IngredientesTransglucosidase (commonly abbreviated TGD or TG) is a microbially derived enzyme used as a dietary supplement, principally for its ability to alter the metabolic fate of dietary starch in the gastrointestinal tract. Transglucosidase (TG, alpha-glucosidase, enzyme code (EC) 3.2.1.20) is an enzyme capable of converting starch to oligosaccharides, such as iso-malto-oligosaccharides from maltose, via the action of amylase. It is also known as α-glucosidase, and it exhibits dual functions of hydrolysis and transglycosylation in the catalytic reactions of sugars. The hydrolysis function can cleave the α-1,4-glycosidic bonds at the non-reducing ends of α-glucosides, oligosaccharides, and polysaccharides, releasing glucose. The transglycosylation function can transfer the released glucose residue to another glucose or maltose substrate via an α-1,6-glycosidic bond, thereby producing non-fermentable isomaltulose oligosaccharides.
As an enzyme, transglucosidase is classified under two enzyme commission numbers depending on its primary activity: the hydrolytic activity places it under EC 3.2.1.20 (alpha-glucosidase), while its transferase activity is also referenced under EC 2.4.1.24 (glucosyltransferase). Aspergillus niger CCRC 31494 has been shown to produce an extracellular glucosyltransferase (EC 2.4.1.24) with a high transglucosylating activity.
The commercial supplement form of transglucosidase is derived from the filamentous fungus Aspergillus niger. Transglucosidase derived from Aspergillus niger has been studied for self-mediation in the gastrointestinal tract as a dietary supplement, and this enzyme is widely used to produce oligosaccharides in industry. The production of transglucosidase by Aspergillus niger has been examined in batch culture; corn steep liquor has been used as the nitrogen source, and activities obtained with different carbon sources have been characterized. The purified enzyme is a glycoprotein, containing approximately 27.6% carbohydrate (most of which is mannose), with an optimal pH of 4.0–4.5, and is stable in the pH range 4.0–6.0 and at temperatures below 50°C.
A transglucosidase of Aspergillus niger has demonstrated hydrolysis and transglucosylation activities toward several types of malto- and isomalto-oligosaccharides. The activity is competitively inhibited by glucose and mannose but is not inhibited by galactose and fructose; the Ki values of glucose and mannose are 12.9 mM and 75.9 mM, respectively.
Transglucosidase is available commercially under several trade names. A well-known industrial preparation is Transglucosidase L, manufactured by Amano Enzyme Inc. of Japan. During industrial-scale production of isomalto-oligosaccharides (IMO), starch is first liquefied with a thermostable bacterial α-amylase to produce limit dextrins, which are further saccharified by fungal α-amylase and transglucosylated using α-glucosidase (e.g., Transglucosidase L, Amano Enzymes Inc., Japan). Amano Enzyme was founded over 120 years ago in Japan as a pharmaceutical business and expanded into enzyme production in 1948.
As a dietary supplement, transglucosidase is sold in encapsulated powder form. Because transglucosidase is an enzyme, the dosages are measured in "units of enzyme activity" rather than milligrams or International Units (IU). This enzyme is currently available in the supplement market and has been acknowledged by the FDA as a new dietary ingredient. In clinical research, the enzyme has been administered as an oral preparation standardized by unit activity (e.g., 3,000,000 U/g preparations used in Japanese trials).
Unlike many botanical dietary supplements with long histories of traditional use in herbal medicine systems, transglucosidase as a defined, isolated enzyme preparation does not possess a pre-modern ethnopharmacological record. Rather, its "traditional" context is industrial and food-technological rather than medicinal.
Isomalto-oligosaccharides (IMOs), the principal products of transglucosidase action, occur naturally in various fermented foods and sugars such as sake, soybean sauce, and honey. These foodstuffs have been consumed throughout East Asian cultures (Japan, China, Korea) for centuries, and small amounts of naturally occurring transglucosidase-like enzymatic activity, contributed by fermenting microorganisms including Aspergillus species, likely played an ancient role in generating these oligosaccharides in fermented foods. However, the isolated enzyme itself was not traditionally recognized or deliberately used.
