| HS Code | 677817 |
| Productname | Transglutaminase |
| Enzymetype | Transferase (EC 2.3.2.13) |
| Source | Microbial fermentation (Streptomyces mobaraensis) |
| Physicalform | White to off-white powder |
| Solubility | Soluble in water; insoluble in organic solvents |
| Phoptimum | 5.0–8.0 |
| Temperatureoptimum | 45–55°C |
| Molecularweight | Approximately 38 kDa |
| Enzymeactivity | Cross-links protein-bound glutamine and lysine residues |
| Phstability | Stable at pH 4.0–9.0 |
| Temperaturestability | Inactivated above 70°C |
| Typicalapplications | Meat binding, dairy texture improvement, bakery protein modification |
| Storagecondition | Store in a cool, dry place below 25°C; avoid moisture |
| Safety | Generally recognized as safe when used as a processing aid |
As an accredited Transglutaminase factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Transglutaminase, 500 g, supplied in a sealed, moisture-proof plastic container with desiccant, under cool, dry storage conditions. |
| Container Loading (20′ FCL) | 20′ FCL container loading of Transglutaminase: palletized, moisture-proofed, temperature-controlled, properly secured for safe chemical transport. |
| Shipping | Transglutaminase is shipped in temperature-controlled packaging, typically refrigerated or frozen, using insulated containers with gel packs or dry ice. It must remain sealed and dry to preserve enzyme activity. Standard, non-hazardous handling applies, but clear labeling such as “Keep Refrigerated” ensures safe, effective transport. |
| Storage | Transglutaminase is typically stored as a lyophilized powder at –20°C, tightly sealed in a desiccated container, protected from light and moisture. Under these conditions, it remains stable for months. Aqueous solutions should be prepared fresh and kept cold, or aliquoted and frozen to avoid repeated freeze-thaw cycles that reduce enzyme activity. |
| Shelf Life | Transglutaminase shelf life: stable for 12 months as lyophilized powder at -20°C; avoid repeated freeze-thaw cycles under these conditions. |
In a federally inspected red-meat establishment, microbial transglutaminase preparations with nominal activity of 100 U/g are pre-hydrated in 4°C water with sodium caseinate at a 1:1 ratio before addition to coarse-cut whole-muscle pieces at 0.3–0.5% w/w of the raw meat block. The slurry is transferred to a vacuum tumbler operated at −0.7 bar and 6 rpm for 45–90 min, while the mass temperature is held at 2–4°C. Binding strength is assessed as cooked slice tensile integrity following USDA FSIS Directive 7120.1; finished products must bear the statement “formed from pieces of whole muscle cuts” under 9 CFR 317.2(f)(2) for beef or 9 CFR 381.117(f)(2) for poultry. The enzyme preparation must conform to the FCC Enzyme Preparation monograph and is handled as a processing aid consistent with 21 CFR 101.100(a)(4). Crosslinking reaches operationally useful gel set within 4–8 h at 0–2°C, but production lines often hold vacuum-packed logs for 18–24 h to ensure maximum bind before freezing or cooking. Typical downstream product categories include bonded beef tenderloin medallions, portion-controlled poultry roasts, and formed filet portions from trimmed cuts. The principal failure mode on actual vacuum-tumbler lines occurs when raw meat pH falls below 5.8, reducing enzyme activity to below 40% of nominal and producing delamination after thermal processing; therefore phosphate buffers are adjusted to pH 6.0–6.5 before the enzyme is added.
Surimi-grade frozen fish mince entering a TGase binder line is processed after screw-press dewatering to 80–82% w/w moisture but before packaging or forming. Compliance is anchored to Codex Standard CXS 165-1989 for quick frozen blocks of fish fillet, minced fish flesh, and mixtures thereof, with the enzyme preparation accepted under JECFA specifications. Addition rates of 0.2–0.5% w/w on wet mince are typical, with activity normalised to 100 U/g. The refined paste is adjusted to pH 6.8–7.2 and mixed with sodium chloride at 2–3% w/w and ice water to maintain 5–10°C during a 5–8 min silent cutter cycle. The paste is extruded into crab-stick sheets or fish-ball moulds, then subjected to a low-temperature setting interval of 30–60 min at 40°C, followed by steam heating at 90°C for 20–30 min to inactivate the enzyme and set the gel. Gel strength is evaluated with A-grade surimi values in the range 400–600 g·cm and AA-grade values in the range 600–800 g·cm using a RheoTex gelometer at 20°C; the presence of TGase shifts the network from predominantly salt-induced aggregation to covalent ε-(γ-glutamyl)-lysine bonding. Finished product categories include crab analogues, fish balls, imitation shrimp, and extruded kamaboko. A process incompatibility exists when residual calcium chloride exceeds 0.15% w/w in the paste; the resulting gel becomes brittle and crosslinking efficacy drops because competitive protein aggregation interferes with the enzyme-substrate contact surface.
