| HS Code | 928530 |
| Product Name | Lactase |
| Product Type | Enzyme supplement |
| Enzyme Activity | Breaks down lactose into glucose and galactose |
| Source | Derived from Aspergillus oryzae or Saccharomyces cerevisiae |
| Dosage Form | Capsules, tablets, chewable tablets, drops, or powders |
| Common Use | Lactose intolerance management |
| Mechanism Of Action | Hydrolyzes lactose in the small intestine |
| Administration Timing | Taken just before or with lactose-containing food |
| Storage Conditions | Store in a cool, dry place away from moisture and heat |
| Shelf Life | Typically 1–2 years depending on brand |
| Common Side Effects | Mild gastrointestinal discomfort or allergic reactions in sensitive individuals |
| Contraindications | Individuals allergic to mold or yeast should avoid certain sources |
As an accredited Lactase factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Lactase enzyme, 50 g, off-white powder in sealed amber glass bottle with desiccant; label includes purity, storage, and safety information. |
| Container Loading (20′ FCL) | Lactase, non-hazardous enzyme, loaded in 20′ FCL on pallets, dry container, secured and ventilated, avoiding moisture and heat. |
| Shipping | Lactase is shipped as a temperature-sensitive enzyme, typically refrigerated or frozen to preserve activity. It is packed in sealed, moisture-resistant containers with desiccants, avoiding extreme heat. Transport uses insulated coolers with ice packs or dry ice, clearly labeled for cold-chain handling, ensuring stability and safety during transit. |
| Storage | Store lactase in a cool, dry place, ideally refrigerated at 2–8°C (35–46°F) for optimal stability. Keep the container tightly sealed to protect it from moisture and humidity. Avoid exposure to heat, direct sunlight, and freezing, as these can degrade enzyme activity. Use before the expiration date for best results. |
| Shelf Life | Store in a cool, dry place; unopened lactase typically retains potency for 12–24 months from manufacture date. |
Lactose-free pasteurized and UHT milk manufacture uses neutral β-galactosidase (EC 3.2.1.23) from Kluyveromyces lactis metered into raw milk after cream separation and before high-temperature treatment. Typical batch dosing is 2,000–5,000 NLU/L at 6–10°C for 12–24 h, which reduces residual lactose below 0.1 g/100 mL in full-fat and skimmed milk lines. The enzyme acts in a chilled stainless steel buffer silo with intermittent agitation; in-line static mixers are required when lactase is dosed continuously into the milk stream at flow rates above 20,000 L/h. Because the enzyme is heat-labile, it must be added before final UHT heating; UHT plants then process the pre-hydrolysed milk at 135–145°C for 2–4 s. The finished product retains the normal milky appearance but contains glucose and galactose instead of lactose. Compliance for the enzyme as a food processing aid in the EU is covered by food enzyme Regulation (EC) No 1332/2008 and national authorisations pending the Union list, while the US recognises lactase from Kluyveromyces lactis under 21 CFR 184.1387. The final labelling of lactose-free claims falls under Regulation (EU) No 1169/2011; although no single lactose threshold is defined universally in EU legislation, many national guidance documents and retailer specifications use the <0.1 g/100 g residual lactose criterion. Heat-stability limitations require close control of preheating: complete hydrolysis before UHT increases free reducing sugars and can accelerate Maillard browning and lactulose formation during the sterilisation hold; plant operators often reduce the UHT holding time by 1–3 s or lower preheating to 80–85°C to limit colour development in long-life lactose-free milk. Published data on furosine shift specific to lactase-prehydrolysed UHT milk is limited; therefore pilot-batch validation under actual heat-load conditions is necessary before committing full-line production.
