| HS Code | 788274 |
| Product Name | Lipase |
| Enzyme Class | Hydrolase |
| Source | Candida rugosa, Aspergillus niger, porcine pancreas |
| Catalytic Activity | Hydrolysis of triacylglycerols into glycerol and fatty acids |
| Optimal Temperature | 30-50°C |
| Optimal Ph | 7.0-9.0 |
| Molecular Weight | 30-60 kDa |
| Cas Number | 9001-62-1 |
| Ec Number | 3.1.1.3 |
| Solubility | Soluble in aqueous buffers; insoluble in organic solvents |
| Storage Conditions | Store at 2-8°C, avoid moisture and high heat |
| Applications | Food processing, detergents, biodiesel production, pharmaceuticals, diagnostics |
As an accredited Lipase factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Lipase, supplied as a fine powder, packaged in 25 kg sealed polyethylene-lined fiber drums for stability. |
| Container Loading (20′ FCL) | 20′ FCL: Lipase sealed in drums/packages, secured, labeled, temperature-controlled, ventilated, with full container documentation for safe transport. |
| Shipping | Lipase should be shipped refrigerated or on ice to maintain enzyme stability. Use insulated packaging with cold packs, and avoid temperature fluctuations. Ensure leakproof, sealed containers, proper labeling, and compliance with biological material transport regulations. For international shipments, include required documentation and avoid prolonged transit times to preserve activity. |
| Storage | Store Lipase powder at -20°C in a tightly sealed, desiccated container, protected from moisture and light. If prepared as a solution, aliquot into small volumes and freeze at -20°C or -80°C. Avoid repeated freeze-thaw cycles, as they reduce enzyme activity. Bring to room temperature gently before use. |
| Shelf Life | Shelf life: typically 6–24 months if stored cool, dry, and airtight; avoid moisture, heat, and repeated exposure. |
A soluble triacylglycerol acyl hydrolase (EC 3.1.1.3) dosed at 0.3–1.0 wt% relative to oil mass is used in batch stirred-tank reactors processing used cooking oil and high-free-fatty-acid feedstocks, where sodium methoxide catalysis would otherwise generate soap from free fatty acid contents up to 15%. Compliance for B100 fatty acid methyl ester requires EN 14214:2012+A2:2019 Table 2 limits of total glycerol 0.25 wt%, free glycerol 0.02 wt%, and acid number 0.50 mg KOH/g; ASTM D6751-23 independently sets total glycerol 0.24 wt% and free glycerin 0.020 wt%. Downstream production is executed in an agitated reactor fitted with a four-blade pitched-blade turbine operating at 400–700 rpm, 35–45 °C, and a controlled water content of 0.1–0.5 wt% measured according to ISO 12937:2000. Because methanol concentrations above one molar equivalent per addition cause phase separation and lipase unfolding, the stoichiometric 3:1 methanol-to-oil ratio is split into three equal additions at 0 h, 8 h, and 16 h; after each addition, agitator speed is held at the upper range for 10–15 min to maintain methanol dispersion. Glycerol is decanted when the glycerol layer exceeds 0.3 wt% of the oil phase to limit reverse transesterification. For continuous operations, immobilized lipase packed-bed reactors run at 0.5–2.0 h residence time and 0.5–1.0 kg enzyme per tonne of oil per hour, with feedstock moisture adjusted to 200–500 ppm. Terminal finished product types include B100 biodiesel for inland marine blending, R99/R100 renewable diesel co-processing streams after subsequent hydrotreatment, and crude glycerin as a secondary output. Operational boundaries include avoidance of phospholipid-rich oils without prior enzymatic degumming, because phosphorus above 30 ppm can coat the immobilized carrier and reduce half-life.