In set-style and Greek-style yogurt manufacture, microbial TGase is dosed after milk pasteurisation and homogenisation because exposure to 85°C for 1 min during pasteurisation reduces activity to below 5%. The milk base is standardised to 4.5–6.0% protein, homogenised at 200 bar and 65°C, then cooled to 40°C; TGase is added at 0.5–2.0 U/g casein and allowed to crosslink for 20–40 min before starter culture inoculation. The covalent bonds formed between casein micelles increase apparent viscosity and reduce syneresis, with 24-h whey separation values typically below 4 mL/100 g at 4°C. Compliance references include Codex Standard for Fermented Milks CXS 243-2003, and the enzyme preparation must meet JECFA microbial enzyme specifications. The process is transferred to a jacketed fermentation tank with internal cooling loops to maintain 40–42°C during crosslinking; subsequent lactic fermentation at 42°C proceeds until pH 4.5 is reached. Finished product types are high-protein spoonable yogurt, Greek-style strained yogurt with 9–10% protein, and dairy dessert bases. An operational boundary appears at addition levels above 2.5 U/g casein, where gel firmness can exceed 600 g·cm and produce a grainy, over-bound texture; at pH below 4.5 the enzyme is essentially inactive, so late dosing after fermentation is not recommended.
Cheese milk treated with TGase in the vat before rennet addition exhibits a distinct gel chemistry that must be managed within a narrow moisture-retention window. Cheese milk at 32–35°C is adjusted to pH 6.4–6.6, and TGase is added at 0.3–1.5 U/g casein; a holding time of 30–60 min is observed before calf rennet is introduced at 0.015–0.03% w/w. The crosslinking of casein in the milk gel increases curd moisture retention measured by AOAC 926.08 by 1–4% w/w at 0.5 U/g casein relative to untreated control; however, dosing above 1.5 U/g casein produces a rennet coagulation time exceeding 35 min and a weak curd because the enzyme competes for the same casein substrate. The manufacturing line uses jacketed open vats with curd cutting at 12.5 mm cube size, cooking at 38–39°C over 30 min, and pressing at 0.5–1.0 bar for 6 h. Regulatory compliance for finished cheese is anchored to Codex General Standard for Cheese CXS 283-1978 and processing-aid status under 21 CFR 101.100(a)(4). Finished products produced with this treatment include high-moisture mozzarella, process cheese base, and fresh cheese curd. A process constraint arises when thermophilic cultures acidify below pH 5.5 within 2 h; the rapid pH decline arrests TGase activity before the intended ε-(γ-glutamyl)-lysine network has fully formed.
In industrial bread and frozen dough production, TGase is applied on a flour basis to strengthen the gluten network, with a typical dosage of 10–30 mg/kg flour. The enzyme is dry-blended into flour before mixing to avoid the rapid hydration loss observed when it is first dissolved in dough water. The dough is mixed in a spiral mixer to a final dough temperature of 26–28°C, rested for 30–45 min, and sheeted at line speeds above 30 m/min; Brabender Extensograph recordings show an increase in Rmax of 20–40% relative to control at 20 mg/kg. Compliance for the enzyme preparation rests on the FCC Enzyme Preparation monograph and JECFA specifications; the final baked product remains subject to Codex Standard for Wheat Flour CXS 152-1985. Process constraints appear when dough floor time exceeds 90 min or when the enzyme level reaches 35 mg/kg; the dough becomes excessively elastic, and high-speed sheeting yields tearing and irregular crumb cell structure because the crosslink density restricts gas-cell expansion. Oven spring measured by baked loaf volume decreases if the crosslink density is above the optimum, while at 10 mg/kg the effect is limited to better slicing and improved crumb resilience. Finished product types include pan bread, whole-wheat high-fibre bread, and frozen dough for retail in-store baking. The operational window is widest at pH 5.5–6.2; formulation with sourdough systems below pH 4.8 reduces TGase activity to below 30% and is not recommended.