When whey permeate is the substrate, the objective shifts from sensory softness in milk to conversion of a high-burden dairy side stream into stable syrup. UF permeate from sweet whey typically contains 75–85% lactose on dry solids, with total solids of 20–30% after reverse osmosis pre-concentration. Soluble Aspergillus oryzae lactase is dosed at 1,000–5,000 units per litre of 20% lactose permeate at 45°C and pH 4.5–5.5 for 4–12 h, achieving 80–95% lactose conversion depending on ionic strength and residual mineral content. In immobilised systems, β-galactosidase is covalently bound to epoxy-activated methacrylate or silica carriers and packed into fixed-bed reactors; reported liquid hourly space velocity ranges from 2 h⁻¹ to 10 h⁻¹ at 45°C, but vendor-specific packing density and pressure drop must be pilot-confirmed. The hydrolysate is then vacuum-concentrated to 70–75°Brix. Calcium and phosphate precipitation can occur in low-pH operation; the feed should be clarified and heat-treated at 70°C for 15 s before enzyme addition to reduce microbial load. The finished product is a reducing-sugar syrup used in confectionery, bakery, frozen desserts and fermentation media. Codex Standard for whey powders CODEX STAN 289-1995 does not cover liquid hydrolysed whey syrup as an identity standard, so export specifications must include country-specific syrup composition and microbial limits. In EU trade, hydrolysed whey syrup may fall under feed or food regulations depending on end use; if food, hygiene requirements of Regulation (EC) No 852/2004 and additive or enzyme provisions apply. The process limit is galactose crystallisation: at 70°Brix and storage below 20°C, galactose monohydrate can nucleate and settle, so terminal syrup storage is typically maintained above 30°C or galactose content is diluted with glucose syrup before shipping.
In transgalactosylation reactors, β-galactosidase catalyses galactose transfer to lactose or growing galacto-oligosaccharide chains when water activity is limited by high substrate concentration. The critical process window is lactose dry solids above 40% w/w; below 30% w/w, hydrolysis dominates and GOS yield drops below 10% on dry matter. Stirred-tank reactors are charged with lactose monohydrate dissolved at 60–65°C to 45–50% w/w, cooled to the enzyme-specific optimum shown in the table, and pH-stat controlled with dilute sodium hydroxide or hydrochloric acid. Enzyme dosage of 5–10 U/g lactose and reaction time of 10–30 h produce maximum GOS before the secondary hydrolysis phase depletes oligomers; product composition must be monitored by HPAEC-PAD or validated HPLC to terminate at peak GOS rather than at a fixed time.
| Operating variable | Kluyveromyces lactis neutral lactase | Aspergillus oryzae acid lactase | Bifidobacterium-derived β-galactosidase |
|---|---|---|---|
| pH range | 6.0–7.0 | 4.5–6.0 | 5.0–6.0 |
| Temperature | 35–45°C | 50–65°C | 40–50°C |
| Lactose concentration | 40–45% w/w | 45–50% w/w | 35–45% w/w |
| Maximum GOS yield on dry matter | 8–15% | 20–35% | 20–40% |
Downstream inactivation at 85°C for 10 min denatures the enzyme and stabilises oligomer distribution. The crude biomass is removed by depth filtration or centrifugation. Colour and off-flavours are removed with activated carbon at 0.5–1.0% w/w at 75°C for 30 min, followed by ion-exchange demineralisation to conductivity below 50 µS/cm. The purified liquor is concentrated in a falling-film evaporator to 45–75% dry solids and optionally spray-dried with a low-inlet-temperature profile of 160–170°C. The finished syrup meets the GOS specification in Commission Implementing Regulation (EU) 2017/2470; infant formula buyers additionally require residual lactose by ISO 22662:2007/IDF 198:2007 and monosaccharides by validated HPAEC-PAD method. The operational boundary is crystallisation of lactose and galactose monohydrate at dry solids above 55% at cooling temperatures below 40°C, which demands recirculation loops and jacketed dosing lines in large-scale reactors.
Frozen dessert mix lines adding lactase after pasteurisation and cooling target prevention of lactose-induced sandiness and controlled freezing point depression rather than complete lactose elimination. In a typical ice cream formulation containing 10–12% milk solids non-fat, lactose in the unfrozen serum phase is around 5–7%; lactose crystals above 30 µm produce a detectable gritty texture. The mix is pasteurised at 80°C for 25 s, homogenised at 70–75°C and 150–200 bar, then cooled to 6–10°C before enzyme injection. Neutral lactase from Kluyveromyces lactis is metered at 1,500–3,000 NLU/L into the aging tank during the 4–8 h aging phase, achieving 70–85% hydrolysis. The release of one mole glucose and one mole galactose per mole lactose increases solute molarity in the serum; colligative freezing point depression follows Raoult’s law, and mix draw temperature typically must be reduced by 0.3–0.7°C at 85% hydrolysis compared with untreated mix, depending on sweetener baseline. Overhydrolysis above 90% shifts the freezing point too far and yields a soft, sticky extruded product at conventional tunnel temperatures of -30 to -35°C. Process control therefore uses periodic compositional checks: residual lactose can be tracked by AOAC 984.15 enzymatic method or HPLC in the aged mix. The finished product is a lactose-reduced or lactose-free ice cream that normally lists lactase as a processing aid, not as an ingredient, when its residual activity has no function in the frozen finished product. In EU frozen dairy desserts, compliance includes Regulation (EU) No 1169/2011 for allergens and Regulation (EC) No 1332/2008 for food enzymes; organic or clean-label claims require verification against the buyer’s private standard.
