| HS Code | 780383 |
| Product Name | Chicken Liver Hydrolase |
| Source | Chicken liver (Gallus gallus domesticus) |
| Appearance | Lyophilized powder |
| Color | Light beige to tan |
| Solubility | Soluble in distilled water and standard buffers |
| Optimal Ph | 7.0 |
| Optimal Temperature | 37°C |
| Molecular Weight | Approximately 50 kDa |
| Specific Activity | ≥50 U/mg protein |
| Storage Condition | Store at -20°C |
| Shelf Life | 12 months when stored unopened |
| Enzyme Classification | Hydrolase (EC 3.-.-.-) |
As an accredited Chicken Liver Hydrolase factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Chicken Liver Hydrolase supplied as off-white powder in a sealed polyethylene liner, 1 kg net, inside a fiber drum. |
| Container Loading (20′ FCL) | 20′ FCL: palletized drums of Chicken Liver Hydrolase, securely braced, temperature-controlled, full container load for safe transport. |
| Shipping | Ship Chicken Liver Hydrolase as a cold-chain biological enzyme. Store at –20°C during transit. Use insulated containers with dry ice or gel packs. Package in sealed, leak-proof vials to prevent contamination. Avoid extreme temperatures, heat, and shaking. Label as Biohazard? Typically non-hazardous, but handle per safety data sheet. Ensure expedited delivery. |
| Storage | Store Chicken Liver Hydrolase lyophilized powder at -20°C, tightly sealed, protected from light and moisture. For reconstituted solutions, store at 2–8°C for short-term use. For longer stability, aliquot and freeze at -20°C, avoiding repeated freeze-thaw cycles. Allow product to equilibrate to room temperature before opening to prevent condensation. |
| Shelf Life | Shelf life is typically 12 months when stored at -20°C, protected from moisture and repeated freeze-thaw cycles. |
Enzymatic liver digests for pet food palatants are manufactured in jacketed scrape-surface reactors fitted with anchor agitators operating at 12–18 rpm. Fresh or frozen chicken liver is minced below 3 mm, diluted with process water to 30–34% w/w dry matter, and pasteurized at 93–95 °C for 10 min. After cooling to 52 °C, the slurry is adjusted to pH 6.8 with food-grade sodium bicarbonate solution at 10% w/v. Chicken liver hydrolase is metered at 0.10–0.50% w/w of raw liver protein, but the actual addition is converted from supplier-certified casein protease units per gram and is not fixed by weight alone. Hydrolysis proceeds under low-shear mixing to limit foam, and a polydimethylsiloxane food-grade antifoam may be used at 0.02–0.05% w/w when batch height exceeds 70% of reactor volume. Free amino nitrogen is monitored every 30 min by the OPA method. The reaction is terminated by heating to 85–90 °C for at least 20 min when the target free amino nitrogen is reached. Residual enzyme activity above 1.0 U/g after thermal inactivation indicates insufficient time, temperature, or post-heat mixing.
The hydrolyzed slurry is cooled below 40 °C and passed through a 500 μm inline strainer before one of two finishing routes. Liquid palatant is stabilized with phosphoric acid to pH 5.8–6.2, held at 5–8 °C, and shipped with a maximum shelf life of 28 days; addition of potassium sorbate at 0.15% w/w can extend shelf life to 60 days only when a cold-chain audit confirms no excursion above 8 °C. Dry palatant is produced in a co-current spray dryer at inlet air 160–180 °C and outlet air 75–85 °C, with maltodextrin DE 10–15 used at 25–35% w/w of dry solids as carrier. The powder is agglomerated to bulk density 450–550 g/L and screened below 0.8 mm. Palatability is not governed by an ISO or AAFCO nutrient profile; acceptance must be confirmed by two-bowl preference testing against an internal control lot, and no universal pass criterion exists across species or kibble bases. Bitter taste rises sharply above DH 15% due to accumulation of hydrophobic dipeptides, so the hydrolysis target for palatability is usually DH 8–12%. The same batch may be rejected for extruded kibble top-coating if viscosity exceeds 1,200 mPa·s at 25 °C, because nozzle blockage becomes immediate on high-pressure atomization lines operating at 2,000–4,000 kPa.
| Enzyme dosage, % w/w raw liver protein | Hydrolysis time, h | DH, % | FAN, mg/g protein | Viscosity, mPa·s at 25 °C |
|---|---|---|---|---|
| 0.15 | 2 | 5.0 | 45 | 1420 |
| 0.25 | 4 | 8.5 | 82 | 960 |
| 0.35 | 6 | 13.0 | 126 | 710 |
| 0.50 | 6 | 17.5 | 171 | 530 |
These representative pilot records for 32% dry matter liver slurry show that dosage and DH are not interchangeable; two lots with similar DH may differ in viscosity if mincing particle size or pasteurization hold time varied.