The modern industrial history of transglucosidase begins in Japan in the mid-to-late 20th century. Traditionally, IMOs are produced by α-amylase, maltogenase, and pullulanase, which are employed for the first saccharification step, followed by transglucosidase to catalyze a second hydrolase/transferase step and to introduce resistant α-1,6 bonds. IMOs have been developed to prevent dental caries, as substitute sugars for diabetics, or to improve the intestinal flora. Several companies currently manufacture isomaltooligosaccharides, of which Showa Sangyo (Japan) is the major producer. Of the emerging prebiotic oligosaccharides, IMOs are used in the largest quantities for food applications.
The dietary supplement application of transglucosidase — distinct from its use as an industrial food-processing enzyme — is a relatively recent development originating in Japan in the early 21st century. A novel strategy using Aspergillus niger transglucosidase (TGD) was introduced to produce oligosaccharides from starch in the digestive tract of humans to decrease postprandial blood glucose levels in individuals with impaired glucose tolerance and at high risk of developing type 2 diabetes mellitus (T2DM).
Transglucosidase is itself the active constituent, not a botanical extract. It is a single glycoprotein enzyme derived from Aspergillus niger culture filtrate. Its catalytic activity is the defining functional property.
A transglucosidase that has been purified to homogeneity from culture broths of A. niger gives a single protein band on SDS-gel electrophoresis (molecular weight approximately 116,000 daltons) and two protein bands on isoelectric focusing (pI values 5.1 and 5.0). It is a glycoprotein, containing 27.6% carbohydrate, most of which is mannose, has an optimal pH of 4.0–4.5, and is stable in the pH range 4.0–6.0 and at temperatures below 50°C.
Transglucosidase operates through a dual enzymatic mechanism that distinguishes it from simple digestive carbohydrases:
The net result of this dual mechanism is that digestible starch — which would ordinarily be fully hydrolyzed to absorbable glucose — is instead partially converted to oligosaccharides bearing α-1,6 linkages that mammalian intestinal enzymes cannot efficiently cleave. NMR and mass spectrometry data indicate that α-glucosidase from A. niger reacts with the non-reducing end of oligosaccharides to form an α-1,6 linkage, and a sugar unit with two α-1,6 linkages is gradually produced. Mass spectrometry data suggest that the sugar unit with two α-1,6 linkages originates mainly from a 3-mer and/or 4-mer when oligosaccharides are used as substrates.
Transglucosidase produces isomalto-oligosaccharides (IMO) such as panose and isomaltose by transferring glucose to maltose or glucose at the alpha-1,6 bond. IMO has a low glycemic index (GI) and is classified as a prebiotic. Transglucosidase (or glucosyl transferase) converts carbohydrates to oligosaccharides, such as panose and iso-malto-oligosaccharide, which are fermented to fecal short-chain fatty acids (SCFAs) by gut bacteria. Oligosaccharides in the alimentary tract modulate gut microbiota composition.
In the gastrointestinal context, using rat gastrointestinal and gastric ligation models, TGD has been shown to convert carbohydrates to oligosaccharides in the digestive tract. Products such as panose and isomaltooligosaccharide, which are predominantly utilized by bifidobacteria, are indigestible oligosaccharides that reach the cecum.
An important biochemical feature of transglucosidase is that its hydrolysis vs. transglucosylation activity is concentration-dependent. The enzyme catalyzes transglucosylation only when the substrate concentration is high, while it catalyzes hydrolysis alone when the substrate concentration is low. This means that the enzyme's prebiotic-generating activity depends on sufficient substrate (starch or maltodextrins) being present simultaneously — a relevant consideration for supplement dosing relative to meal composition.
The most studied application of transglucosidase is the reduction of postprandial (after-meal) blood glucose spikes. Transglucosidase decreases postprandial blood glucose levels in individuals with impaired glucose tolerance (IGT) and type 2 diabetes (T2D).
The foundational clinical study in this area was published in the Journal of Clinical Biochemistry and Nutrition in 2007 by Sasaki and colleagues. Sasaki et al. investigated "a novel strategy in production of oligosaccharides in digestive tract: prevention of postprandial hyperglycemia and hyperinsulinemia," published in J Clin Biochem Nutr (2007), volume 41, pages 191–196. In this study, the clinical investigation was performed in 21 healthy volunteers and patients with type 2 diabetes mellitus to check the glucose level in blood and secretion of insulin after meal; the enzyme showed good improvement in biological parameters.