A vacuum bowl chopper operating at 4–6°C provides the cold-bind site for TGase in plant-based meat formulations because the high-moisture extrusion stage denatures the enzyme above 80°C. The enzyme is prepared as a 10% w/w aqueous solution and injected into the bowl chopper containing hydrated soy or pea protein, with an addition rate of 0.2–0.8% w/w on dry protein mass; mixing continues under vacuum at −0.8 bar for 6–10 min to eliminate air pockets. The mixed matrix is formed into patties or sausages and held at 4–6°C for 60–120 min to allow covalent gel formation before freezing or cooking. Binding strength is measured as raw patty tensile strength using a texture analyser with a 5 kN load cell and crosshead speed of 50 mm/min; treated soy-pea patties typically reach 4–7 N compared with 1–2 N for control formulations without TGase. The product falls under Codex General Standard for Vegetable Protein Products CXS 174-1989, and the enzyme preparation is covered by JECFA specifications. The critical incompatibility occurs in a twin-screw extruder with a length-to-diameter ratio of 40:1 when melt temperature exceeds 80°C; TGase activity is lost within 2 min, so the enzyme is added post-extrusion or in a separate cooling former at 40–50°C. Finished product categories are vegan burger patties, plant-based nugget pieces, and hybrid meat-vegetable binders with reduced methylcellulose content.
In edible film and collagen casing manufacture, TGase is used to crosslink gelatin hydrolysates and improve tensile strength and heat-seal integrity. A casting solution of 5–7% w/v gelatin or collagen hydrolysate is prepared in deionised water at 50°C, adjusted to pH 7.0 with sodium hydroxide, and dosed with TGase at 10–20 U/g protein. The solution is held at 40°C for 30–60 min under gentle agitation in a jacketed vessel, then cast onto a stainless-steel belt at a thickness of 0.4–0.6 mm and dried at 60°C for 4–6 h to reach 10–12% moisture. Tensile strength after conditioning at 23°C and 50% RH is reported in the range 20–40 MPa, with elongation at break of 5–15% measured following ASTM D882-18. Food-contact compliance for the final film is evaluated under 21 CFR 174.5, and the enzyme preparation itself is a processing aid. Finished product types include co-extruded collagen casings for sausage, water-soluble edible pouches, and dissolvable film strips for seasoning. A sharp processing boundary occurs when drying air temperature exceeds 70°C before full crosslinking; residual enzyme activity can cause later film brittleness after storage. Addition of TGase into gelatin solutions with pH below 5.0 or above 8.0 causes activity loss of greater than 50% and inconsistent crosslink density across the film web.
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Transglutaminase (EC 2.3.2.13) is a transferase that catalyses acyl-transfer between the γ-carboxamide group of peptide-bound glutamine residues and primary amines, principally the ε-amino group of lysine, forming ε-(γ-glutamyl)-lysine isopeptide bonds. The enzyme is obtained commercially from fermentation of Streptomyces mobaraensis and is standardised as a food-processing aid rather than as a pure protein. The mature microbial enzyme is a monomer of approximately 38 kDa; its calcium-independent catalysis proceeds through a thioester intermediate with the glutamine substrate before amine attack. This molecular feature has direct process consequences: the enzyme can crosslink proteins in the presence of calcium-chelating agents such as citrates and polyphosphates, which would inhibit calcium-dependent transglutaminases. Its catalytic action increases molecular weight of protein networks without requiring calcium or oxidative cofactors, distinguishing it from plasma-derived factor XIII and from calcium-dependent eukaryotic transglutaminases. In industrial practice, the enzyme is used in restructured meat, fish, dairy, bakery and plant-protein extrusion where texture, sliceability, water retention and elastic modulus are controlled by the number of crosslinks formed per unit protein mass. The preparation is not a binder in the adhesive sense; it does not contribute viscosity by hydration but modifies the protein matrix itself, so the response depends on substrate lysine and glutamine availability, pH, temperature, ionic strength and mixing history.
