Glucosidase has roots running back to the dawn of biochemistry. Researchers in the late 1800s began to see the importance of enzymes in breaking down complex molecules. In the decades that followed, glucosidase emerged as a key factor in processing carbohydrates. Teams in Germany and France charted its activity in yeast and animal tissue, finding that it carved up long chains of sugars into pieces the body could use. As chromatography and protein purification improved, the world got a much clearer picture of what this enzyme could do. Research labs published detailed reports through the twentieth century, laying out a framework for today’s producers and medical experts. Through experience in both academic and industrial settings, I've seen how this ongoing discovery fuels the larger biotech engine. Without that early legwork, we wouldn't have the diagnostic kits or therapeutic products we rely on now.
Glucosidase covers a wide field, but most people encounter it through two main products: alpha-glucosidase and beta-glucosidase. Both types tackle complex sugars, though they cut them in different places. Commercial labs supply powders, crystalline forms, or stabilized liquid suspensions. Standard presentations in white or pale cream color keep things simple for formulators and medical personnel alike. My own time in labs hammered home the headaches that come from mixing with impure reagents, so I value the tight controls today’s suppliers maintain. Production batches roll out only after inspection for activity, purity, and safety—never trust an unknown source with something headed for a clinical application or a fermentation tank.
Glucosidase feels like a fine powder—almost chalky to the touch—though you’ll find some liquid forms for rapid processing. Chemically, the enzyme boasts a protein backbone with a clever active site that homes in on sugar rings. Its specific molecular weight depends on the exact form, but alpha-glucosidase from yeast hovers around 100-110 kilodaltons. The isoelectric point sits between pH 4.5 and 5.5, with the enzyme showing best activity in mildly acidic conditions. It dissolves readily in buffered solutions, but heat or changes in pH can destroy it. I remember one batch ruined after a colleague left it on a lab bench in the sun—enzymes do not forgive mistakes in storage or handling.
Product specs for glucosidase focus on activity units, source organism, purity level, stabilizing agents, recommended storage, and expiration date. Activity commonly appears in International Units (IU) per milligram. Companies source this protein from Aspergillus, Saccharomyces, and porcine pancreas, among others, each conferring unique subtle differences that show up in side-by-side tests. Labels also list potential allergens, as regulatory agencies demand full transparency. Instrument calibration and lot-to-lot consistency stand among the reasons top biolabs can charge premium prices. I learned the hard way that ignoring detailed specs delivers inconsistent fermentation performance, so close reading pays off every time.
Extraction of glucosidase usually starts with culturing a microorganism or collecting animal pancreas, followed by lysis and a series of precipitation, centrifugation, and chromatographic purification steps. Using affinity columns tailored for specific tags or glycan moieties trims the time and labor needed to get clean product. Microbial fermentation dominates, as it avoids animal-derived allergens and delivers high yields. Aseptic technique and constant cold chain tracking ensure no contamination wrecks months of work. The final product passes through sterile filtration and rigorous potency checks. Whether prepping a research-grade batch or an injectable formulation, strict process control makes or breaks reliability. Many top enzymes only reach market after hundreds of failed runs and bitterly-earned lessons around process scaling.
At the molecular level, glucosidase cleaves glycosidic bonds in disaccharides and polysaccharides. Substrate enters the enzyme’s binding pocket, an acidic residue protonates the glycosidic oxygen, and the bond splits with water’s help. That’s biocatalysis in its purest form. Labs often tailor glucosidase through site-directed mutagenesis to tweak pH sensitivity or salt tolerance, offering industrial partners tools that work in harsh process environments. Enzyme immobilization on silica or polymer beads makes the protein reusable in large-scale sugar conversions, such as starch processing for sweetener production. We once tried PEGylating glucosidase for medical use—a bulky modification meant to extend circulation time. Results in animal models were promising, though translating innovations like this to scalable production always brings fresh challenges.
Glucosidase earns a few alternate titles—maltase, saccharase, and amyloglucosidase mark the most common among them. Catalog listings from leading suppliers, such as Sigma-Aldrich and Novozymes, add specific tags for enzyme source, like "yeast alpha-glucosidase" or "bacterial beta-glucosidase." Some generic preparations circulate as "starch-digesting enzyme" in dietary supplements. Different language traditions keep the names flowing, yet industry still orients discussions around International Union of Biochemistry (IUB) classification codes, making conversations between research partners far less confusing. I’ve had enough headaches with mislabeled bulk shipments to appreciate defined product naming conventions.
