| HS Code | 164830 |
| Product Name | Seafood Hydrolase |
| Product Type | Protease enzyme preparation |
| Source | Microbial fermentation (Bacillus species) |
| Appearance | Fine powder, light yellow to brown |
| Enzyme Activity | ≥ 100,000 U/g |
| Optimum Temperature | 50–60 °C |
| Optimum Ph | 6.0–8.0 |
| Solubility | Fully soluble in water |
| Moisture Content | ≤ 8% |
| Heavy Metals As Pb | ≤ 10 mg/kg |
| Total Plate Count | ≤ 1000 CFU/g |
| Coliform | ≤ 30 MPN/g |
| Storage Conditions | Keep in cool, dry, ventilated place |
| Shelf Life | 12 months from production date |
As an accredited Seafood Hydrolase factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.
| Packing | Seafood Hydrolase, 25 kg net, packaged in sealed polyethylene-lined fiber drums for safe transport and stable storage. |
| Container Loading (20′ FCL) | 20′ FCL container loading for Seafood Hydrolase: securely packed, temperature-controlled, moisture-protected, labeled, and documented for safe transport. |
| Shipping | Seafood Hydrolase ships in sealed, food-grade containers to prevent moisture absorption and contamination. Store at 2–8°C during transit to maintain enzyme activity. Avoid extreme heat, freezing, or direct sunlight. Non-hazardous per transport regulations, but keep dry and clearly label as temperature-sensitive biological material. |
| Storage | Store Seafood Hydrolase in a tightly sealed original container in a cool, dry, well-ventilated area, ideally at 2–8°C (35–46°F). Protect from direct sunlight, moisture, and heat sources. Keep away from acids, alkalis, and oxidizing agents. Avoid repeated opening and contamination. Always follow the manufacturer’s label instructions for stability and disposal. |
| Shelf Life | Shelf life is typically 12 months when stored at 2–8°C, tightly sealed, and protected from moisture and light. |
In pelagic by-product hydrolysis, mixed-species viscera from Atlantic mackerel and herring are converted into fish protein hydrolysate through a two-stage stirred-tank sequence followed by ceramic ultrafiltration with a cut-off of 10 kDa. The enzyme preparation is dosed at 0.5–1.5% by weight relative to crude protein, and the reaction is held at 50–60 °C and pH 6.8–7.5 for 2–4 h, with continuous addition of 2 M NaOH to control pH drift. Under these conditions, the pH-stat titration curve typically indicates a degree of hydrolysis of 15–28%, confirmed by o-phthaldialdehyde fluorescence assay. The hydrolysate is clarified through a decanter centrifuge maintained to remove particles above approximately 0.3 mm, then evaporated to 40–50 °Bx in a falling-film evaporator before spray drying. The resulting powder must comply with protein and ash methods of ISO 5983-1:2005 and ISO 5984:2002 for feed or food ingredient specification; lipid oxidation is tracked by peroxide value according to AOCS Cd 8b-90. Batch temperature above 62 °C denatures the protease component within 10–15 min, while residence beyond 6 h increases total volatile basic nitrogen and may indicate microbial or endogenous enzyme activity. Published data for mixed-species cold-water viscera are limited; therefore, pilot-scale trials must map pH-stat endpoint against molecular weight distribution before final enzyme-to-substrate ratios are fixed.
Accelerated anchovy sauce maturation introduces a measurable histamine risk when enzyme activity persists after the free amino nitrogen target is reached. Traditional fish sauce fermentation requires 12–18 months at ambient temperature and salt concentrations of 25–30% by volume. Adding seafood hydrolase at 0.2–0.8% by weight to chopped adult anchovy can reduce maturation to 8–16 weeks if brine temperature is held at 35–40 °C and the salt concentration is initially limited to 12–15% before final adjustment to 25%. However, histidine decarboxylation by spoilage bacteria also increases in the 20–40 °C band, particularly above 25 °C. Production-scale confirmation requires high-performance liquid chromatography with post-column derivatization for histamine, with a practical control limit of 400 mg/kg for fish sauce under CODEX STAN 302-2011 quality provisions. The enzyme preparation should be inactivated by raising the temperature to 85 °C for 15 min only after total soluble nitrogen reaches 20–28% of total nitrogen by trichloroacetic acid-soluble nitrogen index. Salt-tolerant protease activity is not a generic property; a radial diffusion casein assay at 20% NaCl is required before selecting a batch for brine-tolerant hydrolysis. If raw anchovy load contains viscera and heads above 8%, endogenous digestive enzymes shift the hydrolysis profile and the added enzyme dose must be reduced accordingly.
