Products

Alkaline Protease

    • Product Name: Alkaline Protease
    • Factroy Site: Yudu County, Ganzhou, Jiangxi, China
    • Price Inquiry: admin@ascent-chem.com
    • Manufacturer: Ascent Petrochem Holdings Co., Limited
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    Specifications
    HS Code 609860
    Product Name Alkaline Protease
    Type Serine protease
    Appearance Light yellow to brown powder or liquid
    Enzyme Activity Typically 100,000 to 500,000 U/g
    Optimal Ph pH 9.0–11.0
    Ph Stability Stable in pH 7.0–12.0
    Optimal Temperature 50–60°C
    Temperature Stability Stable up to 60°C; rapidly inactivated above 70°C
    Molecular Weight Approximately 27,000–45,000 Da
    Substrate Specificity Hydrolyzes peptide bonds adjacent to hydrophobic or aromatic amino acid residues
    Inhibitors Phenylmethylsulfonyl fluoride (PMSF), diisopropyl fluorophosphate (DFP)

    As an accredited Alkaline Protease factory, we enforce strict quality protocols—every batch undergoes rigorous testing to ensure consistent efficacy and safety standards.

    Packing & Storage
    Packing Alkaline Protease is packaged in 25 kg sealed fiber drums with polyethylene liners, protected from moisture and heat.
    Container Loading (20′ FCL) Alkaline Protease loaded in 20′ FCL as palletized drums, secured firmly, kept dry, ventilated, and protected from heat and moisture.
    Shipping Alkaline Protease: Ship as Enzyme Preparation, not restricted as dangerous goods. Pack in UN-approved HDPE drums or plastic-lined bags. Protect from moisture, heat, and strong oxidizers. Keep below 25°C in ventilated storage. Avoid contact with acids/bases. Provide MSDS, COA, and labeling for dust inhalation hazard.
    Storage Alkaline Protease should be stored in a cool, dry, air-tight container, ideally between 2–8°C to preserve enzyme activity. Avoid exposure to high temperatures, humidity, and direct sunlight. Keep the original seal intact and use desiccants if necessary. Under proper conditions, stability is maintained for extended periods.
    Shelf Life Alkaline Protease has a shelf life of approximately 12 months when stored in a cool, dry place away from sunlight.
    Application of Alkaline Protease

    In spray-dried heavy-duty laundry powder production, alkaline protease is rarely introduced into the aqueous slurry ahead of the cocurrent spray-drying tower. Slurry pH of 10.8–11.5 and inlet air temperature of 180–230 °C during cocurrent drying produce a base granule that retains less than 10% of added subtilisin activity when the enzyme is exposed to the slurry for more than 15 min at 55–65 °C. Post-tower dry dosing of an encapsulated granulate is therefore standard on lines where the enzyme is not chemically stabilized. The granulate, typically declared at 2.5 Anson units per gram (AU-A/g) for Alcalase-class subtilisin, is metered with a loss-in-weight feeder into the finished base powder at 0.3–0.8 wt% of total formulation mass after the powder has cooled below 32 °C. In a horizontal ribbon mixer operating at 20–30 rpm, mixing time is limited to 5–8 min because longer residence generates dust and mechanical shear that fractures the granulate coating. Detergency evaluation under ASTM D4265-14 in a Terg-o-tometer bath at 20 °C and 150 ppm water hardness uses EMPA 116 blood/milk/ink soiled cotton swatches to quantify reflectance difference. A formulation containing 0.5 wt% protease granulate produces a larger reflectance change on EMPA 116 than the identical base powder without enzyme, with the largest delta obtained when perborate or percarbonate is present as the activated oxygen source. In hypochlorite-containing powder formulations, the oxidant reacts with the active-site serine and destroys activity within minutes; separate bleach sachets or post-wash sanitizer dosing are required if chlorine bleach is marketed with the product. Occupational exposure to subtilisin dust is controlled to the ACGIH TLV of 60 ng/m³ inhalable fraction; enclosed transfer, local exhaust ventilation, and dust-free granulate design are mandatory in dry dosing stations. Powder residual moisture below 2.0 wt% and packaging in moisture-impermeable laminate pouches are required to prevent premature enzyme activation and autolysis during storage at 25–30 °C. Retail formulation labelling must comply with EC 648/2004 Annex VII for enzyme declaration and function.