When liver hydrolysate is converted into bacteriological peptone powder, the first refining step is clarification through a plate-and-frame filter charged with diatomaceous earth at 1.5–2.5% w/w of dry solids. The clarified filtrate is concentrated in a falling-film evaporator at 55–65 °C under 650–700 mm Hg vacuum until total solids reach 35–40% w/w. Freeze drying is preferred over spray drying for culture-peptone release because it preserves heat-labile peptides and reduces formation of pyrrolidone carboxylic acid from glutamine deamination. Final powder is blended to total nitrogen 12.0–14.0% on dry basis, amino nitrogen 4.0–6.0% on dry basis, ash below 10.0% after sulfated ignition, and chloride below 2.0% for fermentation-grade material. According to ISO 11133:2014/Amd 1:2018, culture media manufacturers cannot release a lot on chemical composition alone; growth promotion must be evaluated against a reference lot using target strains from the intended diagnostic application. Fastidious anaerobe media containing liver-derived hemin and peptides are qualified with productivity ratios between 0.5 and 2.0. Productivity below 0.5 suggests the peptide profile has shifted too far toward free amino acids, while a ratio above 2.0 may signal selective enrichment from undefined growth factors that complicates diagnostic interpretation. Microbial limits are controlled under ISO 4833-1:2013 for aerobic plate count and ISO 21528-1:2017 for Enterobacteriaceae; acceptance for pathogen detection media is often below 1,000 CFU/g total aerobic count. Acid hydrolysis must be avoided during clarification because it increases neutralization salts and narrows the usable pH window of subsequent buffered media. The main incompatibility for powder stability is moisture pickup above 6% loss-on-drying; in tropical packaging lines, aluminium-laminated bags with silica gel sachets are required to block caking and Maillard browning during warehouse storage above 30 °C.
Chicken liver hydrolase is operated upstream of a thermal Maillard reaction to convert avian liver protein into a controlled pool of free amino acids and small peptides before reducing sugars are introduced. Hydrolysis is carried out in a jacketed stirring vessel at pH 6.0–6.5 and 48–52 °C for 3–5 h. If temperature is raised above 55 °C, the crude hydrolase loses aminopeptidase activity faster than endopeptidase activity, shifting the hydrolysate toward longer peptides and reducing final pyrazine yield. After inactivation at 85 °C for 20 min, the hydrolysate is blended with D-xylose at 2.0–4.0% w/w and ribose at 0.5–1.5% w/w. The mixture is transferred to a closed pressurizable reaction vessel and held at 95–120 °C for 30–90 min, with maximum pressure below 2 barg. The IOFI Code of Practice for process flavour manufacture permits heating up to 180 °C, but the liver hydrolysate route runs significantly lower because sulphur-containing volatiles degrade into hydrogen sulfide and mercaptan off-notes above 130 °C. Free amino nitrogen before the thermal stage dictates Strecker aldehyde, thiophene, and pyrazine intensity; hydrolysis is therefore terminated before DH exceeds 12% so residual peptides survive and reduce burnt off-notes. The finished reaction flavour is homogenized at 150–250 bar and spray dried onto gum arabic carrier at 12–18% w/w of carrier solids. Analytical release by gas chromatography-mass spectrometry is product-specific; no universal marker exists for chicken liver-derived process flavour, but the ratio of 2-acetyl-1-pyrroline to 2-ethyl-3,5-dimethylpyrazine is often monitored as a roast-versus-liver balance indicator for dry soup and gravy applications. Incorporation into extruded snack coatings is commonly 0.5–2.0% w/w of finished product, and EU market labelling follows Regulation (EC) No 1334/2008 when the material is sold as a flavour preparation. Free cysteine above 0.3% w/w before heating is an operational boundary; it increases hydrogen sulfide evolution and can corrode 316L stainless steel vent lines when repeated campaigns exceed 1,000 h.
When a poultry rendering line is required to upgrade heat-sterilized liver cake into feed-grade peptide fractions, chicken liver hydrolase is added after the co-products have been comminuted below 5 mm and cooled to 50 °C. The reaction is run in a horizontal ribbon blender reactor, with pH maintained at 6.4 using 85% phosphoric acid. Hydrolysis time is limited to 4 h because prolonged incubation raises mesophilic plate counts and reduces single-shift throughput. The liquid hydrolysate is acidified to pH 4.0 with formic acid, stabilized with sodium benzoate at 0.1% w/w, and stored below 25 °C for a maximum of 21 days. For dry feed use, the liquid is spray dried with wheat bran flow aid at 20–30% w/w of final solids to a water activity below 0.70. Nutritional improvement is not assumed; published data for this specific configuration is limited, so apparent ileal digestibility should be measured using the adult rooster assay before ration inclusion exceeds 5.0%. The main operational boundary is avoidance of Maillard browning during drying: air inlet above 180 °C can reduce available lysine by more than 20%, which is unacceptable in monogastric feed formulation. In addition, formic acid must not be mixed with sodium hypochlorite sanitation residues because chlorine gas may form in the liquid storage tank. The resulting feed-grade peptide fraction is typically blended into broiler or swine rations as a restricted-inclusion protein replacement, but batch records must document inactivation of avian pathogens according to the rendering plant’s HACCP plan and local veterinary sanitary regulations.Competitive Chicken Liver Hydrolase prices that fit your budget—flexible terms and customized quotes for every order.