At the post-refiner screen reject stream of a thermomechanical pulping line processing Norway spruce (Picea abies) and radiata pine (Pinus radiata), pitch deposition on press felts, drying cylinders, and calender stacks is controlled by introducing a thermostable lipase formulation directly into the stock before the latency chest. Compliance for enzyme preparations used in papermaking depends on the intended paper grade: food-contact packaging grades require adherence to EU Regulation (EC) No 1935/2004 on materials and articles intended to come into contact with food, while mill quality programmes reference TAPPI T 204 cm-17 for dichloromethane extractives and TAPPI T 213 om-21 for dirt count. Typical addition ratio is 0.1–0.5 kg enzyme preparation per 1 tonne of oven-dry fiber, adjusted to solvent extractives load rather than total pitch mass; when dichloromethane extractives exceed 2.5 kg/t, the upper dosage is applied. Downstream production requires the stock to be held at 50–65 °C and pH 5.5–7.5 for 45–120 min in a latency chest or high-density storage tower, after which the pulp passes through screens and centrifugal cleaners before reaching the paper machine. Terminal finished products include standard newsprint, supercalendered SC-B magazine paper, and lightweight coated rotogravure grades, where pitch agglomerates larger than 0.04 mm² are counted as sheet defects. The enzyme is incompatible with chlorine dioxide or hypochlorite carryback from the bleach plant, and residual peroxide above 50 ppm in the stock at the injection point causes measurable activity loss within 15 min; published data for specific enzyme formulations and wood species remains limited.
The degreasing bath for Merino sheepskins in the beamhouse is set at pH 9.5–11.0 and 26–30 °C, with lipase addition calculated at 0.2–1.5% on fleshed hide weight; the higher dosage is applied when natural grease content exceeds 15% on dry matter. Regulatory compliance for leather chemicals requires REACH (EU) No 1907/2006 registration and ZDHC MRSL v3.1 conformance, while analytical sample preparation follows ISO 4044:2017. Downstream production uses a stainless-steel tanning drum at 4–6 rpm, float ratio 80–150%, and a nonionic surfactant at 0.2–0.5% on hide weight to solubilise hydrolysed triglycerides; the drum runs for 40–90 min before the float is drained and the skins are relimed or bated. Terminal finished products include automotive upholstery leather, full-grain gloving leather, and suede garment splits. Process control is critical because pH excursions below 9.0 or temperature above 32 °C can reduce lipase activity by more than 30% within one drum cycle, while overdosing beyond 1.5% does not improve degreasing but increases COD load in the spent float.
In heavy-duty liquid laundry detergent formulation, a liquid lipase preparation is post-added at 0.1–0.5 wt% of the final formula, with activity typically specified between 50,000 U/g and 100,000 U/g, where one unit releases 1 µmol of butyric acid per minute from triolein at pH 7.0 and 37 °C. Formulation compliance for detergent enzymes includes OECD 301B ready biodegradability testing and EU Detergent Regulation (EC) No 648/2004 labelling and ingredient degradation requirements, while stain removal is evaluated according to ASTM D4265-14. Downstream production in a blending vessel requires the finished base liquid to be cooled below 40 °C and adjusted to pH 7.5–8.5 before the enzyme is added under low-shear mixing at 100–300 rpm; the enzyme stream is never co-fed with hydrogen peroxide or hypochlorite bleach because oxidative species destroy the catalytic triad. Terminal finished products include standard liquid laundry detergents, single-dose polyvinyl alcohol pouch detergents with low water activity, and institutional laundry prespotters. At pH above 10 or storage temperatures above 50 °C, residual lipase activity declines by more than 20% within 24 h; the enzyme effect on dried triglyceride soils is progressive across multiple wash cycles rather than immediate in a single cycle.