Evidence strength: The initial 2007 study by Sasaki et al. was a proof-of-concept investigation. While it provided early human evidence for glucose and insulin reductions, it was a relatively small study (n=21) and its limitations include small sample size, mixed populations (healthy volunteers and T2DM patients), and limited duration. Results were characterized as promising but preliminary.
A pivotal 12-week randomized, double-blind, placebo-controlled trial published in Diabetes, Obesity and Metabolism in 2012 evaluated TGD in patients with established T2DM. In this 12-week, randomized, double-blind, placebo-controlled trial, the efficacy and safety of transglucosidase (TGD) were compared with placebo in patients with type 2 diabetes mellitus (T2DM). At 12 weeks, TGD 300 mg/day and TGD 900 mg/day significantly reduced HbA1c by 0.18% and 0.21%, and insulin concentration by 19.4 and 25.0 pmol/l, respectively, versus placebo.
Additional cardiovascular and lipid findings from this same trial included: TGD 300 mg/day and TGD 900 mg/day also significantly reduced low-density lipoprotein (LDL) cholesterol by 0.22 and 0.17 mmol/l, respectively. TGD 900 mg/day significantly reduced triglycerides by 0.24 mmol/l and diastolic blood pressure by 8 mmHg.
Evidence strength: This was a well-designed randomized controlled trial (RCT) with placebo control and blinding, conducted over a clinically meaningful 12-week period. The reductions in HbA1c (0.18–0.21%) are modest but statistically significant. The additional findings on LDL cholesterol, triglycerides, and diastolic blood pressure, if reproducible, would suggest broader cardiometabolic effects. Limitations include the relatively short follow-up and the fact that this trial was conducted at a single center in Japan with a specific ethnic population, limiting generalizability.
A second major RCT by the same Japanese research group, published in BMC Gastroenterology in 2013, examined TGD's effects on gut microbiota composition and body weight in T2DM patients. The randomized, double-blind, placebo-controlled study aimed to evaluate the efficacy of transglucosidase (TGD) in modulating blood glucose levels and body weight gain in patients with T2DM and to clarify the underlying mechanism by analyzing gut microbiota. The study included 60 patients who received placebo or TGD orally (300 or 900 mg/day) for 12 weeks, and blood and fecal samples were collected before and after 12 weeks.
Results showed significant changes in microbial populations: the Clostridium cluster IV and subcluster XIVa components were significantly decreased, whereas the Lactobacillales and Bifidobacterium populations significantly increased in the T2DM patients. The overall conclusion was that TGD treatment decreased blood glucose levels and prevented body weight gain in T2DM patients by inducing the production of oligosaccharides in the alimentary tract and modulating gut microbiota composition.
The proposed mechanism is a caloric and glycemic dilution effect: the mechanism underlying the reduction in the total amount of orally ingested calories is the consequent transformation of digestible substrate to indigestible fiber in the alimentary tract. The downstream effect on energy balance is further elaborated: the reduction in total calorie intake and the effect of the oligosaccharides generated by TGD can explain the reduction in blood glucose and lipid concentrations. Another mechanism may be the improvement in gut microbiota composition, as evident by the increase in the Bacteroidetes-to-Firmicutes ratio.
Evidence strength: This RCT (n=60, 12 weeks) is the strongest human evidence available for TGD's prebiotic and body weight effects. The trial used validated microbial analysis methods (T-RFLP). However, the study population was limited to Japanese T2DM patients. No long-term (>12 weeks) human RCT data are available. The body weight prevention effect specifically (as opposed to weight loss) suggests a modest metabolic benefit rather than a pronounced anti-obesity action.
A further RCT from the same research group, published in 2017, specifically examined the effects of TGD on bowel movements in T2DM patients — a relevant population given the high prevalence of diabetes-associated intestinal enteropathy. The objective was to evaluate transglucosidase treatment efficacy for bowel movements in patients with T2DM and to clarify the relationship between bowel movements, dietary habits, gut microbiota, and fecal short-chain fatty acids. In this randomized double-blind, placebo-controlled study, 66 patients received placebo or transglucosidase (300 or 900 mg/day) orally for 12 weeks, and fecal bacterial communities and short-chain fatty acids were analyzed before and after treatment.