Microbial transglutaminase remains catalytically active across a broad but bounded window. The optimum temperature is generally 50–55°C, with significant activity retained at 4–10°C for cold-set meat and fish binding over 2–6 h. Thermal inactivation occurs rapidly above 70°C; therefore, processes that preheat protein streams above this threshold must introduce the enzyme after cooling. The pH optimum lies between pH 5.0 and pH 8.0, with activity falling sharply below pH 4.5 and above pH 9.0. In high-salt brines above 2% NaCl, catalytic rate can decline, yet cold-set binding is still observed if contact time is extended and the substrate is not denatured. The enzyme is calcium-independent, unlike guinea pig liver transglutaminase, and is inhibited by ammonia and by thiol-blocking agents above 5 mM dithiothreitol. Enzyme dosing is expressed per unit protein mass rather than total batch weight; typical addition ranges from 0.05–0.5% w/w of raw protein. Activity assays follow the hydroxamate method described in Food Chemicals Codex enzyme monographs, where one unit liberates 1 μmol of hydroxamic acid per minute at 37°C and pH 6.0 from a protected glutamine peptide substrate. Because the reaction is progressive and kinetically controlled, overdosing or excessive holding time produces a dense, elastic network that may register as texture hardening on instrumental texture profile analysers.
Commercial preparations are differentiated mainly by carrier matrix, enzyme activity per gram, and particle size. The product model designation therefore specifies handling and dosing behaviour more than catalytic mechanism. Activa TI is supplied as a granular powder with maltodextrin as the carrier and a declared activity of 100 U/g. Activa RM uses a sodium caseinate–maltodextrin carrier system and is specified for low-temperature restructured meat lines because the caseinate carrier contributes additional protein binding sites. High-potency powders declared at 1000 U/g are used where fill weight or powder load must be minimised, while liquid preparations in the range of 20–100 U/g allow inline dosing through static mixers or piston pumps. Differences between models should be read against the material safety and handling sections of supplier technical bulletins; published data for some specific configurations is limited. Table 1 summarises the formulation profiles commonly cited in industrial specifications.
| Model/Type | Carrier matrix | Declared activity | Physical form | Primary application zone |
|---|---|---|---|---|
| Activa TI | Maltodextrin | 100 U/g | Granular powder | Restructured fish, meat, dairy |
| Activa RM | Sodium caseinate / maltodextrin | 100 U/g | Granular powder | Cold-set restructured meat |
| High-potency powder | Maltodextrin | 1000 U/g | Granular powder | Bakery and dairy lines requiring reduced filler |
| Liquid preparation | Glycerol / water | 20–100 U/g | Liquid | Inline dosing and pumped injection |
Granular preparations require pre-dispersion in clean water at 10–15°C before addition when batch equipment does not provide sufficient shear. Direct dry addition into a bowl cutter with high-shear knives is acceptable because local shear disperses the powder and prevents carrier lumps. In low-shear mixture systems, undispersed granules can create localised over-crosslinked protein masses that are visible as hard specks after cooking. Thus, dispersion method is a more significant process variable than enzyme activity itself. Specifications for granular preparations commonly include moisture below 5%, particle size passing 60 mesh, heavy metals as lead below 5 mg/kg, total aerobic count below 10,000 CFU/g, and absence of Salmonella in 25 g according to the supplier certificate of analysis. These are release criteria rather than performance criteria, and they do not predict enzyme activity loss under humid storage.
Substitution changes more than carrier composition. In a typical cold-set whole-muscle binding line, Activa TI is applied as a dry powder at 0.1–0.3% w/w of meat block during vacuum tumbling at 4°C for 60–90 min, followed by forming and holding at 4°C for 2–6 h. When Activa RM is used, the sodium caseinate carrier dissolves into the meat exudate and contributes additional available lysine and glutamine at the cut surfaces, which can increase binding strength but also raises the risk of over-firming if the same dose and holding time are retained. Production-scale vacuum tumblers with 0.8 bar to 0.9 bar vacuum and variable speed control have shown better reproducibility than non-vacuum massage systems because vacuum-induced pore expansion increases contact between the enzyme solution and protein surfaces. Binding performance is assessed by cook loss and sliceability after thermal processing to a core temperature of 72°C; instrumental shear force using a Warner-Bratzler attachment is used as a texture reference. Storage and handling limitations include the following: the powder is hygroscopic, and prolonged exposure to relative humidity above 60% causes caking and uneven activity distribution. Avoid direct contact with high-pH phosphate brines above pH 8.5, because rapid activity loss occurs before uniform substrate contact is reached.