Post-pelleting liquid spraying of a thermostable lipase onto broiler finisher crumbles creates a narrow processing window, because the enzyme must be applied after the pellet cooler reduces product temperature to 30–40 °C but before coating fats set on the particle surface. Feed additive compliance is governed by EU Regulation (EC) No 1831/2003 for feed enzymes, with Good Manufacturing Practice under FAMI-QS and GMP+ International for cross-border shipments. The formulated addition ratio in finished feed is typically 500–2,000 U/kg, where one unit is defined by the release of 1 µmol of fatty acid per minute from tributyrin at pH 7.0 and 37 °C; in dry carrier form this corresponds to 0.5–2.0 kg/t of a 1,000,000 U/kg product. Downstream production uses low-pressure atomizing spray nozzles at 60–80 psi, applied at 1–2% moisture addition in a continuous coating drum; the liquid enzyme is diluted in reverse-osmosis water immediately before spraying to avoid tank hydrolysis. Terminal finished products include piglet creep pellets with high fat content, broiler finisher crumbles, and extruded aquaculture feeds. The main process conflict is the pellet die temperature: when the enzyme is added in the mash before pelleting at 75–85 °C, uncoated liquid lipase loses more than 50% of activity, so only encapsulated or thermostable dry lipase is used in the mixer.
When immobilized sn-1,3-specific lipase is substituted for sodium methoxide in the interesterification of palm mid-fraction and coconut oil, the reaction is run in a packed-bed reactor at 55–70 °C, water activity 0.10–0.50, and residence time 30–120 min. Regulatory compliance for food-grade lipase includes EU Regulation (EC) No 1332/2008 on food enzymes and the common authorization procedure under EU Regulation (EC) No 1331/2008, with FCC identity and purity monographs applied for North American shipments. The addition ratio in batch solvent-free systems is 2–8 wt% of lipid substrate, while continuous packed-bed operation consumes 0.5–1.0 kg enzyme per tonne of oil per hour after initial hydration equilibration. Downstream production involves dissolving the lipase on a hydrophobic carrier, controlling water activity by pre-equilibrating the feedstock over saturated salt solutions or a humidified nitrogen stream, and then passing the mixed triglycerides through the bed at 0.5–1.5 h⁻¹ space velocity. Terminal finished product types include cocoa butter equivalents with stearic-oleic-stearic triglycerides, human milk fat substitutes with palmitic acid enrichment at the sn-2 position above 60%, and trans-free margarine hardstocks. Because the reaction equilibrium is sensitive to water content above 500 ppm, high water activity in feedstock shifts selectivity toward free fatty acid and diglyceride formation; the enzyme is also inactivated by exposure to acid-activated bleaching earth fines if the oil is not filtered to below 1 µm before the reactor.
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Lipase, designated EC 3.1.1.3 and registered under CAS 9001-62-1, is a triacylglycerol acylhydrolase supplied as a brownish-cream powder, a buffered liquid, or an immobilised granular preparation for hydrolysis, esterification, transesterification, and enantioselective resolution. The product model referenced in this technical introduction is a food-grade microbial lipase standardised to a representative minimum activity of 50,000 U/g; activity is measured by pH-stat titration against tributyrin at pH 7.0 and 37 °C, where one unit liberates 1 µmol of titratable butyric acid per minute. The powder is standardised with maltodextrin and food-grade salts to a tapped bulk density of 0.50–0.65 g/cm³, loss on drying below 8%, and a particle size distribution with 90% passing a 250 µm sieve. Unlike soluble esterase, lipase requires interfacial adsorption at an oil-water boundary before the lid domain reorients and exposes the catalytic serine; therefore the enzyme shows low activity on soluble short-chain esters and high activity on emulsified triglycerides. The preparation is not compatible with strong anionic surfactants above 0.1 wt%, because these displace the enzyme from the interface and suppress lid opening.
