance, scotch whiskey is usually kept in sherry cask to combine the different flavors of sherry, sugars present in the wood as well as the distinct flavor of the whiskey. The resulting product is quite unique and more flavorful.

If you will take a look at commercial whiskey products, you will find that the age is about three to eight years and even twelve. You may also begin to wonder why your spirit soaked with oak chips to achieve aging takes only a few days instead of years.

The answer greatly depends on the surface area of the oak wood chips that come in contact with a certain amount of spirit. Essentially, the surface area of the oak chips is greater than that of the barrel which makes the exchange of flavor more rapid. Using Fresh Wood Chips Is Ideal For Enhancing Taste New wood can age spirit more than old wood does.

It is recommended to use fresh wood chips rather than the old one because your spirit can have a woody taste if the chips are very old and this can negatively affect the flavor of your finished product Sweet Bourbon Essence Can Also Enhance Your Flavor To intensify the taste, even more, you can filter it in a muslin cloth and include the sweet bourbon essence into it.

After this, you can proceed with bottling the product into 700g bottles which should be stored in a cool dark place for one month or more.
With this, you can achieve bourbon that is smooth and mellow to drink.
Avoid Using a Carbon Filter You must not filter it using a carbon filter to remove wood chips because it will only remove much of its flavor which makes you lose all your efforts.

Using a muslin or tea towel is highly recommended in this case so that you can retain all the flavors that you would like to keep. You may also try a coffee filter which may take slowly compared to muslin, but it is really quite effective too. Adding sugar can also adjust the taste of your moonshine To add final touches, you can add 5 teaspoons of caramelized raw or white sugar per liter of your spirit.

Why add amylase?

Amylases are enzymes that convert starch to sugar. Bakers add amylase to bread dough to supplement the small amount found naturally in wheat flour. The sugar that the amylases produce serves as food for the fermenting yeast and also makes for better-tasting, better-toasting bread.

How long does it take for amylase to work?

Procedure – SAFETY: All solutions once made up are low hazard. Wear eye protection, as iodine may irritate eyes. Preparation a Check the speed of the reaction with the suggested volumes of reactants to be used – 2 cm 3 of starch: 2 cm 3 of amylase: 1 cm 3 of buffer at pH 6.

Ideally the reaction should take about 60 seconds at this pH: this is the usual optimum for amylase (see note 1).
If the reaction is too fast, either reduce the enzyme volume or increase the starch volume.
If the reaction is too slow, increase the enzyme volume or concentration or reduce the starch volume or concentration.

Investigation b Place single drops of iodine solution in rows on the tile. c Label a test tube with the pH to be tested. d Use the syringe to place 2 cm 3 of amylase into the test tube. e Add 1 cm 3 of buffer solution to the test tube using a syringe. f Use another syringe to add 2 cm 3 of starch to the amylase/ buffer solution, start the stop clock and leave it on throughout the test.

Mix using a plastic pipette.
G After 10 seconds, use the plastic pipette to place one drop of the mixture on the first drop of iodine.
The iodine solution should turn blue-black.
If the iodine solution remains orange the reaction is going too fast and the starch has already been broken down.
Squirt the rest of the solution in the pipette back into the test tube.

h Wait another 10 seconds. Then remove a second drop of the mixture to add to the next drop of iodine. i Repeat step h until the iodine solution and the amylase/ buffer/ starch mixture remain orange. j You could prepare a control drop for comparison with the test drops.

What is amylase in moonshine mash?

$ 4.00 A mylase enzyme is a naturally occurring enzyme that is used to aid in the conversion of starches to sugars in the all grain brewing process. It is especially helpful in lighter beers with delicate malt character.35 in stock

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How long does it take for amylase to rise?

Using lipase and amylase in combination – Prior studies have clearly shown that using lipase and amylase in combination does not improve their diagnostic accuracy, In a very elegant retrospective study by Corsetti et al. the performance of lipase and amylase alone and in combination was studied in patients for whom both these tests were ordered.