Compared with phosphate-based binders, transglutaminase does not require salt-soluble protein extraction, which allows reductions in sodium chloride and sodium tripolyphosphate. Compared with calcium alginate cold-set gels, the covalent crosslinks formed by transglutaminase remain intact after steam retort at 121°C for 30 min, whereas ionically crosslinked alginate networks may lose gel strength in high-ionic-strength brines. These differences are operational rather than subjective, and the choice between systems is made on the basis of final texture, clean-label constraints, and cost per kilogram of bound protein.
In acidified dairy systems, transglutaminase is added before acidification to crosslink casein micelles, altering gel firmness and serum retention. Typical dosage is 0.5–1.5 U/g protein, with incubation at 40–50°C for 30–60 min before fermentation. Overdosing above 2 U/g protein can produce a coarse aggregate network and increased syneresis, measurable as expelled serum volume after centrifugation at 1000 × g for 10 min. In bakery systems, the enzyme modifies gluten viscoelasticity by crosslinking high-molecular-weight glutenin subunits. Dough extensibility decreases and elastic modulus increases; farinograph water absorption and resistance to extension are used as process controls. Addition levels in bakery trials generally fall between 0.05–0.2% w/w of flour weight, but published data for this specific configuration is limited because flour batch strength dominates the response. The enzyme is inactivated during baking when crumb temperature exceeds 70°C, so it functions only during mixing and proofing.
High-moisture extrusion of plant proteins presents a process conflict for transglutaminase addition. Extruder barrel temperatures of 130–150°C exceed the thermal inactivation threshold, so pre-extrusion addition results in total activity loss before the crosslinking reaction can occur. Instead, production lines inject the enzyme after the cooling zone or apply it as a surface treatment to the exiting strand at temperatures below 55°C. In twin-screw extruders with an L/D ratio of 25:1, the cooling die must be designed with sufficient residence time to reduce the melt below the inactivation threshold before liquid enzyme injection. Carrier selection influences hydration in high-moisture tofu-like matrices: maltodextrin carriers dissolve rapidly but do not buffer locally high enzyme concentrations, while caseinate carriers can initiate enzymatic crosslinking before complete dispersion, causing visible lumps. Observed failure modes on production-scale equipment include die-face build-up from prematurely crosslinked protein, torque fluctuations when undispersed powder accumulates in the feed throat, and batch-to-batch moisture variation when relative humidity in the powder dosing hopper exceeds 60%. These are equipment-mediated effects, not intrinsic enzyme deactivation, and they are controlled by adjusting carrier type, pre-hydration, and injection point rather than by increasing enzyme dose.
Commercial transglutaminase from Streptomyces mobaraensis is evaluated as a food enzyme and processing aid in multiple jurisdictions. Safety assessments are based on the FCC hydroxamate activity method, purity criteria for heavy metals and microbial load, and absence of antibiotic activity in the production strain. The enzyme is covered by FDA GRAS notifications for specific preparation conditions, including GRN 000095, and by JECFA specifications for transglutaminase from Streptomyces mobaraensis. In the European Union, authorisation for food enzyme use is process-specific under Regulation EC 1332/2008, and importing batches must satisfy the microbiological criteria of ISO 4833-1:2013 for total aerobic count and ISO 21528-2:2017 for Enterobacteriaceae. Users should verify the regulatory status of the specific commercial model because carrier materials such as sodium caseinate or lactose may themselves trigger allergen labelling or standardisation changes. No activity claim should be carried into final product specifications without a validated enzyme assay, because residual enzyme activity after cooking is generally absent but may persist in cold-set products held below 50°C.
In surimi processing, transglutaminase is used to increase gel breaking force and deformation without raising salt content. The enzyme is mixed with minced fish after refining and before setting at 30°C for 30–60 min or cold setting at 4°C for 2–4 h. Typical addition is 0.1–0.3% w/w of surimi protein, depending on the heat-dependent endogenous transglutaminase activity of the fish species. Gel strength is measured as breaking force and deformation using a texture analyser with a spherical plunger at 5 mm/s crosshead speed. Over-crosslinking above 0.5% w/w can produce a brittle gel with high breaking force but low deformation, which is considered a failure in kamaboko-style products. The enzyme also covalently crosslinks myosin heavy chain, and this effect can be followed by SDS-PAGE band disappearance under reducing conditions. This application remains one of the most tightly specified uses because endogenous proteases and residual sarcoplasmic proteins modify the response.