In stirred-tank hydrolysis, the enzyme is pre-slurried in process water at 25–35 °C before addition to avoid insoluble lumps. A starting enzyme dose of 0.1–1.0 wt% of neat oil is applied; the dose is adjusted for the substrate fatty acid chain length because long-chain monoenoic and polyenoic acyl groups may create steric constraints at the active site. The vessel is maintained at 45–55 °C for soluble powder, with pH controlled at 7.0–8.5 by automated caustic addition and a Rushton turbine for mixing. Feedstock peroxide values above 10 meq O₂/kg depress activity and are controlled by nitrogen blanketing or bleaching; free fatty acid levels above 15 wt% can lower phase inversion and increase foaming, requiring a mechanical foam breaker or a silicone-free antifoam at 0.05–0.2 wt%. Immobilised preparations are operated in packed columns with particle diameters between 300 µm and 850 µm; particles below 150 µm increase bed pressure drop and channeling risk. Pre-drying of feedstock is required when moisture exceeds 0.3 wt% and when the process target is hydrolysis control rather than spontaneous emulsion formation.
High lipase loadings do not produce proportionally higher conversion in low water-activity esterification. The limiting factor is the water generated by the condensation reaction, which accumulates in the interfacial film and raises local water activity. If local water activity exceeds 0.5, hydrolysis competes with esterification; if it falls below 0.1, the enzyme loses the hydration shell required for catalytic conformation. For this reason, the process window is maintained at water activity 0.2–0.4 with vacuum distillation or molecular sieves. A starting dose of 2–5 U per gram of substrate is used in solvent-free esterification of fatty acids with primary alcohols; above 10 U/g, conversion is usually controlled by interfacial area rather than catalyst availability. Droplet diameter is reduced to 10–50 µm in a high-shear rotor-stator mixer at 5,000–10,000 min⁻¹ for 10–15 min. Impeller tip speeds above 20 m/s may reduce soluble lipase half-life by more than 50% in high-shear recycle loops due to gas-liquid cavitation and shear denaturation.
In structured triglyceride production, a 1,3-specific microbial lipase is selected because it substitutes fatty acids only at the sn-1 and sn-3 positions; the sn-2 position remains largely intact, preserving the fatty acid stereochemistry and melting behaviour of the oil. This is different from a nonspecific lipase or a sodium methoxide chemical catalyst, both of which randomise acyl groups across all three positions. The 1,3-specific preparation shows reduced incorporation when long-chain polyunsaturated fatty acids exceed 20 wt% of the total fatty acid pool, and it may require a diluent such as high-oleic sunflower oil to maintain fluidity below 60 °C. In packed-bed operation, the substrate is brought to 60–70 °C and water activity is adjusted to 0.2–0.5; bed temperature is held below 70 °C to limit acyl migration from sn-2 to sn-1/3. When sn-2 acyl migration exceeds 5 mol%, the structured lipid loses its intended positional composition. Feed free fatty acid values above 15 wt% may require vacuum stripping at 80–90 °C and 10–15 kPa absolute pressure before the bed to prevent carrier hydrolysis and pH drop below 5.5.
Esterification for flavour and fragrance applications is operated in solvent-free conditions at 35–50 °C with vacuum at 5–15 kPa or molecular-sieve baskets. A fatty acid-to-alcohol molar ratio between 1:1 and 1:3 is maintained because excess alcohol increases equilibrium conversion but can strip hydration water from the enzyme. The reaction is continued until the acid value falls below 5 mg KOH/g; subsequent distillation at 80–120 °C removes the ester product. Unlike mineral acid catalysis, the lipase does not generate sulfated or oxidised by-products. The enzyme is incompatible with free amine-containing substrates because local pH above 9.0 causes irreversible denaturation.
Bakery applications use a low-dust powder at 10–30 ppm flour weight to hydrolyse endogenous triglycerides and modify the lipid-starch interface during mixing and proofing. The dosage is adjusted according to flour extraction rate and endogenous lipid content; high-extraction flour above 0.8% fat may require the lower dose to prevent excess polar lipid accumulation. The enzyme is denatured during baking at oven temperatures above 95 °C, and no residual activity is expected in the finished product. Premix segregation at 0.2–0.5 wt% carrier addition can cause batch-to-batch variation in loaf volume, so the powder must have a narrow particle size distribution.