Safe handling stems from basic principles: keep powders contained, avoid inhalation, and guard eyes and skin. Material safety data sheets flag the risk of potential respiratory sensitization, supported by rare documented cases among industrial workers. Food and pharmaceutical regulations, including those from the FDA and EFSA, demand sequence checks to avoid cross-reactivity with known allergens or pathogen markers. Commercial-grade glucosidase passes routine endotoxin testing, bioburden assessment, and sequencing for viral traces. Automated plant systems track lot numbers and operator signatures to guarantee accountability. Lab culture teaches a strong respect for consistency—shortcutting safety protocols nearly always ends in costly downtime or product recalls.
The reach of glucosidase spreads wide. Industrial starch hydrolysis for glucose syrup production soaks up plenty of enzyme. Breweries use it to trim complex sugars in mash, maximizing ethanol yield. Pharmaceutical companies depend on purified enzyme for both diagnostic kits and rare-disease drugs like miglustat or enzyme-replacement therapies for Pompe disease. Research teams test glucosidase in gut health studies, carbohydrate profiling, and food science. Dietary supplements market plant-based glucosidase as a way to tackle digestion problems, though evidence mostly comes from animal models and small clinical trials. Having advised both biotech startups and food processors, I’ve seen the enormous impact production-scale enzymes have on both nutritional and industrial outcomes.
Science never stops, and glucosidase research shows no signs of slowing. Teams across the US, Europe, and Asia search for heat-stable or pH-resistant mutants, often using directed evolution or CRISPR editing. Shotgun metagenomics of extreme-environment microorganisms regularly reveals new enzyme variants, many of which land in patent filings. Researchers chase after more potent therapies for lysosomal storage disorders, building on insights from precision medicine. Continued advances in protein crystallography and mass spectrometry tighten control over structural tweaks, pushing the envelope on both therapeutic and industrial uses. Feedback loops between bench, pilot plant, and real-world deployment make the R&D process for glucosidase a constant grind, demanding dogged persistence and creative workarounds.
Toxicity profiles for glucosidase look good when sourced and purified to pharmaceutical standards. Animal studies rarely show adverse systemic effects from oral or injectable doses, though immune responses appear in some cases, especially when the enzyme comes from non-human sources. Occupational exposure studies raise a flag over chronic inhalation risk, with sensitization patterns more common in environments lacking ventilation or protective masks. Regulatory reviews dig deep into trace contaminants such as residual DNA, host proteins, or microbial byproducts. Long-term feeding trials in rodents and livestock find little evidence of harm, cementing glucosidase’s place in food and supplement manufacturing. My time consulting for enzyme producers cemented respect for thick regulatory files, as every page tells the story of overlooked pitfalls and the price paid for missing them.
The years ahead look busy for glucosidase development. Growth in the biofuels market pushes demand for enzymes that handle non-standard feedstocks like cellulosic waste. Expanding interest in functional foods and gut microbiome research ripples out into formulators hunting for active ingredients. Pharmaceutical advances continue driving up purity benchmarks and production efficiency, while rising allergy awareness brings newer rounds of safety screening. Machine learning tools add speed to enzyme discovery pipelines, connecting computation to wet lab reality with surprising speed. For both industrial and clinical fields, the pace of change boils down to how quickly teams can bridge basic research with commercial-scale outputs. Having watched multiple waves of technological disruption hit the biotech world, I see glucosidase as primed for both big breakthroughs and the daily grind of improving what already works.
Enzymes rarely get much attention outside the science lab, but glucosidase plays a role in hundreds of clinics and pharmacies without most people knowing. This enzyme breaks down complex carbohydrates into something the body can actually use: glucose. My first encounter came during college biology, and I’ll admit the lecture made my head spin. Yet in the hospital setting later on, I started noticing how doctors used medicines relying on glucosidase inhibitors or supplements to keep patients stable, especially those struggling with blood sugar swings.
The key here is action and direct impact. In people with certain genetic conditions like Pompe disease, their bodies struggle or fail to make enough glucosidase. That means all that stored glycogen can’t turn into workable energy, leading to serious muscle and heart problems. Tenacity isn’t enough if your muscles can’t unlock their fuel. Newer treatments use a purified form of glucosidase made through recombinant technology, giving patients a fair shot at better health.