This study confirmed that simply using both tests together has no advantage over using lipase alone.
It was, however, found in the study using logistic regression analysis that use of a statistical model based on logistic regression discriminant function lead to a statistically significant improvement in performance of both tests together over the use of lipase alone.

In order to apply this approach clinically, a discriminant rule and analytic techniques, which are specific to the population under study, need to be developed which is not always practically feasible. Thus only if a bivariate approach is used, the combination offers meaningful advantage over use of lipase alone.

However, due to the difficulties associated with implementing this approach mentioned above, the use of bivariate approach is not routinely possible.
Also, as mentioned before, lipase starts to increase within 4-8 hours of onset of acute pancreatitis and peaks at 24 hours.
Amylase on the other hand, starts to rise after 6- 24 hours and peaks at 48 hours.

Lipase stays elevated for 8-14 days, much longer than amylase, which stays elevated for 5-7 days, Therefore, it is clear that from the point of view of diagnosing AP in patients who present very late in the course of the disease, lipase is clearly superior to amylase.

Although amylase tends to increase slightly earlier than lipase and peaks slightly earlier too, the difference appears to be not significant enough to affect sensitivity early in the course of the disease. Thus, routine measurement of both lipase and amylase simultaneously for the diagnosis of acute pancreatitis is likely to add additional cost without any meaningful advantage and hence should be avoided.

As an example, in a 600-bedded community hospital in New Jersey, the approximate annual cost of all the amylase assays to the provider was roughly 90,000 USD. (Personal communication, Monmouth Medical Center Biochemistry laboratory, January 2014) Using this as a guide, the total annual cost of amylase assays across the United States is likely to be significant.

How is amylase used in brewing?

The Oxford Companion to Beer Definition of alpha amylase The Oxford Companion to Beer definition of Alpha Amylase is a major mash enzyme of critical concern to brewers in their production of fermentable wort. It digests starch, a large polymer of glucose, into smaller units, exposing it to further digestion by beta amylase.

Together these two amylases produce the spectrum of wort sugars essential in the production of a beer.
Alpha amylase is an endo enzyme mainly digesting the alpha 1–4 bonds of starch at points within the chain, not at the ends.
To focus on the use of alpha amylase in brewing, it is necessary to look at the needs of a successful mash, in particular the spectrum of sugars required in the final wort.

Ideally these should be a suitable balance of simple fermentable sugars—glucose, maltose, and maltotriose—and larger unfermentable dextrins roughly in a 3:1 proportion. Unlike wine, where virtually all of the sugars are fermented, beer is distinct in having residual sugars to provide sweetness, body, and mouthfeel.

Dextrins contribute strongly to this and give beer a major part of its character. See, A starch molecule is, in essence, a group of glucose molecules linked together. Enzymes break those links. Alpha amylase contributes to the digestion of starch by breaking internal bonds between glucose molecules. As a result it opens up the starch molecule, breaking it into a range of intermediate sizes.

Beta amylase further digests these intermediate molecules mostly into maltose—a sugar of two glucose units—but also to glucose itself and to the three-glucose molecule maltotriose. The major limitation to this digestion is the side bonds of starch amylopectin, which are not digested by either alpha or beta amylase.

The parts of the starch molecule containing these side bonds form the basis of the important unfermentable dextrins produced by mashing. The alpha amylase used in the mash comes from the malt, where it is entirely produced in the aleurone layer during malting. See, In the barley seed, its mobilization is induced in order to digest the starch reserves in the endosperm and provide nutrients for the growing seed.

The maltster stops this at the point when enzyme levels are maximal and are preserved in the dry grain ready for use in mashing. Levels of alpha amylase are typically high in pale malt but are virtually zero in roasted malt due to heat degradation. Levels vary according to malt variety and to malting conditions.

Generally six-row barleys have higher levels than two-row barleys due to grains being smaller with less endosperm in proportion to aleurone. Alpha amylase is not restricted to barley but occurs in most organisms from bacteria to humans. Salivary amylase, ptyalin, is a well-known amylase that initiates starch digestion in the mouth of mammals.