Transglucosidase treatment significantly (p < 0.05) affected fecal microbiota (Prevotella spp., Bacteroides spp., Bifidobacterium spp., and Clostridium subcluster XIVa) and fecal short-chain fatty acid (acetate, valerate, succinate, and lactate) content. Clostridium cluster IV, Clostridium subcluster XIVa, Clostridium cluster XVIII, and fecal pH increased significantly and order Lactobacillales decreased in patients with bowel movement disorder compared with controls. The conclusion was that transglucosidase treatment alleviates bowel movement disorder symptoms in T2DM patients by increasing fecal acetate level.
Evidence strength: This was a preliminary randomized trial (n=66, 12 weeks). The bowel movement effects are mechanistically plausible given the prebiotic action of IMOs generated in situ, and the changes in microbial short-chain fatty acid production provide a coherent explanatory framework. However, this was explicitly characterized as a preliminary study, and the endpoint (bowel movements) was a secondary objective in the broader TGD research program. Independent replication is lacking.
Several preclinical studies have evaluated TGD in animal models. Transglucosidase (EC 3.2.1.20) is an enzyme capable of converting starch to oligosaccharides, such as iso-malto-oligosaccharides from maltose, via the action of amylase. The aim of one study was to evaluate whether oral administration of TG with maltose or dextrin is capable of reducing postprandial serum glucose concentration in streptozotocin (STZ)-induced diabetic dogs fed on a high-fiber diet. Five healthy and five STZ-induced diabetic dogs were employed in this study. TG supplementation with dextrin or maltose had no detrimental effect in healthy dogs.
Preclinical research also examined the enzyme in a rat gastrointestinal model: using rat gastrointestinal and gastric ligation models, it was demonstrated that TGD can convert carbohydrates to oligosaccharides. Products such as panose and isomaltooligosaccharide, which are predominantly utilized by bifidobacteria, are indigestible oligosaccharides that reach the cecum.
The IMOs generated by TGD activity have themselves been studied in animal models of diabetes and dyslipidemia: to simulate type 2 diabetes in rats, a high-fat diet along with small doses of streptozotocin was administered. These rats showed similar changes to diabetic patients, including high glucose levels and weight loss. Treatment of the rats with inulin and IMOs resulted in metabolic improvements.
An enzyme mixture study including transglucosidase (as glucosyl transferase) provided further mechanistic data: transglucosidase converts carbohydrates to oligosaccharides, such as panose and iso-malto-oligosaccharide, which are fermented to fecal short-chain fatty acids (SCFAs) by gut bacteria. Oligosaccharides in the alimentary tract modulate gut microbiota composition. The microbiota is implicated in T2DM pathogenesis and treatment.
Evidence strength: Animal and in vitro studies provide mechanistic support for the effects observed in human trials, but cannot substitute for clinical evidence. Results in diabetic dog and rat models are consistent with the human trial findings but must be interpreted with appropriate caution regarding cross-species translation.
Research is still in the early stages on whether the enzyme transglucosidase helps support healthy blood glucose levels. The mechanism of transglucosidase has been described as follows: "Instead of allowing starch to be converted into sugars that spike blood glucose and trigger an excessive release of insulin, transglucosidase converts starch into beneficial prebiotic fibers — oligosaccharides." In vitro and in vivo laboratory studies have shown the ability of transglucosidase to reduce insulin and glucose levels. Commentators have noted that "smaller science should not be overstated," and that the "newer" enzymes like transglucosidase "lack significant research in general." The available clinical evidence, while consistently positive within its scope, derives almost entirely from a single Japanese research group (led by Sasaki et al.), conducted in Japanese populations with T2DM. Independent multicenter or non-Japanese replication has not been published.
Transglucosidase has been studied in connection with the following body systems and health areas:
Transglucosidase is administered orally as an enzyme supplement. Because it is an enzyme, its potency is expressed in units of enzymatic activity. Because transglucosidase is an enzyme, the dosages are measured in "units of enzyme activity." A 450,000 unit dose is typically the amount found in one capsule.
The following dosages have been reported in peer-reviewed clinical studies:
The standardization of TGD preparations in clinical research has been described by reference to specific activity levels. The preparation used in the Japanese clinical trials is described as 3,000,000 U/g of TGD (per the activity assay used by the investigators). The mg dosages (300 mg, 900 mg) in those trials therefore correspond to specific enzyme activity units based on this preparation's standardization.