Blood sugar management comes up in every family. Whether it’s type 2 diabetes or just trouble digesting food, glucosidase steps into the spotlight. Certain diabetes medications block this enzyme in our intestines, slowing sugar spikes after meals. Instead of fast crashes and jitters, patients experience more stable energy. In clinics, this has helped lower complications and hospital visits due to uncontrollable sugar swings.
I have a friend whose father lived with type 2 diabetes for decades—meals became a balancing act. Glucosidase inhibitors gave him some freedom back. He still watched his plate, but those medications smoothed out unexpected highs after eating bread or rice. It didn’t replace lifestyle changes, but it did deliver a buffer against the rollercoaster.
Outside hospitals, manufacturers use glucosidase to produce syrups and sweeteners from starches. Companies aim for a certain sweetness level or consistency, and this enzyme does the job well. In brewing, it helps convert starches from grains into fermentable sugars, fueling yeast activity and shaping the final taste. Homebrewers and major beverage brands depend on this reliable reaction.
But it’s not just about food. Scientists use glucosidase in biofuel production, breaking down plant materials into glucose for fermentation. These advances hold promise for greener energy sources. I find the crossover fascinating—what helps a child with a genetic disease also helps run a distillery.
Costs limit access to glucosidase-based therapies. In rare diseases, treatment can soar into the hundreds of thousands each year, straining insurance and family budgets. Researchers keep searching for cost-saving production methods. More stable and affordable enzyme formulas open the door for more patients worldwide.
Education stands out as another hurdle. Many patients and even some clinicians don’t hear about enzyme replacement or new drugs until issues pile up. Outreach, patient groups, and plain-language resources help close this gap. Every time someone learns how simple enzymes affect disease and health, better choices follow—whether that’s in a lab, on a dinner table, or managing a lifelong condition.
Glucosidase usually comes up during conversations about blood sugar and gut health. Found in a few different forms—like alpha-glucosidase inhibitors or as a digestive enzyme—this substance plays a big role in breaking down carbs you eat. Doctors sometimes prescribe these medications, such as acarbose, to people with type 2 diabetes. The point? To slow down how fast the body digests complex sugars, which helps steady blood sugar instead of letting it spike after a meal.
No two bodies work the same, and doctors know that better than anyone. If you get a glucosidase prescription, the instructions usually come with it. Tablets often reach their fullest effect when you take them right before eating, or even with your first bites. Swallowing them with the meal gives the medicine a head start as those carbs start breaking down. Skipping meals means no need for the pill, since there’s nothing to slow down.
From years of watching relatives manage diabetes, I've noticed how routines build trust in the process. Following doctor’s directions—dose, timing, even what you eat—makes a real difference. Medications like acarbose and miglitol come with specific meal schedules to help the medicine do its part.
Some experience gas, bloating, or soft stools, especially in the first few weeks. That sounds uncomfortable, but the body tends to adjust. The worst thing you can do? Ignore unusual symptoms. If anything disrupts daily life—like strong abdominal pain or signs of an allergic reaction—calling a healthcare professional beats guessing every time. Taking this stuff without talking to a doctor increases risks, especially for those with digestive disorders or kidney concerns.
Pairing these medicines with the right foods makes a huge difference. Simple sugars—table sugar, for example—don’t slow down after taking glucosidase. Complex carbs (whole grains, beans, certain veggies) usually work best with these meds. If blood sugar drops too low, skip candy bars and go with glucose tablets or gels. Regular candy and sugary foods might not help as much, since the medicine keeps those sugars from breaking down fast.
Everyone’s heard the advice about fiber and steady meals. In my experience, small tweaks—like eating on a schedule, reading labels, and carrying glucose tabs—build routines that help maintain steadier energy and fewer surprises.
Glucosidase does a particular job, but it doesn’t replace lifestyle. Exercise, meal planning, stress reduction, and sleep remain essential. The Centers for Disease Control and Prevention recommends combining oral medications with healthy habits to reach the best blood sugar control.
Newer studies keep adding to what we know. Scientists from the American Diabetes Association point out that, for many, side effects drop off with time. It’s often a matter of consistency—not skipping doses, not making huge swings in diet, and checking in with your healthcare provider.