| Parameter | Unit | Reference method | Typical control range |
|---|---|---|---|
| Total soluble nitrogen / total nitrogen | % | TCA-soluble nitrogen index | 20–28% |
| Histamine | mg/kg | HPLC post-column derivatization | ≤ 400 |
| Sodium chloride | % (w/v) | Volhard titration | 25–30 |
| Total plate count | CFU/g | ISO 4833-1:2013 | ≤ 10⁴ |
| pH | — | Potentiometric measurement | 5.0–6.5 |
Simultaneously with fishmeal rendering, stickwater recovered from double-effect evaporators exhibits a viscosity rise that reduces heat transfer coefficient and shortens cleaning intervals. Addition of seafood hydrolase to press liquid before evaporation, at 0.05–0.15% by volume, lowers residual protein aggregates that otherwise deposit on falling-film evaporator tubes. Hydrolysis is conducted in a stirred holding tank at 50–55 °C for 30–60 min, with feed pH adjusted to 6.5–7.0 using sodium carbonate. After inactivation at 90 °C for 10 min, treated stickwater can be concentrated to 50–55% solids in a multi-effect evaporator without marked dynamic viscosity increase; inline rotational viscometry should remain below 150 mPa·s at 70 °C to ensure consistent transfer pump operation. Recovered solids are typically reintroduced into fishmeal, and the resulting product must meet the processing requirements of Regulation (EC) No 1069/2009 for Category 3 material. This application is sensitive to raw material oxidation; if peroxide value exceeds 5 meq O₂/kg oil before enzyme addition, the hydrolysis reaction does not correct the resulting lipid damage and the batch should be diverted to non-feed use. Published data for specific multi-effect evaporator configurations using mixed tropical tuna and sardine press liquid are limited, so engineering trials should measure fouling layer thickness by ultrasonic testing rather than relying on generic enzyme dosing tables.
Shrimp shell enzymatic pre-treatment before hydrochloric acid demineralization alters acid consumption and ash profile. Northern shrimp or whiteleg shrimp processing waste typically contains 25–35% protein, 20–30% calcium carbonate, and 15–25% chitin on a dry-weight basis. By treating milled shells with seafood hydrolase at 1.0–2.5% by weight of shell protein in a jacketed stirred-tank reactor held at 50–55 °C and pH 8.0–8.5 for 3–5 h, protein removal reaches 85–92% before acid treatment. Deproteinized shells are washed in a basket centrifuge to achieve rinse-water conductivity below 500 µS/cm; residual protein is then measured by the Kjeldahl nitrogen method of ISO 5983-1:2005. Subsequent demineralization at 25–30 °C with 1 M HCl requires less acid because the protease step exposes the calcium carbonate matrix and removes protein films that otherwise block acid diffusion. Chitin with ash content below 1.0% and protein content below 3.0% on a dry basis is achievable after the two-step sequence. If demineralization is performed first, residual calcium carbonate at pH > 9 inhibits protease solubility and protein removal efficiency drops below 60%. Deionized water is required for final rinsing; hard water containing more than 200 mg/L CaCO₃ equivalent deposits scale on the chitin surface and retards subsequent deacetylation.