    What Limits Protease Shelf Life in Anionic Surfactant-Rich Liquid Laundry Formulations?

    Subtilisin-class alkaline protease in heavy-duty liquid detergents is exposed to linear alkylbenzene sulfonate at 10–25 wt% and alcohol ethoxylate sulfates at 5–15 wt%. The anionic sulfate and sulfonate head groups bind to the enzyme surface and unfold the tertiary structure within hours when water activity exceeds 0.6 and formulation pH is above 9.0. To maintain at least 80% initial activity after 12 weeks at 37 °C, the liquid is formulated with a reversible protease inhibitor such as boric acid at 0.5–2.0 wt% or 4-formylphenylboronic acid at 0.05–0.2 wt%. These inhibitors cap the active-site serine during storage but dissociate on dilution in the wash liquor. Calcium chloride at 100–500 ppm Ca²⁺ is also added because the subtilisin molecule has a high-affinity calcium-binding site that stabilizes the β-sheet core; however, formulation above 500 ppm Ca²⁺ can precipitate anionic surfactants at low temperature. Cleansing performance is measured by ASTM D4265-14 using EMPA 116 swatches after a 20 min wash at 20–40 °C in water hardness of 150 ppm as CaCO₃. Without stabilizer, proteolytic activity falls below 20% of declared activity within 7 days at 37 °C; with borate-based reversible inhibition and pH held at 8.5–9.2, the same liquid retains 70–85% activity over 12 weeks. Bleach compatibility is restricted to percarbonate or perborate systems; hypochlorite bleach must be separated because the chlorinated oxidant attacks the serine hydroxyl and histidine imidazole moiety faster than substrate binding. Viscosity and phase stability of the liquid detergent also interact with the enzyme stabilizer: boric acid can increase viscosity through crosslinking with nonionic ethoxylates, and phase separation may occur below 5 °C if the calcium ion concentration is not balanced with citrate or polyacrylate dispersants.

    Limed cattlehide pelt entering bating operations after unhairing contains residual calcium hydroxide at pH 12.0–12.5, which must be reduced by ammonium sulfate deliming to 8.0–8.5 before an alkaline protease is active. In a stainless-steel drum mixer at 6–12 rpm and liquor ratio of 1.0–2.0 L/kg pelt weight, a bacterial subtilisin is dosed at 0.1–0.4 wt% of fleshed pelt weight and allowed to act for 30–60 min at 30–34 °C. The primary bating action is hydrolysis of non-collagenous skin proteins such as albumin, globulin, and proteoglycan fragments inside the fibre network. Collagen is protected by its triple-helical supercoil, but overtreatment occurs when the enzyme attacks telopeptide regions and cross-links. Process control uses a drop test in which pelt softening is correlated with air permeability and compression set, but tensile data from finished leather tested under ISO 3376 provides the objective limit. A 15 min overtreatment at 34 °C can reduce grain side firmness and produce looseness in subsequent drum dyeing; under-bating leaves the pelt too firm for uniform dye penetration. Batch-to-batch variation in pelt water content requires adjustment of the enzyme dose by conditioned pelt weight rather than raw hide weight. The drum wash following bating must remove enzyme protein and hydrolyzed skin fragments before pickling; residual protease in the pickling bath at pH below 3.0 is largely inactivated, but residual peptide fragments can interfere with chrome uptake in the tanning drum if not rinsed at 30 °C for 10 min.