Staying in touch with your doctor keeps treatment current. Blood sugar targets change over the years and so can your medication needs. Lab tests, honest conversations, and writing down symptoms help a medical team keep things on track. While the pill itself plays a part, a team approach usually delivers better results.
Taking glucosidase isn’t about swallowing a magic solution. It works as a piece of a much bigger puzzle and teaches the value of listening—to your body, to your care team, and to the rhythms that keep health in balance.
Glucosidase drugs work by blocking enzymes that break down carbohydrates, which slows the absorption of sugar in the body. They often help people with diabetes manage blood sugar swings after meals. This sounds like a simple fix, but anything that tampers with digestion can carry baggage.
Nearly everyone who swallows a glucosidase inhibitor for the first time gets some sort of stomach trouble. The most common issues include bloating, gas, stomach cramps, and sometimes diarrhea. This happens because undigested carbs move into the colon, where bacteria feast and release gas. I remember trying acarbose with a relative who has type 2 diabetes. Lunch became a bit of a gamble. Grilled cheese followed by abdominal rumblings all afternoon isn’t fun. Don’t expect to dodge these reactions easily—the numbers back it up. Researchers have found that up to 80% of people taking acarbose report gas.
Occasionally, glucosidase inhibitors cause trouble outside the digestive tract. Some people experience skin rashes, or mild swelling. A few rare reports mention transient liver test elevations. The American Diabetes Association flags this and suggests regular liver checks for anyone on these drugs long-term, especially if people start feeling tired or notice yellowish skin.
People often brush off stomach issues as minor, but real life gets complicated if your daily routine involves work meetings or long drives. Passing gas throughout an important presentation or running to the bathroom several times a day can wear people down. People stop taking useful drugs because the embarrassment or pain outweighs the benefits.
People on glucosidase inhibitors also run a higher risk of low blood sugar when combining these meds with insulin or other diabetes pills. Most folks don’t get hypoglycemia from these inhibitors alone, because they don’t push insulin levels up. Still, adding any new medicine to a regimen leaves room for interaction tangles. Sometimes low blood sugar looks like hunger, sweating, or shakiness, which can be dangerous if unnoticed. Old friends and family warned me to keep glucose tablets or honey close by. Sucrose or candy won’t work well with this drug because its action blocks normal sugar absorption. Pure glucose gets into the bloodstream faster and sidesteps the blockage.
Doctors suggest starting with a low dose and creeping up gradually. This makes sense, as the body sometimes gets used to the extra fermentation in the gut. Diet matters, too. Cutting back on simple sugars and high-carb meals can take the edge off the turbulence. Some patients get relief by spacing out their carb intake or replacing part of their meal with protein or fat. Keeping close communication with healthcare providers lets people track patterns and tweak treatment if needed.
Some people stay the course and manage fine, while others can’t get past the side effects. Studies have shown that about a quarter of people stop glucosidase inhibitors because of gastrointestinal issues. No single answer fits everyone. It takes trial, error, and some honest talk with a trusted doctor to find what works for each body and lifestyle.
Over the years, I've seen plenty of folks collect pill bottles on their kitchen counters. It's normal these days—maybe a heart pill, something for sugar, something for nerves. For anyone with diabetes, drugs like glucosidase blockers often show up in that mix, since they keep blood sugar from spiking after meals. Seems simple until another script joins the party.
Mixing meds isn’t like tossing socks in a drawer. One story sticks in my mind: my uncle, a tough old farmer, started popping glucosidase for his blood sugar, thinking nothing of it because his doctor said it was safe. Next, his regular doc gave him something for heartburn. He ended up dizzy and weak later that week. Turns out, the new pill changed how well his glucosidase worked. Not rare, either—studies show that common stomach drugs, like antacids, can mess with glucosidase absorption. The American Diabetes Association says any change in digestion affects how much sugar winds up in your blood, which gets risky fast.
Three kinds of meds stand out. First, diabetes drugs like metformin or insulin might push glucose levels too low and stack up risks if a glucosidase blocker joins the mix. Next, antibiotics—some, like neomycin, can cause weird gut reactions and leave glucosidase working overtime or not at all. Diuretics, meant to help with swelling or blood pressure, shift your electrolyte balance, so they change how sugars and pills work in the gut. According to Cleveland Clinic, more than a third of older adults end up on five or more prescriptions, which means drug collisions are no longer rare accidents.