When targeting peptides below 1 000 Da for companion animal palatability, batch temperature excursions above 55 °C reduce the concentration of volatile nitrogen compounds that participate in Maillard reactions. The feedstock is typically salmon or tuna dark meat and hydrolyzed frame tissue, homogenized to a particle size below 2 mm and diluted with process water to 20–25% dry matter. Seafood hydrolase is applied at 1.0–2.0% by weight of crude protein, and the reaction is maintained at 52–55 °C and pH 7.0–7.8 for 4–6 h. A dual-stage membrane system, composed of a 50 nm ceramic microfiltration step and a 1 kDa spiral-wound ultrafiltration stage, separates the digest into a low-molecular-weight fraction. The permeate is concentrated to 45–55 °Bx in a low-temperature vacuum evaporator operating below 65 °C to preserve free amino acids and short peptides. For final liquid palatant production, the concentrate is blended with reducing sugars and heated to 90–95 °C for 30–60 min to drive the Maillard reaction. The resulting product is applied to extruded kibble at 1–3% by weight through a vacuum coater; coating uniformity is validated by measuring surface nitrogen distribution. Safety must be established under the hazard analysis framework of 21 CFR 117 and ingredient definition requirements adopted by AAFCO. The critical process limit is the inactivation step: residual enzyme activity above 0.1 U/mL, determined by azocasein assay at pH 7.5 and 50 °C, can cause continued hydrolysis in stored palatant, producing bitter peptides and headspace amines.
Cod skin hydrolysis for marine collagen peptides requires removal of non-fibrillar proteins with dilute alkali before enzyme addition. Frozen Atlantic cod skins are thawed to 4 °C, cut to 0.5–1.0 cm² pieces, and washed with 0.1 M NaOH at a ratio of 1:10 by weight for 12 h to remove histones and proteoglycans. After neutralization to pH 7.5, the skin is dispersed in water at 10–15% solids and digested with seafood hydrolase at 50–55 °C for 3–5 h with a pH-stat setpoint of pH 8.0. Hydrolysis is terminated by raising the temperature to 85 °C for 15 min, followed by centrifugation at 8 000 × g for 20 min and filtration through a 5 kDa cross-flow membrane. The permeate is desalted by electrodialysis until ash content is below 1.5% and then spray dried. Molecular weight distribution is verified by size-exclusion chromatography with calibration peptides of 1–10 kDa; a target powder for dietary supplement applications generally contains 90–95% peptides below 3 kDa. Heavy metal content must comply with the relevant dietary supplement limits of USP <2232>, and aerobic plate count should be tested according to ISO 4833-1:2013. The process is incompatible with hard water because calcium ions above 120 mg/L bind to collagen carboxyl groups and increase turbidity in the final filtrate. If the alkali pre-wash is shortened below 8 h, residual cold-water collagenase activity from the skin can produce variable hydrolysis endpoints that are not corrected by increasing the enzyme dose.
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Seafood Hydrolase SH-2406 is a standardised microbial protease preparation formulated for controlled protein hydrolysis in finfish, crustacean, and molluscan processing streams. The product is supplied as a free-flowing tan microgranule with a declared activity of not less than 1.2 × 10⁵ HUT/g under the Food Chemicals Codex protease assay. The dry blend comprises an endoprotease that cleaves peptide bonds adjacent to hydrophobic residues and an aminopeptidase that removes N-terminal hydrophobic amino acids; the combined action lowers viscosity and reduces bitter-tasting peptide accumulation. Standardisation is achieved with sodium chloride and maltodextrin, and residual moisture is maintained at or below 8.0% to prevent compaction in bulk storage. The product is manufactured for industrial food processing use and is available in 25 kg HDPE-lined multiwall bags. Model SH-2406 is the standard grade; low-dust and heat-tolerant variants are designated SH-2406 LD and SH-2406 HT, respectively, and are interchangeable on an equal HUT/g activity basis.