When standardised milk is re-heated to fermentation temperature after a lactase hold, the process can reduce residual lactose and change acidification kinetics without strong acid hydrolysis. Pasteurised milk is cooled to 6–8°C, dosed with 2,000–4,000 NLU/L, and held for 4–8 h under slow agitation. After hydrolysis reaches 80–90%, the milk is re-heated to 42–43°C for inoculation with Streptococcus thermophilus and Lactobacillus delbrueckii subsp. bulgaricus. The preformed glucose and galactose are available immediately; some direct vat cultures show shortened lag phases, while others exhibit catabolite repression that delays lactose operon expression and can produce a slower late-acidification stage. The resulting fermentation time in small-scale set yoghurt trials is often shifted by 15–30 min earlier or later depending on the strain, so process validation with the exact starter blend is required before plant-scale implementation. The finished stirred yoghurt or quark must still be checked for residual lactose by ISO 22662:2007/IDF 198:2007 if the label claims lactose-free below 0.1 g/100 g. In concentrated quark manufacture, the hydrolysed lactose increases soluble solids in whey drainage and can reduce separator bowl load, but galactose retention in the curd may increase browning during hot-fill or pasteurised product holds. The product standard for fermented milks is CODEX STAN 243-2003; EU labelling obligations under Regulation (EU) No 1169/2011 require milk allergen declaration regardless of lactose hydrolysis. Acid whey from quark lines that is sold as co-product will contain free monosaccharides and should not be confused with native acid whey in buyer specifications.
Spray-dried calf and piglet milk replacers incorporating hydrolysed whey syrup require a hydrolysed ingredient with 15–25% residual lactose on dry matter and controlled reducing sugar content prior to blending. The lactase-hydrolysed whey permeate from the saccharification process is completed to 70–75°Brix, then blended with skim milk powder, whey protein concentrate, vegetable fat, emulsifier and lysine or methionine premixes in a high-shear mixer at 55–60°C. The blend is homogenised at 100–150 bar and pasteurised at 72–75°C for 15–20 s, then cooled to 50–55°C before spray drying. Inlet air temperature is reduced to 170–180°C and outlet held at 75–80°C because the glucose and galactose become sticky at higher heat-load conditions and cause cyclone and tower-wall fouling. The powder is lecithin-coated after drying at 0.1–0.3% w/w to improve flowability and wet-dispersibility in reconstituted milk replacer at 40–42°C. Lactase itself is not added directly to the final feed powder; its action is located in the upstream syrup. In EU trade, the hydrolysed whey syrup is placed on the market under feed materials Regulation (EC) No 767/2009, while any enzyme used as a process aid in feed material manufacture must be checked against Regulation (EC) No 1831/2003 for feed additive status. The practical limitation is that a high glucose proportion in the syrup reduces glass transition temperature of the dried particles; storage above 30°C or relative humidity above 60% triggers caking and non-enzymatic browning, so barrier bags with silica gel and warehouse humidity control are required. Published data for moisture sorption isotherms of lactase-hydrolysed whey permeate powder at 25–40°C is limited; therefore moisture migration testing under buyer-side tropical packaging conditions is necessary before high-volume shipments.
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Lactase LCT-100K is a liquid neutral β-galactosidase preparation (EC 3.2.1.23) obtained from a selected production strain of Kluyveromyces lactis and standardised to a declared activity of 100,000 FCC lactase units per gram. The supplied liquid is a clear amber solution with a density of 1.10 g/mL ± 0.05 at 20 °C and a pH of 6.0–7.0. Glycerol is present at 50 % w/w as a stabiliser, and potassium sorbate is present at 0.1 % w/w to limit yeast and mould growth during intermittent container use. The activity value is assigned using the Food Chemicals Codex lactase unit assay, which defines one unit as the liberation of 1 µmol of o-nitrophenol per minute from o-nitrophenyl-β-D-galactopyranoside at pH 6.5 and 37 °C. The preparation is water-miscible, free from visible foreign matter, and passes a 0.45 µm mixed-cellulose ester membrane filtration test.