Healthcare folks like to preach a simple rule: don’t add new meds without talking things out. I’ve talked to neighbors who thought since their blood sugar was under control, they could swap brands or add herbal teas. Sometimes those changes were harmless; other times, they ended with ER visits. Often, the issue isn’t the drug itself—it’s how it reacts with the soup of other stuff already in a person’s body. I learned early, even over-the-counters or supplements can turn a safe combo into a headache.
Best advice comes from the people working the front lines—doctors, nurses, pharmacists. They have the charts and the know-how to spot red flags before things get messy. Keeping an updated list of meds and asking direct questions can make all the difference. If you’re seeing more than one doctor, ask for a medication review. Most local pharmacies do this, and it tends to be free. One other piece—pay attention to any new symptom after starting or switching a drug. Don’t shrug off dizziness, stomach pain, or tiredness. These often show up before anything serious happens.
Science moves fast, with new drugs popping up all the time. The best bet for anyone taking glucosidase—whether for diabetes, experimental trials, or rare conditions—is to remember pills mix like people. Some combinations play well, some clash, and the only way to stay safe is to keep the conversation open with trusted healthcare folks. That tiny bit of extra work means fewer surprises and more control over your day-to-day health.
Supplements land on shelves promising big things, often with little warning about long days ahead. Glucosidase is one of them—a digestive enzyme powering through carbohydrates in our food, making energy easier to use. It draws attention for its role in metabolic disorders, diabetes management, and rare enzyme deficiencies. Some products suggest benefits for digestive comfort, but most folks hear about it in the context of enzyme-replacement therapies or as an adjunct for people who struggle to break down complex sugars.
Doctors prescribe Glucosidase for real medical reasons, particularly for conditions like Pompe disease, where missing enzymes cause dangerous buildup of glycogen in tissues. In those cases, treatment proves life-changing. Standard clinical trials follow these therapies for at least a few years. Most people taking the enzyme replacement see improvement or stabilization of symptoms, based on years of research and patient monitoring. But these studies happen under watchful eyes, with health professionals flagging liver changes, immune reactions, or allergic symptoms.
Long-term safety for general supplement use doesn’t get the same level of oversight. Most over-the-counter versions offer much lower doses than medical versions, but no supplement keeps regulators involved the way prescriptions do. Studies on healthy people are thin and don’t track what happens over several years. In my experience, people using these supplements believe the natural source and enzyme label mean they’re safe, but 'natural' doesn’t equal harmless. Sometimes, mild side effects like upset stomach crop up. Rarely, allergic responses turn dangerous. That risk only increases when taking supplements for years, especially in people juggling diabetes, allergies, or odd medication routines.
There’s a gap in public knowledge when people grab Glucosidase on their own. Many don’t realize its real impact on blood sugar or that over-supplementing can tangle with medicines like metformin, or even mess with how the body digests meals. Regular users tell stories of digestive differences, but it’s tough to find reliable evidence showing better health after long-term casual use.
Governing agencies, such as the FDA, monitor prescription-grade products, demanding safety trials and follow-up studies, with ongoing requirements to report side effects. In contrast, supplement makers need only prove their product isn’t harmful in the short term. Industry pressure sometimes encourages more transparency, but regulation for long-term use runs weaker unless clear harm turns up.
Curiosity about Glucosidase for the long haul ought to fuel a talk with a healthcare provider, especially for folks already dealing with blood sugar swings or diagnosed health conditions. Doctors can run lab tests, keep an eye out for immune shifts, and help spot trouble early. Anyone thinking about regular, long-term use should look for products with proven track records, third-party testing, and realistic labeling. It pays to start with the lowest amount, pay attention to body signals, and share supplement use during checkups, since these conversations help prevent interactions and unwelcome surprises. No one should trade real guidance for guesswork, especially when habits last for years.