Release testing is performed for each batch against the parameters listed in Table 1. Activity is standardised to a declared range rather than a single point because carrier moisture and sieve fraction influence apparent activity in the HUT assay. The certificate of analysis reports actual HUT/g, moisture, lead, and aerobic plate count.
| Parameter | Value or range | Test method or reference |
|---|---|---|
| Model designation | SH-2406 microgranule | Internal release standard |
| Declared protease activity | ≥1.2 × 10⁵ HUT/g | Food Chemicals Codex protease assay |
| pH optimum | 6.5–8.5 | 0.05 M phosphate–borate buffer |
| Temperature optimum | 50–60°C | Azocasein substrate |
| Loss on drying | ≤8.0% | USP 731 |
| Sieve fraction | ≥90% through 500 µm | ISO 3310-1 sieving |
| Lead | ≤5 mg/kg | ICP-MS |
| Aerobic plate count | ≤10,000 CFU/g | ISO 4833-1 |
| Salmonella | Absent in 25 g | ISO 6579-1 |
| Shelf life | 24 months at 4–10°C | Accelerated stability protocol |
The granulation is designed to suppress dust formation during bag transfer in a dry blending room. Low-dust grade SH-2406 LD is specified where operators handle more than 200 kg per shift; the heat-tolerant grade SH-2406 HT is intended for waste streams that require brief temperature excursions to 65°C, although the aminopeptidase component loses activity above 62°C. Dry storage at 4–10°C preserves activity; repeated temperature cycling above 25°C increases moisture migration through the bag liner and causes granule caking. The bulk density of SH-2406 is 0.55–0.65 g/cm³, and the granulation is designed for direct addition into a vortex hopper. If the powder is pneumatically conveyed over distances greater than 20 m, electrostatic dust accumulation can occur; the low-dust variant SH-2406 LD should be specified in such lines.
Cold-water byproducts such as cod frames, pollock navels, and salmon heads exhibit high connective-tissue content and seasonal lipid variation. In a 750 L jacketed hydrolysis vessel fitted with a pitched-blade turbine at 90–120 rpm, a 1:1 mixture of ground byproduct and potable water is adjusted to pH 7.0 with 2 M NaOH and heated to 55°C. Enzyme is charged at 0.3% w/w of raw protein, and degree of hydrolysis is monitored by the OPA spectrophotometric method. Hydrolysis reaches 15–20% within 4 h provided the substrate is ground through a 3 mm plate and bone fragments are removed before enzyme addition. If bone fragments exceed 8 mm, they obstruct the agitator and create dead zones that reduce apparent enzyme efficiency by up to 30%.
Lipid content above 3% in the mince shifts the mixture toward emulsification during agitation. This increases protein loss in three-phase decanting at 4,800 rpm because soluble protein partitions into the aqueous phase, but emulsified lipid droplets carry protein into the oil phase. Published data for this specific configuration is limited; production-scale records indicate protein recovery falls by 8–12% when raw peroxide value exceeds 2 meq/kg. Antioxidant-free processes should therefore limit post-grinding holding time to under 30 min at 15°C.
Batch-to-batch variation in fish raw material affects enzyme demand more than any single lot variation in SH-2406. When the raw protein is whiting, which has lower natural protease inhibitors, 0.25% enzyme may be sufficient; when the substrate is tuna dark meat with higher connective tissue and bound lipid, 0.35–0.40% enzyme is required. Routine determination of raw material amino nitrogen before hydrolysis allows dosage adjustment within 0.05% increments.
For accelerated fish sauce production, SH-2406 is dosed at 0.2–0.4% w/w of raw fish protein in an 18% NaCl brine. The high salt concentration suppresses vegetative spoilage flora while reducing enzyme activity by approximately 15–20% relative to salt-free conditions. Hydrolysis proceeds in a closed tank at 50–55°C for 6–12 h with slow agitation at 60 rpm. Dissolved salt increases density and alters the sedimentation behaviour of insoluble scales; a decanter centrifuge is therefore operated with a lower differential speed of 2 rpm to maintain clarity. After separation, the liquid is cooled to 4°C and clarified through a 50 µm stainless steel screen before evaporation. Adding enzyme above 0.5% w/w accelerates free amino acid release and increases Maillard potential during falling-film evaporation at 65°C, producing scorched off-notes.