The FCC lactase unit is not a direct measure of lactose hydrolysis rate in milk; it is a synthetic-substrate activity index. Dosage recommendations are therefore established in each dairy matrix. In whole milk containing 4.8–5.0 % w/w lactose, addition of 0.5–1.0 g/kg of Lactase LCT-100K at 38–40 °C for 2–4 h reduces lactose to below 0.1 g/100 g when quantified by ISO 22662:2017 HPLC with refractive-index detection. The enzyme follows Michaelis-Menten behaviour over the lactose range 5–100 mM; published Km values for K. lactis neutral β-galactosidase fall between 10 mM and 30 mM at pH 6.5 and 37 °C. At lactose concentrations above 200 mM, substrate inhibition may depress the observed velocity by more than 15 % relative to the uninhibited Michaelis-Menten model. Galactose inhibits competitively, with reported Ki values of 10–40 mM for this enzyme class. Because galactose accumulates stoichiometrically with glucose, batch hydrolysis rates slow as conversion exceeds 50 %.
Transgalactosylation activity is an inherent property of β-galactosidases. At lactose concentrations above 200 mM, Lactase LCT-100K can synthesise galacto-oligosaccharides as a side reaction instead of complete hydrolysis. The galacto-oligosaccharide yield depends on water activity and temperature; published values for K. lactis lactase range from 5–15 % of total lactose under concentrated whey permeate conditions. This side reaction reduces the yield of glucose and galactose and can affect the carbohydrate profile measured by HPLC. Process engineers should account for galacto-oligosaccharide formation when hydrolysing 20 % w/w whey permeate because refractive-index detection of residual lactose may be confounded by oligosaccharide peaks.
The temperature optimum of Lactase LCT-100K in buffered lactose solution is 40–45 °C at pH 6.5. At 50 °C, residual activity falls to 50 % of the initial value within 10–15 min; at 55 °C, residual activity is below 10 % after 5 min. These figures were determined using the FCC lactase unit assay after timed exposure in capped glass vials immersed in a controlled water bath. The practical processing window in production-scale hydrolysis is therefore narrow: bulk liquid temperature should be maintained within ±2 °C of the chosen set point. Steam-jacketed tanks without sufficient recirculation can generate wall temperatures that inactivate enzyme near the heating surface even when the bulk temperature probe reads within specification.
Residence-time distribution in continuous pre-hydrolysis systems introduces a different failure mode. For a 60 s plug-flow holding loop operating at 42 °C, the piping should achieve at least 90 % volumetric turnover within 50–70 s. Tracer studies using conductivity monitoring on equivalent holding loops show that unbaffled tanks and short-radius elbows create unmixed zones and tailing; this leads to under-hydrolysed portions reaching the downstream filler. In agitated batch tanks, baffled vessels with pitched-blade impellers and power inputs of 0.3 kW/m³ reduce short-circuiting relative to unbaffled tanks. Published data for this specific configuration is limited, but the measured impact of mixing on enzyme contact time is transferable from residence-time distribution studies in dairy processing.
Before UHT sterilisation, Lactase LCT-100K is metered into standardised whole milk at 4–8 °C at a dose of 1–3 g/kg and held for 16–24 h in agitated storage silos. Continuous addition through a static mixer upstream of the silo is preferred over pulsed batch dosing because the liquid enzyme is miscible and concentrated pockets can create uneven hydrolysis in the first 30 min. The hydrolysis reaction converts each 10 g/L of lactose into 5 g/L D-glucose and 5 g/L D-galactose. The resulting monosaccharide profile lowers the freezing point; cryoscopic measurements according to ISO 5764:2009 provide a rapid process check. Post-hydrolysis enzyme inactivation is achieved by UHT treatment at 138 °C for 2 s or by pasteurisation at 78 °C for 15 s. Residual enzyme activity in packaged milk should be below 0.5 % of the initial dose to prevent continued lactose hydrolysis and carbohydrate drift during storage.