Enzymes tend to have specific temperature and pH ranges at which they will be active—this range is referred to as “optima.” Alpha amylase has a significantly different temperature and pH optima than beta amylase. For alpha amylase the temperature optima is higher at around 70°C compared to 60°C–65°C for beta amylase as the enzyme may be stabilized by calcium ions.

The pH optima of alpha amylase is also higher at 5.3–5.7 compared to 5.1–5.3 for beta amylase. These differences can result in different wort sugar profiles from mashes conducted at different temperatures and are one means of varying beer character by control of mash conditions. In traditional breweries, all the enzymes needed for brewing are contained within the natural ingredients out of which the beer is made.

However, exogenous alpha amylase is available in purified form from enzyme suppliers and may have different properties according to its origin. These are widely used in the production of “light beers.” See, The most relevant differences for brewers are thermal and pH tolerances.

Heat-labile alpha amylases can be used to supplement malt enzymes or to digest adjunct starch. Because of their heat sensitivity, they will be denatured by pasteurization. Heat-tolerant alpha amylases will, however, survive into the final beer, which may become sweeter over time if residual dextrins are available for digestion into flavor-active sugars.

Commercial alpha amylases may also cause problems if they are impure and contain beta amylase and proteases or if they contain toxins from their bacterial or fungal growth. However, their use is growing in many food industries and will continue to have application in brewing, particularly if novel ingredients are sourced for future beers.

How do you make 1% amylase?

Prepare the stock solution of 1% amylase by dissolving 2.0 grams of fungal amylase in 200 ml of pH 7 buffer. Refrigerate this solution if it is to be stored over night. The amylase powder dissolves slowly in the buffer so allow amply time for a solution to form.

What pH level does amylase work best at?

Abstract – Purified human pancreatic alpha-amylase (alpha-1,4-glucan 4-glucano-hydrolase, EC 3.2.1.1) was found to be stable over a wide range of pH values (5.0 to 10.5) with an optimal pH for the enzymatic activity of 7.0. The Michaelis constant of the enzyme at optimal pH and assay conditions was found to be 2.51 mg per ml for soluble starch.

Halide ions were required for the activity of the enzyme whereas sulfate and nitrate were not.
The order of effectiveness of activation was found to be: Cl- greater than Br- greater than I- greater than F-.
Calcium and magnesium were activators at concentrations of 0.001M and 0.005M, respectively, but exhibited inhibitory effects at concentrations higher than 0.005M.

At 0.01M ethylenediamine tetraacetic acid (EDTA) concentration the enzymatic activity upon seven min incubation, was inhibited up to 96%. The inhibition of EDTA and calcium could be reversed upon addition of calcium and EDTA, respectively.

At what temperature does amylase work best?

Effect of Temperature on Enzyme Activity – Several authors have reported that the majority of the bacterial amylases have an optimum temperature in range of 30–100 o C ( 9, 12 ). The effect of temperature on the activity of α-amylase was found to be maximum at 37 o C ( Figure 3 ) when compared to 35 o C as reported by Vidyalakshmi et al,, 2009 ( 24 ). Effect of temperature on the activity of the enzyme.

Does boiling destroy amylase?

Does boiling water deactivate malt enzymes? Yes, heating to boiling temperature will destroy amylase. Depending on the ratio, the goal of that recipe may be to destroy the enzymes, to gel the starch, or to help the enzymes be most effective. It’s not uncommon for particularly old and traditional recipes to use a combination of boiling water, ice-cold water, and room-temperature ingredients to reach a particular temperature, as the ratio of inputs will determine the final temperature pretty accurately without a need for a thermometer.

What is the best way to get amylase?

Digestive enzymes play a key role in breaking down the food you eat. These proteins speed up chemical reactions that turn nutrients into substances that your digestive tract can absorb. Your saliva has digestive enzymes in it. Some of your organs, including your pancreas, gallbladder, and liver, also release them.