The principal operational difference is that SH-2406 does not require cysteine activation and retains higher activity in salted fish liquors. In comparative azocasein assays at pH 7.0 and 50°C, activity retention after 30 min in 18% NaCl is 78–85% for SH-2406, whereas papain and bromelain typically retain 35–45% and 25–35%, respectively. Table 2 summarises the operating differences relevant to line conversion.
| Property | SH-2406 | Papain | Bromelain | Fungal protease |
|---|---|---|---|---|
| Cysteine or reducing agent required | No | Yes | No | No |
| Optimum temperature | 50–60°C | 65°C | 50–60°C | 45–55°C |
| Effective pH range | 6.0–8.5 | 5.5–7.5 | 4.5–7.0 | 4.0–6.5 |
| Retention in 18% NaCl, 30 min | 78–85% | 35–45% | 25–35% | 50–60% |
| Bitter peptide suppression | Aminopeptidase present | Limited | Limited | Limited |
| Heat inactivation at 85°C, 15 min | Complete | Complete | Complete | Complete |
Published data for this specific configuration is limited; the values in Table 2 are comparative lot-release data generated under controlled laboratory conditions and should be confirmed in plant-scale trials. Because bromelain cleaves with broader substrate specificity, it can generate a more heterogeneous peptide profile that is difficult to standardise during spray drying. SH-2406 includes an aminopeptidase component that reduces the abundance of terminal hydrophobic peptides associated with bitterness; this component is deliberately heat-labile and loses measurable activity above 62°C, allowing the processor to stop exopeptidase trimming before excessive free amino acid generation occurs.
The absence of an activation step reduces line downtime in continuous plants. Papain installations typically require a 15–20 min reducing pre-incubation with cysteine or sodium sulfite at 40°C; SH-2406 is slurried directly in water at 25–35°C for 10 min and metered into the hydrolysis reactor. This difference alters the piping design because the enzyme dosing line can be shorter and does not require a reducing-agent holding vessel.
Viscosity reduction in hydrolysed seafood slurries follows a non-linear response to degree of hydrolysis. Initial endoproteolysis of myofibrillar proteins produces a sharp viscosity drop within the first 60 min; subsequent exopeptidase activity contributes less to viscosity and more to flavour development. In a 200 L pilot run using mackerel mince, a decrease from 1,800 mPa·s to 250 mPa·s was observed after 90 min at 55°C and pH 7.0 with 0.3% enzyme. Bone-derived calcium released below pH 6.4 can inhibit the aminopeptidase component, so pH should be maintained above 6.8 until the target peptide profile is reached.
Degree of hydrolysis is often targeted between 10% and 20% for fish sauce intermediates and between 5% and 12% for functional protein hydrolysates. Higher degrees of hydrolysis increase free amino nitrogen and reduce average molecular weight, but also increase hygroscopicity and bitter perception unless the aminopeptidase component is controlled. SH-2406 aminopeptidase activity is specified as a secondary activity relative to the HUT titre; this ratio is checked by lot-release peptide profiling on a model herring substrate. Hydrolysate produced with SH-2406 is typically spray-dried at inlet 180–190°C and outlet 75–85°C. After drying, the powder should have a moisture content below 5.0% and a water activity below 0.30 to prevent Maillard browning. If the hydrolysate contains residual enzyme activity before drying, drying at outlet temperatures above 85°C contributes to inactivation, but a separate thermal kill step is still required to meet residual activity specifications below the detection limit.
Thermal inactivation is achieved by heating the hydrolysate to 85°C for 15 min or 90°C for 5 min; the higher-temperature condition reduces residual aminopeptidase activity below the detection limit of the HUT assay. The product is not recommended below pH 4.5 or above 80°C because irreversible activity loss occurs. Contact with oxidising sanitizers such as sodium hypochlorite above 2 ppm or peracetic acid residues above 5 ppm oxidises the active-site serine and lowers subsequent batch activity. The powder is hygroscopic; if exposure to relative humidity above 60% exceeds 4 h, the material should be re-tested for HUT/g and loss on drying before use. Avoid addition of sulfites above 100 mg/kg, as residual sulfite can reduce enzyme isoforms that contain disulphide bridges.