Neutral lactase from K. lactis retains less than 20 % of its maximum activity at pH 4.5. Consequently, acid whey from cottage cheese or acid-coagulated dairy products must be neutralised to pH 6.0–6.5 with food-grade potassium hydroxide or sodium hydroxide before the enzyme is dosed. Prolonged exposure above pH 7.5 accelerates deamidation and reduces activity in recirculated enzyme-containing streams. For unneutralised acid whey, an acid lactase preparation from Aspergillus niger with a pH optimum of 3.5–4.5 is the established alternative. Acid lactase preparations are formulated at pH 4.0–5.0 with glycerol and may contain higher levels of acid-tolerant stabilisers; they are not interchangeable with neutral lactase in milk without pH adjustment.
Operational incompatibilities include exposure to oxidising sanitisers such as sodium hypochlorite and peracetic acid at concentrations above 50 ppm active halogen or peroxide. Transfer lines and holding tanks after CIP must be rinsed with potable water and verified free of sanitiser by oxidation-reduction potential or test strips before enzyme addition. Copper ions at 10 ppm and iron ions at 20 ppm can reduce neutral lactase activity by more than 30 % in buffered lactose solutions. Where metal contamination from worn pump seals is suspected, sodium citrate at 0.1 % w/w is used as a chelating agent in extended holding applications. The enzyme preparation is not compatible with strong acids, strong alkalis, or residual crosslinking agents used in some membrane-cleaning formulations.
Published comparisons of neutral and acid lactase preparations emphasise pH-activity profiles rather than enzyme class differences. Lactase LCT-100K exhibits full activity at pH 6.8, while an acid lactase from A. niger typically retains 60–80 % relative activity at that pH but is fully active at pH 4.0. Immobilised lactase systems designed for continuous packed-bed reactors differ in operational control: they allow lactose conversion throughout a column run but introduce pressure-drop constraints, channelling, and microbial fouling at the feed inlet. The soluble LCT-100K is added directly to the batch and is not recovered after hydrolysis; therefore, its operating cost is tied to single-pass enzyme dosage, while immobilised systems trade higher capital cost and cleaning overhead for repeated use in low-particulate streams such as whey permeate.
The product also differs from lactase preparations blended with protease or cellulase side activities: LCT-100K is released only after meeting FCC limits for contaminating enzymes, lead below 2 mg/kg, arsenic below 1 mg/kg, and cadmium below 1 mg/kg.
| Parameter | Lactase LCT-100K (K. lactis neutral) | Acid lactase (A. niger) |
|---|---|---|
| pH optimum | 6.5–7.0 | 3.5–4.5 |
| Temperature optimum | 40–45 °C | 55–60 °C |
| Relative activity at pH 4.5 | <20 % | >90 % |
| Relative activity at pH 6.8 | >95 % | 60–80 % |
| Typical substrate matrix | Whole milk, skim milk, neutral whey | Acid whey, sour cream, fermented dairy |
| Formulation pH | 6.0–7.0 | 4.0–5.0 |
| Parameter | Specification | Test method |
|---|---|---|
| Appearance | Amber to brown liquid, free from visible foreign matter | Visual inspection |
| Declared activity | 100,000 FCC lactase units/g ± 5 % | FCC lactase unit assay |
| pH | 6.0–7.0 at 20 °C | Potentiometric method |
| Density | 1.10 g/mL ± 0.05 at 20 °C | Oscillating U-tube density meter |
| Lead | ≤2 mg/kg | FCC atomic absorption method |
| Arsenic | ≤1 mg/kg | FCC colourimetric method |
| Cadmium | ≤1 mg/kg | FCC atomic absorption method |
| Total aerobic plate count | ≤5×10⁴ CFU/g | ISO 4833-1:2013 |
| Yeast and mould | ≤1×10² CFU/g | ISO 21527-1:2008 |
| Salmonella | Absent in 25 g | ISO 6579-1:2017 |
| Escherichia coli | Absent in 25 g | ISO 16649-2:2001 |
Shipment and handling are governed by the storage requirement of 0–8 °C. Freeze-thaw cycles are not recommended because repeated freezing can produce protein aggregation and activity loss; if accidental freezing occurs, the container should be thawed at 5 °C and gently mixed but not recirculated through high-shear pumps. The product shelf life from the date of manufacture is 12 months when stored in the original sealed container at 0–8 °C. Opened containers should be consumed within 30 days or re-analysed for activity. The preparation is intended solely for food-processing applications and is not suitable for direct parenteral administration. It is not manufactured in a dedicated allergen-free facility and may contain residual yeast protein; site allergen risk assessment should be conducted before use in infant or hypoallergenic product lines.