Amylase breaks down carbs and starches Protease works on proteins Lipase handles fats

Fruits, vegetables, and other foods have natural digestive enzymes. Eating them can improve your digestion.

Honey, especially the raw kind, has amylase and protease.Mangoes and bananas have amylase, which also helps the fruit to ripen.Papaya has a type of protease called papain. Avocados have the digestive enzyme lipase.Sauerkraut, or fermented cabbage, picks up digestive enzymes during the fermentation process.

If your body doesn’t make enough digestive enzymes, it can’t digest food well. That can mean stomachaches, diarrhea, gas, or other painful symptoms. Some digestive disorders prevent your body from making enough enzymes, such as: Lactose intolerance,

This is when your small intestine doesn’t make enough of the enzyme lactase, which breaks down the natural sugar in milk called lactose. With a shortage of lactase, lactose in dairy products that you eat travels straight to your colon instead of getting absorbed into your body. It then combines with bacteria and causes uncomfortable stomach symptoms.

There are three kinds of lactose intolerance: Primary. You are born with a gene that makes you lactose intolerant. The gene is most common in people of African, Asian, or Hispanic background. Your lactase levels drop suddenly as a child. Then you’re no longer able to digest dairy as easily.

This is the most common type of lactose intolerance. Secondary. Your small intestine makes less lactase after an illness, injury, or surgery. It can also be a symptom of both celiac disease and Crohn’s disease, Congenital or developmental. From the time you are born, your body doesn’t make lactase. This is rare.

You have to inherit the gene for this from both your mother and father. People with lactose intolerance need to move their bowels a lot and have gas and bloating after eating or drinking dairy products like milk and ice cream, Some people can manage symptoms by eating smaller amounts of dairy.

Pancreatitis, or inflammation of the pancreas Pancreatic cancer, which starts in the tissues of your pancreas Cystic fibrosis, a genetic condition that damages the lungs, digestive system, and other organs

To treat EPI, your doctor may suggest lifestyle changes, such as:

If you smoke, quitAvoid drinking alcohol Eat a low-fat dietTake vitamin and mineral pills

Prescription medicine may also improve your symptoms. You may have noticed digestive enzyme pills, powders, and liquids on the aisles of pharmacies or health and nutrition stores. These supplements may ease digestive disorder symptoms. Your age, weight, and other things determine the right dose.

But remember, over-the-counter enzyme supplements are not regulated by the FDA the same way as prescription medicines.
The makers of these products do not have to prove that they are effective.
Always talk to your doctor before trying any kind of supplement.
More research is needed to study how safe they are and how well they work.

But over-the-counter lactase supplements help many people with lactose intolerance, and there is a supplement that seems to help people digest the sugars that are in beans. Experts do not recommend lactase supplements for children under age 4. Also, talk to your doctor about the pros and cons if you’re pregnant or breastfeeding,

How do you dissolve amylase powder?

Prepare amylase solution by adding 0.1 g of amylase to 100 mL of water. Stir until the amylae dissolves.

How do you increase amylase production?

12. Ginger – Ginger has been a part of cooking and traditional medicine for thousands of years. Some of ginger’s impressive health benefits may be attributed to its digestive enzymes. Ginger contains the protease zingibain, which digests proteins into their building blocks.

Zingibain is used commercially to make ginger milk curd, a popular Chinese dessert ( 61 ).
Unlike other proteases, it’s not often used to tenderize meats, as it has a short shelf life ( 62 ).
Food sitting in the stomach for too long is often thought to be the cause of indigestion.
Studies in healthy adults and those with indigestion show that ginger helped food move faster through the stomach by promoting contractions ( 63, 64 ).

Animal studies have also shown that spices, including ginger, helped increase the body’s own production of digestive enzymes like amylases and lipases ( 65 ). What’s more, ginger appears to be a promising treatment for nausea and vomiting ( 66 ). Summary Ginger contains the digestive enzyme zingibain, which is a protease.

How do you make 1% amylase solution?

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