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Chicken Liver Hydrolase, model CLH-100, is a lyophilized carboxylic-ester hydrolase preparation derived from clarified Gallus gallus domesticus liver tissue and assigned to EC 3.1.1.1. The reference unit is defined by hydrolysis of p-nitrophenyl butyrate at 37 °C in 50 mM Tris-HCl buffer adjusted to pH 7.4. Lot-specific activity is reported in U/mg on the certificate of analysis rather than as a fixed nominal value. The powder is white to off-white, free-flowing after cold storage, and contains residual moisture at ≤ 5.0%, total protein at ≥ 45% by dry weight, and no added cofactors beyond phosphate buffer salts. Product is packaged in double polyethylene-aluminum laminate pouches under nitrogen and held at −20 °C. A carrier-bound form, model CLH-200, is produced by covalent attachment to methacrylate-divinylbenzene beads with a particle size fraction of 150–300 µm for packed-bed reactors. A liquid stabilized form, model CLH-300, is supplied in 50% glycerol for direct dosing into aqueous buffer systems.
Release testing includes microbial enumeration according to USP <61>, specified pathogens according to USP <62>, bacterial endotoxin by the Limulus amebocyte lysate method described in USP <85>, and water content by USP <921> Method Ia. Filling is performed in an ISO 14644-1:2015 Class 8 controlled area. The specification matrix is given below.
| Parameter | Specification | Method |
|---|---|---|
| Appearance | White to off-white lyophilized powder | Visual inspection |
| Residual moisture | ≤ 5.0% | USP <921> Method Ia |
| Total protein | ≥ 45% dry weight | Biuret with bovine serum albumin standard |
| Specific activity | Lot-specific, reported in U/mg | p-nitrophenyl butyrate, 37 °C, pH 7.4 |
| pH of 10 mg/mL solution | 6.5–8.0 | Potentiometric pH |
| Microbial limits | ≤ 100 CFU/g total aerobic count | USP <61> |
| Bacterial endotoxin | ≤ 0.5 EU/mg | USP <85> |
The hydrolase accepts a broad range of short-chain alkyl esters, aryl esters, and N-acetylated amino acid esters. The reference substrate is p-nitrophenyl butyrate; reported screening data also include hydrolysis of ethyl butyrate, phenyl acetate, and N-acetyl-L-methionine methyl ester. Activity is highest between pH 6.5 and pH 8.5. Exposure below pH 5.0 or above pH 9.5 produces rapid and largely irreversible loss of esterase function. The preparation operates without nicotinamide cofactors, flavins, or added metal ions, which permits its use in reaction media that would be incompatible with whole-cell biocatalysts.
Published kinetic data for chicken liver hydrolase in immobilized continuous-flow systems are limited. Process limits should therefore be verified by a scouting matrix at the intended co-solvent concentration. Dimethyl sulfoxide is tolerated at ≤ 10 vol% for contact times up to 2 h; higher concentrations produce measurable activity loss that is aggravated by free fatty acid accumulation and must be assessed lot-to-lot. Methanol and ethanol at 5 vol% are generally compatible, but acetonitrile at 5 vol% can shift the apparent active-site pH and reduce observed conversion. If the process requires increasing a water-miscible co-solvent from 10 vol% to 25 vol%, the enzyme should be removed or re-isolated after the solvent step rather than maintained in the binary mixture. This boundary is material in continuous-flow systems because solvent addition alters viscosity and residence time distribution.
Model CLH-200 is produced as a slurry in 20% ethanol–water and packed into glass or stainless-steel columns with internal diameters of 10 mm or 25 mm. Bed height should be at least 100 mm to limit wall channeling. A typical 10 mm × 150 mm bed is operated at a superficial linear velocity of 0.5–2.0 cm/min and produces a pressure drop below 1.5 bar for aqueous substrate solutions at 25 °C. The carrier typically carries 10–20 mg protein per gram dry beads, but apparent activity is governed by pore diffusion. Substrate molecular weight above 300 g/mol can reduce observed per-bead activity. Because published data for this specific configuration are limited, a laboratory residence time distribution study using a sodium chloride tracer should be performed before scale-up.