When short-chain fatty acid release from milk fat is required, a pre-gastric or microbial lipase is added before homogenisation at 0.1–1.0 U/g milk fat and incubated at 30–40 °C for 30–120 min. The reaction is stopped by pasteurisation at 72 °C for 15 s or by pH reduction below 5.0. Because soluble lipase is heat-labile, residual activity is generally not detected after pasteurisation. The choice of lipase model determines the free fatty acid profile: oral-gastric lipases preferentially release butyric and caproic acids, whereas microbial preparations release a broader spectrum from C4 to C18.
Soluble powder is retained in the batch vessel and is deactivated by heat or pH adjustment at the end of the run, whereas immobilised lipase is recovered by filtration or retained in a fixed bed for repeated cycles. The immobilised product is typically supplied on a macroporous acrylic or silica carrier with particle diameter between 300 µm and 850 µm, which balances external mass transfer against bed pressure drop at superficial velocities of 0.5–2.0 cm/min. In continuous service, the carrier loses activity progressively through protein leakage, fouling by oxidised triglycerides, and mechanical attrition. Batch-to-batch reuse of 20–50 cycles has been reported for refined substrates with peroxide values below 5 meq O₂/kg; crude feedstocks with phospholipids and trace metals reduce reuse below 10 cycles. The fixed bed is loaded uniformly to avoid channeling, with a bed height-to-diameter ratio of at least 3:1. Pressure drop across the bed should remain below 0.5 bar; if pressure exceeds 1.0 bar, the bed is inverted or backwashed with warm solvent. Immobilisation also shifts the apparent pH optimum to 5.5–8.0 because the carrier microenvironment buffers the enzyme from bulk pH swings.
The powdered preparation is assessed against the Food Chemical Codex general monograph for enzyme preparations and JECFA enzyme specifications. Microbial contaminants are controlled by batch testing for Salmonella absence in 25 g, total coliforms below 30 CFU/g, and Escherichia coli absence in 25 g. Food-grade trade specifications often set lead not more than 5 mg/kg, arsenic not more than 3 mg/kg, and cadmium not more than 1 mg/kg. The product is considered a processing aid in many applications and is not required to be declared on the final label when it is denatured or removed, but regional approval status is governed by instruments such as EU Regulation (EC) No 1332/2008 on food enzymes. Dust handling requires occupational exposure limits for enzyme dusts; a dust concentration below 1 mg/m³ is commonly applied for process operators, and powder charging operations require local exhaust ventilation and HEPA filtration.
Lipase is selected over other hydrolases when the substrate is a water-insoluble long-chain triglyceride or when enantioselective hydrolysis of an ester is required. The following distinctions guide formulation selection; specific product data must be confirmed because pH and temperature optima vary by strain and immobilisation chemistry.
| Property | Lipase | Esterase | Phospholipase A₂ | Protease |
|---|---|---|---|---|
| Natural substrate | Long-chain triglyceride | Water-soluble short-chain ester | Phospholipid | Protein |
| Interfacial activation | Required | Not required | Not required | Not required |
| Preferred pH range | 6.5–9.0 | 6.0–8.0 | 8.0–10.0 | 7.0–9.0 |
| Common thermal range | 40–70 °C | 40–60 °C | 50–70 °C | 50–80 °C |
| Primary process function | Hydrolysis, interesterification, chiral resolution | Flavour ester formation | Degumming, lecithin modification | Protein hydrolysates |
| Main operational risk | Foaming, interfacial inhibition | Substrate solubility limits | Calcium dependence | Autolysis and off-note formation |
These distinctions are not absolute and are strain-dependent; a thermophilic microbial lipase may operate at 70–80 °C, while a fungal protease may overlap with lipase activity at neutral pH. When replacing a protease in a combined hydrolysis process, the user must verify whether the lipase requires calcium ions at 1–5 mM for thermostability and whether residual phospholipids in the feedstock will compete for interfacial area. Such verification is performed by a pH-stat assay at pH 7.0 and 37 °C against the intended process substrate, because supplier activity on tributyrin does not predict activity on mixed industrial triglycerides.