The available clinical trial data from three human RCTs conducted by the Sasaki group indicate a favorable safety profile. Reported data indicate that TGD treatment is safe because of a lack of serious adverse events in the treatments across multiple published studies. No serious adverse events were attributed to TGD at the 300 mg/day or 900 mg/day doses over 12-week treatment periods in T2DM patient populations. TG supplementation with dextrin or maltose had no detrimental effect in healthy dogs, and the human studies similarly did not report detriment in non-diabetic participants.
This enzyme is currently available in the supplement market and has been acknowledged by the FDA as a new dietary ingredient. Enzyme supplements are generally recognized as safe, although they may interfere with other medications.
The production of indigestible oligosaccharides in the gastrointestinal tract carries an inherent potential for fermentation-related side effects. Because IMOs are delivered to the large intestine where they are fermented by colonic bacteria, high doses may theoretically produce flatulence, bloating, or changes in stool consistency — effects well recognized for other prebiotic fibers and oligosaccharides. The clinical studies with TGD at 300–900 mg/day did not report these as significant adverse events, but this class effect deserves acknowledgment. Notably, the bowel movements study found that TGD altered fecal microbiota composition and short-chain fatty acid content, with transglucosidase treatment alleviating bowel movement disorder symptoms in T2DM patients by increasing fecal acetate level. This suggests that the gastrointestinal effects of TGD may be beneficial in the context of diabetic intestinal enteropathy, though individual responses may vary.
A pharmacodynamically significant interaction concern is the potential for TGD to be affected by, or to affect, alpha-glucosidase inhibitor drugs such as acarbose, voglibose, or miglitol. Transglucosidase derived from Aspergillus niger has been studied for self-mediation in the gastrointestinal tract as a dietary supplement; Prof. Sasaki reported that this enzyme showed oligosaccharides production in the digestive tract which improved microflora levels in the large intestine and decreased blood glucose levels and the excretion of insulin. Pharmaceutical alpha-glucosidase inhibitors (acarbose, miglitol, voglibose) work by blocking intestinal alpha-glucosidase enzymes, thereby inhibiting carbohydrate digestion. Since transglucosidase is itself an alpha-glucosidase-family enzyme that acts on the same substrates (starch, oligosaccharides), co-administration with these drugs could theoretically reduce the enzyme's activity, or the drug's effect could be altered — the mechanistic basis is complex and has not been characterized in clinical interaction studies. The enzyme's competitive inhibition by glucose (the activity of Aspergillus niger transglucosidase is competitively inhibited by glucose, with a Ki of 12.9 mM) suggests that blood glucose levels themselves could modulate the enzyme's activity in situ.
Because transglucosidase is derived from Aspergillus niger, individuals with known hypersensitivity to Aspergillus species or fungal-derived enzyme preparations should be aware of the potential for sensitization, though this has not been reported as a clinical problem in published studies of TGD supplementation. The enzyme is purified from the fungal culture filtrate; however, trace amounts of other Aspergillus niger-derived proteins could theoretically remain in commercial preparations.
Given that TGD demonstrably reduces postprandial blood glucose and HbA1c in T2DM patients, with 300–900 mg/day reducing HbA1c and insulin concentrations significantly versus placebo, additive blood glucose-lowering effects are possible in patients already using antidiabetic medications (insulin, sulfonylureas, metformin, GLP-1 receptor agonists, SGLT-2 inhibitors). This theoretically increases the risk of hypoglycemia in such individuals, though no documented cases of clinically significant hypoglycemia attributable to TGD supplementation appear in the published clinical literature. The absolute magnitude of the HbA1c reduction (0.18–0.21%) is modest, making a severe additive hypoglycemic interaction unlikely at the doses studied, but clinical vigilance is warranted in medicated patients.
All safety data for TGD as a dietary supplement derive from short-term (12-week) trials in Japanese T2DM populations. No long-term safety data (beyond 12 weeks), no large-scale post-marketing surveillance data, and no data in special populations (children, pregnant women, individuals with renal or hepatic impairment) are available in the peer-reviewed literature. Researchers and commentators have noted that "newer" enzymes like transglucosidase "lack significant research in general," and this observation applies to the safety evidence base as well.
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