    Silk Degumming Process Boundaries and Fibroin Tensile Loss Measurement

    Raw mulberry silk contains 20–30 wt% sericin around fibroin filaments. Traditional Marseille soap degumming at 98–100 °C for 90 min removes sericin to a 24–27% weight loss but consumes thermal energy and risks surface fibrillation. Protease-based degumming with a Bacillus subtilisin at 1–2 g/L bath concentration and pH 8.5–9.0 at 55–60 °C for 60 min yields 23–26% weight loss in a 1:40 goods-to-liquor ratio. The process window is constrained by fibroin damage: above 60 °C, the amorphous regions of fibroin become accessible to proteolytic attack, and tensile strength retention measured under ASTM D3822-14 drops below 85% of untreated raw silk when the bath pH exceeds 9.5 for more than 90 min. Calcium chloride at 2–5 mM improves enzyme thermal stability but excessive calcium can stiffen the fiber; a subsequent alkaline wash at 70 °C with nonionic surfactant removes enzyme protein and hydrolyzed sericin fragments. Published data for degumming loss variability across Chinese bivoltine and tropical multivoltine cocoon batches shows batch-to-batch sericin content differences of ±2 wt%, requiring dose adjustment by cocoon lot rather than fixed addition. The use of a high-shear circulating pump instead of static soaking reduces treatment time by improving enzyme liquor penetration into the fibre bundle, but excessive shearing above 500 rpm in a jet dyeing machine can cause filament entanglement and surface roughening.

    For production of spray-dried fish protein hydrolysate from Atlantic salmon frames, alkaline protease hydrolysis is run in a jacketed batch reactor with pH-stat control at pH 8.0–8.5 and 55–60 °C. The substrate is comminuted to 2–5 mm particle size and suspended in water to 8–12% protein dry matter; enzyme is added at 0.5–1.5 wt% of dry protein with a high-shear mixer to avoid localized over-hydrolysis. Degree of hydrolysis is monitored by pH-stat consumption of 1.0 M NaOH because peptide bond cleavage releases protons at alkaline pH; hydrolysis is terminated by thermal inactivation at 85 °C for 10 min when DH reaches 10–18% for palatability and 5–8% for functional emulsifying hydrolysates. The hydrolysate is clarified through a decanter centrifuge and spray dried at inlet 180–200 °C with outlet 75–85 °C. Free amino group content is determined by OPA spectrophotometric assay at 340 nm using an L-serine standard. Feed hydrolysates must comply with the FAO/WHO JECFA specifications for enzyme preparations, including microbial absence and heavy metal limits. Thermal inactivation at 85 °C for 10 min is insufficient if substrate solids exceed 15% because heat transfer in the batch reactor becomes laminar; residual activity in powder can continue hydrolyzing during storage and alter peptide profile. Spray-dried hydrolysate with residual moisture above 6% also develops Maillard reactions during storage, reducing available lysine in feed formulations. Published data for this specific configuration is limited, but production-scale observations indicate that viscosity reduction during hydrolysis is dependent on the shear regime: high-shear pre-mixing produces a more uniform particle surface for enzyme attack than paddle agitation alone.

    When Alkaline Protease Is Included in Alkaline CIP Detergents for Dairy Ultrafiltration

    Ultrafiltration membranes in whey processing are cleaned with sodium hydroxide at 0.5–1.0 wt% and surfactants at 70–80 °C; adding alkaline protease at 0.05–0.2 wt% of cleaning solution permits a lower caustic concentration and reduces protein fouling deposits on polyethersulfone spiral-wound elements. The cleaner is recirculated through a membrane skid at crossflow velocity of 2–3 m/s for 30–60 min; permeate pressure is held below 1.0 bar to avoid forcing protein fragments into the membrane pores. Clean water flux recovery is measured against the initial water flux at 25 °C and 1 bar transmembrane pressure; a recovery above 90% is required before the next production batch. The protease must be compatible with the membrane substrate: free chlorine from sanitizer cycles must be rinsed out before enzyme cleaning because residual free chlorine at 1–5 ppm oxidizes the enzyme active site. The enzyme cleaner is not suitable for cellulosic membranes because alkaline pH 10.0–10.5 can degrade the membrane backing and the protease can hydrolyze exposed cellulose-binding proteins. Ceramic membranes are preferred because of higher temperature tolerance to 80 °C. Spiral-wound elements with polysulfone backing may tolerate the cleaner but require pressure control to prevent telescoping; the pressure drop along the element should not exceed 0.5 bar during enzyme cleaning.