For kinetic resolution of racemic methyl esters of 2-arylpropionic acids, CLH-100 is dispersed in cold 50 mM potassium phosphate buffer at pH 7.0 and loaded at 10 g/L. The reaction is held at 37 °C in a jacketed vessel with a pitched-blade impeller at 250 rpm. Conversion is monitored by chiral high-performance liquid chromatography. The desired acid is recovered by extraction after removal of unreacted ester. Because the enzyme remains in the aqueous phase after pH adjustment, it can be separated by ultrafiltration through a 10 kDa polyethersulfone membrane. Dry powder should not be added directly into a vortexing buffer; pilot-scale batch records indicate that this can generate protein aggregates that increase downstream membrane pressure drop. The powder is pre-wetted with a small volume of cold buffer before being introduced into the main reaction mass.
The most direct comparator is porcine liver esterase, which shares the EC 3.1.1.1 classification but differs in tissue source, glycosylation pattern, and thermal stability. Chicken liver hydrolase is avian-derived, which avoids the porcine supply-chain constraint relevant to kosher and halal dietary supplement processing. In comparative substrate screening, the avian preparation often shows higher relative activity on short-chain fatty acid esters and N-acetylated amino acid esters, whereas porcine liver esterase is widely used for hydrolysis of prochiral dimethyl esters. Microbial carboxylesterases from Bacillus or Aspergillus can be more stable at alkaline pH and in organic solvent, but they may require different purification and often exhibit different enantioselectivity. Unlike immobilized Candida rugosa lipase, CLH-100 does not require interfacial activation at a hydrophobic interface; activity is observed in fully aqueous solution.
| Feature | Chicken Liver Hydrolase CLH-100 | Porcine Liver Esterase | Candida rugosa Lipase |
|---|---|---|---|
| Source material | Gallus gallus domesticus liver | Sus scrofa liver | Yeast fermentation |
| Enzyme class | EC 3.1.1.1 | EC 3.1.1.1 | EC 3.1.1.3 |
| Reference pH range | 6.5–8.5 | 7.5–8.5 | 6.0–8.0 |
| Typical operating temperature | 25–37 °C | 25–37 °C | 30–40 °C |
| Interfacial activation | Not required | Not required | Required for maximum activity |
| Common application | Ester resolution, amidase activity | Prochiral diester hydrolysis | Lipid ester hydrolysis, flavor ester synthesis |
For dietary supplement and food-contact applications, the avian origin is often preferred when non-porcine documentation is required. The manufacturer maintains ISO 9001:2015 quality records and can supply lot-specific allergen statements and transmissible spongiform encephalopathy declarations. The enzyme is not automatically food-grade in all jurisdictions; users must verify compliance with 21 CFR 117 or the applicable food enzyme regulation before use.
Amine-based buffers such as triethanolamine or Tris can deplete water at the active site if used at high concentration. When a reaction requires 100 mM Tris, the pH must be adjusted with hydrochloric acid at the working temperature before enzyme addition. The hydrolase should not be pre-dissolved in alkaline Tris without substrate present; prolonged exposure above pH 9.0 produces irreversible activity loss. Divalent metal ions are not required and may precipitate phosphate-based buffer systems, creating particle load in downstream ultrafiltration. The powder is sensitive to phenylmethylsulfonyl fluoride and other serine hydrolase inhibitors. Avoid combination with amine-based additives used as epoxy curing accelerators if the enzyme is later processed in solvent-free resin systems; residual amine can raise local pH above the stability threshold.
If the lyophilized powder is removed from cold storage in an environment above 60% relative humidity, the pouch should be equilibrated to ambient temperature inside a desiccator before opening. Condensation on cold powder can reduce flowability and create localized high-moisture zones, which are difficult to disperse in high-shear mixing. The powder is not pre-dried after opening.
Hydration is carried out with cold buffer under low-shear stirring. In a 50 L jacketed reactor, a retreat-curve impeller at 150–250 rpm is sufficient to dissolve the powder without generating surface foam. Foam formation can alter local protein concentration and reduce reproducible activity; if foam persists, a silicone-free defoamer compatible with the downstream purification train should be evaluated at 0.05 wt% maximum. The enzyme solution is normally clarified through a 0.45 µm polyethersulfone capsule filter before transfer to a chiral resolution vessel or packed-bed feed tank. This step removes aggregated protein and reduces pressure drop across subsequent membranes and immobilized beds.
Continuous operation with CLH-200 in a 10 mL packed bed is typically started with a substrate concentration of 50 mM, a superficial velocity of 1.0 cm/min, and a temperature of 37 °C. Product breakthrough curves are lot-specific because enzyme loading can vary by ±10%. Acceptable operating windows are established by pulse-injection tracer studies using 1 M sodium chloride. The immobilized carrier is not suitable for chlorinated solvents or for media containing more than 1.0 wt% free oil, because channeling and carrier fouling reduce apparent conversion and shorten bed life.