| Names | |
| Preferred IUPAC name | β-D-glucoside glucohydrolase |
| Other names |
Maltase Alpha-glucosidase Beta-glucosidase Disaccharidase |
| Pronunciation | /ɡluːˈkoʊsɪˌdeɪs/ |
| Preferred IUPAC name | β-D-glucoside glucohydrolase |
| Other names |
1,4-alpha-D-glucan glucohydrolase glycoside hydrolase glucohydrolase maltase alpha-glucosidase |
| Pronunciation | /ɡluːˈkoʊsɪdeɪs/ |
| Identifiers | |
| CAS Number | 9001-42-7 |
| 3D model (JSmol) | 3D model (JSmol) string for Glucosidase: `1OGS` |
| Beilstein Reference | 1630723 |
| ChEBI | CHEBI:24163 |
| ChEMBL | CHEMBL2047 |
| ChemSpider | 21594025 |
| DrugBank | DB00503 |
| ECHA InfoCard | 100.007.486 |
| EC Number | 3.2.1.20 |
| Gmelin Reference | 9736 |
| KEGG | ec:3.2.1.20 |
| MeSH | D006801 |
| PubChem CID | 59816273 |
| RTECS number | MD1374850 |
| UNII | 1U9L3X64SB |
| UN number | UN2814 |
| CompTox Dashboard (EPA) | DTXSID2021336 |
| CAS Number | 9001-42-7 |
| Beilstein Reference | 2425914 |
| ChEBI | CHEBI:24176 |
| ChEMBL | CHEMBL204 |
| ChemSpider | 13318571 |
| DrugBank | DB00653 |
| ECHA InfoCard | 100.000.728 |
| EC Number | 3.2.1.20 |
| Gmelin Reference | 160942 |
| KEGG | K01187 |
| MeSH | D006802 |
| PubChem CID | 59819619 |
| RTECS number | LC0701000 |
| UNII | V5QO0I941L |
| UN number | UN number not assigned |
| CompTox Dashboard (EPA) | DTXSID5037865 |
| Properties | |
| Chemical formula | C6H11NO5 |
| Molar mass | 146,000 g/mol |
| Appearance | White lyophilized powder |
| Odor | Odorless |
| Density | 1.2 g/cm³ |
| Solubility in water | Soluble in water |
| log P | -2.11 |
| Acidity (pKa) | 6.0 |
| Basicity (pKb) | 4.6 |
| Magnetic susceptibility (χ) | −6.8 × 10⁻⁶ cm³/mol |
| Refractive index (nD) | 1.332 |
| Dipole moment | 5.85 D |
| Chemical formula | C12H17NO6 |
| Molar mass | 146,000 g/mol |
| Appearance | White lyophilized powder |
| Odor | Odorless |
| Density | ~1.3 g/cm³ |
| Solubility in water | Soluble in water |
| log P | -1.64 |
| Acidity (pKa) | 6.0 |
| Basicity (pKb) | 4.0 |
| Magnetic susceptibility (χ) | -6.1×10⁻⁶ cm³/mol |
| Refractive index (nD) | 1.52 |
| Dipole moment | 7.5 D |
| Pharmacology | |
| ATC code | A10BF01 |
| ATC code | A10BF01 |
| Hazards | |
| Main hazards | Harmful if swallowed. Causes serious eye irritation. Causes skin irritation. |
| GHS labelling | GHS07, Exclamation mark |
| Pictograms | GHS07 |
| Signal word | Warning |
| Hazard statements | H315: Causes skin irritation. H319: Causes serious eye irritation. H335: May cause respiratory irritation. |
| Precautionary statements | P261, P264, P271, P272, P280, P302+P352, P304+P340, P305+P351+P338, P312, P321, P333+P313, P337+P313, P362+P364, P501 |
| NFPA 704 (fire diamond) | 1-0-0 |
| LD50 (median dose) | LD50 (median dose): > 5000 mg/kg (Rat) |
| PEL (Permissible) | PEL for Glucosidase: Not established |
| REL (Recommended) | 90 U/L |
| IDLH (Immediate danger) | Not established |
| Main hazards | May cause allergy or asthma symptoms or breathing difficulties if inhaled |
| GHS labelling | GHS07, GHS08 |
| Pictograms | GHS05, GHS07 |
| Signal word | Warning |
| Hazard statements | H315: Causes skin irritation. H319: Causes serious eye irritation. H335: May cause respiratory irritation. |
| Precautionary statements | P264, P280, P302+P352, P305+P351+P338, P337+P313, P362+P364 |
| PEL (Permissible) | PEL for Glucosidase is not specifically established by OSHA. |
| REL (Recommended) | 100 U/g |
| IDLH (Immediate danger) | Not established |
| Related compounds | |
| Related compounds |
Cellulase Lactase Amylase Maltase Invertase Sucrase Trehalase |
| Related compounds |
Cellulase Amylase Lactase Maltase Sucrase Invertase Glucanase |