    Anaerobic digestion of poultry processing sludge with alkaline protease is operated at pH 8.0–8.5 and 35–40 °C in a pre-treatment holding tank upstream of the mesophilic digester. The substrate contains feather, blood, and soft tissue proteins; without pre-treatment, methane yield from the digester fluctuates with the slaughter line schedule. Protease addition at 0.05–0.15% of sludge total solids and a hydraulic retention time of 6–12 h reduces sludge viscosity and releases soluble chemical oxygen demand, but the benefit is batch-dependent because high ash content and ammonia above 3 g/L inhibit the enzyme. The pre-treated sludge is fed to a continuous stirred-tank anaerobic digester with organic loading rate of 2–3 kg VS/m³/day; enhancement of methane yield is measured by gas flow meter and biogas composition via infrared analyzer, but published data for this specific configuration is limited. The enzyme is not compatible with sludges conditioned with ferric chloride below pH 6.0. Pre-treatment tanks are equipped with top-entry agitators running at 20–30 rpm to keep feather and soft tissue particles in suspension without generating aeration; dissolved oxygen above 0.5 ppm does not directly inhibit alkaline protease but consumes reducing capacity of the sludge and may alter downstream digester redox potential.

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    Certification & Compliance
    More Introduction

    Alkaline Protease AP-200L (liquid) and AP-200G (granulate) are subtilisin-type serine endopeptidase preparations derived from a Bacillus licheniformis production strain, classified under EC 3.4.21.62 and CAS 9014-01-1. The liquid preparation is standardized to a nominal activity of 2.5 AU-A/g using the casein-hydrolysis Anson method referenced in the FCC protease monograph; the granulate is standardized to 8.0 AU-A/g for solid detergent and dry-blend applications. The enzyme hydrolyzes internal peptide bonds preferentially at the carboxylic side of hydrophobic P1 residues, including leucine, tyrosine, and phenylalanine. Downstream processing includes cell separation, ultrafiltration with a nominal molecular weight cut-off of 10 kDa, polish filtration, and stabilization with low-molecular-weight polyols. The material is a formulated enzyme preparation rather than a pure protein, and certificate-of-analysis variation reflects fermentation batch adjustment, residual salts, and stabilizers.

    The catalytic apparatus consists of the Ser-His-Asp triad, and the active-site serine is irreversibly inhibited by organophosphates such as phenylmethanesulfonyl fluoride. Because the enzyme is a serine protease, EDTA and most chelators do not directly inhibit activity over short contact times, but strong oxidants including hydrogen peroxide, hypochlorite, and peracetic acid inactivate the preparation through methionine oxidation. The molecule contains a calcium binding site that stabilizes the tertiary structure; calcium concentrations above 2 mM improve thermal stability, while prolonged exposure to sodium tripolyphosphate or EDTA can strip calcium and reduce heat tolerance. This calcium dependence is particularly relevant in detergent formulations, where zeolite and carbonate builders may compete for hardness ions but do not fully replace the stabilizing calcium requirement in liquid matrices.

    Specification Limits and Analytical Release Criteria

    ParameterRelease LimitAnalytical Reference
    AppearanceAP-200L: light amber liquid; AP-200G: off-white granuleVisual inspection
    Declared activityAP-200L: 2.5 AU-A/g ±5%; AP-200G: 8.0 AU-A/g ±5%FCC protease monograph, Anson method
    pH as is7.8–9.2pH meter, 25°C
    Density at 20°C1.05–1.10 g/mLOscillating U-tube
    Viscosity at 25°C≤250 mPa·sRotational viscometer
    Particle size, AP-200G150–425 µm; fines below 150 µm <10%Laser diffraction or sieving
    Lead≤5 mg/kgEP 2.4.8
    Arsenic≤3 mg/kgEP 2.4.8
    Total aerobic microbial count≤5,000 CFU/gISO 4833-1:2013
    Yeast and mould≤100 CFU/gISO 21527-2:2008
    SalmonellaAbsent in 25 gISO 6579-1:2017
    Storage stability12 months at 5–15°C, sealedAccelerated stability, retained activity

    Activity release testing uses casein substrate at 40°C and pH 10.5, with released tyrosine quantified spectrophotometrically. Batch-to-batch variation is controlled by post-fermentation adjustment, and certificates of analysis report activity, pH, density, and microbial limits. Packaging for AP-200L is high-density polyethylene jerrycans of 25 kg, drums of 200 kg, or intermediate bulk containers of 1,000 kg; AP-200G is supplied in 20 kg polyethylene-lined multiwall paper bags. The liquid product should not be frozen below 0°C, and the granulate should be stored below 25°C and below 60% relative humidity to avoid particle agglomeration and activity loss.

    Because the product is standardized on protein substrate, direct activity comparisons with other preparations should not be made solely on gross weight. Different suppliers may express activity in Anson units, Kilo Novo Protease Units, or modified hemoglobin assays, and conversion factors are method-dependent. The AP-200L specification of 2.5 AU-A/g is therefore meaningful only against the defined casein substrate, pH, and temperature conditions. Users replacing a neutral or acid protease should compare activity on the target substrate at process pH rather than relying on supplier unit labels.

    Post-tower addition of the dust-free granulate in heavy-duty laundry powder is specified at 0.3–0.8 wt% of the final formulation, depending on the builder system and wash temperature. The granulate is blended after the spray-drying tower to avoid thermal deactivation in the hot slurry and to limit contact with alkaline base particles above 40°C. On a 5 t/h continuous mixer, segregation is minimized when the granulate particle size is maintained between 150 µm and 425 µm and bulk density is kept within 0.7–0.9 g/cm³. High-shear mixing with zeolite and sodium carbonate is acceptable, but prolonged mixing above 50°C or contact with uncoated sodium percarbonate may reduce recovered activity by 15–25% because of oxidative damage to methionine residues. Compatibility with sodium percarbonate therefore requires coated percarbonate grades or separation of enzyme and bleach granules. Trace hypochlorite below 5 ppm can oxidize the active-site methionine and produce rapid activity loss, so the product cannot be used in chlorine-containing pre-spotters or sanitizing washes unless the oxidant is first neutralized.

    Liquid detergent incorporation is performed post-build after neutralization and cooling below 35°C. In a 10,000 L batch mixer, localized pH excursions above 11.0 or anionic surfactant concentrations above 20% can destabilize the protease during storage. Homogenization should remain below 300 rpm after enzyme addition, because high shear increases air-liquid interface denaturation. Cold-water dissolution of granular products at 20°C may require additional time; dissolution half-time is formulation-specific and should be tested by a detergent dissolution method before factory release.

    What Limits Substrate Conversion in High-DH Hydrolysates?

    In stirred-tank protein hydrolysis, the enzyme is dosed at 0.5–2.0% of substrate protein by weight. Typical substrates include soy protein isolate, wheat gluten, fish protein, and whey protein concentrate. The process is controlled at 55–60°C and pH 8.0–9.5 using a pH-stat system with 1.0 M sodium hydroxide; alkali consumption is used to calculate degree of hydrolysis (DH) because peptide bond cleavage releases protons. High-DH operation above 20% tends to generate short-chain peptides and free amino acids, but rate declines nonlinearly due to substrate depletion and product inhibition. Published kinetic data for Bacillus licheniformis protease on soy protein show a decline in apparent first-order rate as DH moves from 5% to 15%, but exact parameters are substrate- and pretreatment-specific.

    Production-scale vessels should be jacketed and fitted with low-shear axial impellers. Vigorous agitation does not improve conversion and can increase foaming and interfacial denaturation. Batch times of 2–6 h are common, after which the enzyme is inactivated by heating to 85–90°C for 10–15 min. Incomplete inactivation produces residual activity that can continue hydrolysis during downstream evaporation or spray drying, shifting peptide profile and generating off-spec material. Foaming is controlled by mechanical defoaming or steam injection rather than by increasing impeller speed. The pH-stat method assumes that released protons correspond directly to peptide bond cleavage; carbonate buffers should be avoided because carbon dioxide evolution distorts alkali consumption. Preconditioning of globular proteins improves initial hydrolysis rate, but the magnitude is substrate-specific and should be established in pilot trials.

    Sanitization of enzyme dosing lines in food hydrolysate plants should avoid chlorine-based oxidants. If line sanitization with hypochlorite is required, the alkaline protease must be displaced with water and the line rinsed to an oxidant concentration below 0.5 ppm before enzyme reintroduction. Stainless steel equipment does not inhibit the enzyme, but copper and iron ions may catalyze oxidative damage under alkaline conditions. The product is compatible with most stainless steel grades, including 316L, but prolonged contact with corroded carbon steel may introduce metal ions that accelerate destabilization.

    Alkaline Protease Exhibits a Broader Alkaline pH Window Than Neutral and Acid Proteases

    FeatureAlkaline ProteaseNeutral ProteaseAcid Protease
    Catalytic classSerine endopeptidase, EC 3.4.21.62Metalloprotease, EC 3.4.24.28Aspartic protease, EC 3.4.23.1
    pH optimum8.0–10.56.0–7.52.5–4.5
    Temperature optimum55–65°C40–55°C40–55°C
    InhibitorPhenylmethanesulfonyl fluoride; diisopropyl fluorophosphateEDTA; 1,10-phenanthrolinePepstatin
    Primary industrial useDetergent, high-pH protein hydrolysis, leather batingNeutral pH food protein modificationSour whey, soy sauce, digestive aid formulations

    The operational distinction is most evident in high-pH processes. Neutral metalloprotease loses activity rapidly above pH 8.5, whereas alkaline protease maintains activity up to pH 10.5. Acid protease requires pH adjustment into the range 2.5–4.5, which increases salt formation during neutralization and may acid-hydrolyze starch if the substrate contains starch. Alkaline protease also differs in cleavage specificity: subtilisin accepts hydrophobic P1 residues, producing peptide mixtures with less bitter character in many fish and soy hydrolysates compared with neutral protease, although bitterness is not eliminated and may require exopeptidase debittering if DH exceeds 30%. In detergent applications, alkaline protease is preferred over neutral protease because wash pH in heavy-duty powders typically exceeds 9.0, where neutral metalloprotease is unstable. Acid protease has no meaningful detergent cleaning function at high pH but is used in sour whey processing and digestive aid formulations.

    The differences between alkaline, neutral, and acid proteases also extend to operational hazards and cleaning. Alkaline protease is active at pH values that minimize microbial growth in hydrolysis vessels; neutral and acid processes may require more rigorous microbial control. Acid protease requires pH adjustment with hydrochloric or citric acid and can generate chloride stress on stainless steel; alkaline protease at pH 9.0 is less corrosive to 316L stainless steel than acid conditions but can attack aluminum and zinc. Equipment selection therefore depends on process pH, not only on enzyme compatibility.

    In leather bating, the liquid alkaline protease is applied after ammonium sulfate deliming. Dosage is commonly 0.2–0.5% of limed pelt weight, with float pH adjusted to 8.0–8.5 and temperature maintained at 32–37°C. The enzyme degrades non-collagenous interfibrillar proteins, increasing grain permeability and reducing hide stiffness. Over-bating occurs when dosage exceeds 1.0% or contact time exceeds 90 min, producing empty, loose flanks and reduced tear strength. Production drums with variable speed control are preferred; rotation at 4–6 rpm for 30–60 min is typical. Alkaline protease is an alternative to pancreatic trypsin in bating, with better microbial control and lower odor, but it does not fully reproduce pancreatic bating effects in all leather types. Published comparative data for specific leather lines is limited, and pilot-scale trials are required to set drum time and dosage.

    When Alkaline Protease Replaces Neutral Protease in Soy Hydrolysates

    When alkaline protease replaces neutral metalloprotease in soy protein isolate hydrolysis, the pH is shifted from neutral to 8.5–9.0, and sodium hydroxide consumption increases roughly 1.5–2.0-fold for the same DH because of the higher operating pH. The resulting hydrolysate has lower viscosity at 15% solids and improved solubility at pH 4.0, which is relevant for beverage and feed applications. However, the higher pH promotes racemization of free amino acids if dwell time exceeds 4 h at 60°C, and lysinoalanine formation may be elevated in heat-processed products. The choice of alkaline protease therefore requires a final pH neutralization step and careful control of alkaline hold time. In membrane separation of soy hydrolysates, residual enzyme activity can hydrolyze membrane proteins and foul ultrafiltration elements; the preparation should be inactivated by heating to 85°C for 10 min before filtration.

    For food processing, the preparation is assessed according to the JECFA General Specifications for Enzyme Preparations Used in Food Processing and the FCC enzyme monograph. Detergent and leather applications do not require food-grade certification but must conform to regional industrial chemical inventories such as REACH. The product contains no intentionally added antimicrobial preservatives, and the granular form is not an explosive dust under standard classification; however, enzyme dust is a respiratory sensitizer, and dust control measures are required at blending stations.

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